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ecce/ proteins of the inner membrane/ enzymes
Oxidoreductases
-acting on the CH-OH group of donors
-acting on the CH-NH2 group of donors
-acting on NADH or NADPH with NAD+ or NADP+ as acceptor
-acting on NADH or NADPH with quinone or similar compound as acceptor
-acting on nitrogenous compounds
-acting on diphenols and related compounds with oxygen as acceptor

Transferases
Acyltransferases
Glycosyltransferases:
---Hexosyltransferases
---Pentosyltransferases
---transferring other glycosyl and succinylgroups
Transferases transferring alkyl or aryl groups, other than methyl groups
Transferases transferring phosphorous-containing groups
---Phosphotransferases with an alcohol group as acceptor
---Phosphotransferases with a nitrogenous group as acceptor (sensor proteins of two-component regulatory systems)
---Nucleotidyltransferases
---Transferases for other substituted phosphate groups

Hydrolases
-acting on ester bonds
---Carboxylic monoester hydrolases
---Phosphoric monoester hydrolases
-acting on peptide bonds (proteases)
---Serine endopeptidases
---Aspartic endopeptidases
---Endopeptidase of unknown catalytic mechanism
-acting on acid anhydrides in phosphorous-containing anhydrides

Ligases
-forming carbon-nitrogen bonds
---Acid amino-acid ligases (peptide synthases)

Disulfide bond formation


Oxidoreductases

Ethanolamine utilization protein EutG (eutG )
functionmay act on the acetaldehyde produced from the degradation of ethanolamine
interaction 
cofactors 
regulation 
topologytransmembrane domains: 0 (potential), SP has 2

TMHMM gives 0
SP gives 109-129 261-280

mqnelqtalf qafdtlnlqr vktfsvppvt lcgpgsvssc gqqaqtrglk
hlfvmadsfl hqagmtaglt rsltvkgiam tlwpcpvgep citdvcaava
qlresgcdgv iafgggsvld aakavtllvt npdstlaems etsvlqprlp
liaipttagt gsettnvtvi idavsgrkqv lahaslmpdv aildaalteg 200
vpshvtamtg idalthaiea ysalnatpft dslaigaiam igkslpkavg
yghdlaares mllascmagm afssaglglc hamahqpgaa lhiphglana
mllptvmefn rmvcrerfsq igralrtkks ddrdainavs eliaevgigk
rlgdvgatsa hygawaqaal ediclrsnpr tasleqivgl yaaaq

MW41031 Da; 395 aa


NiFe reductase HyaA (hyaA )
function2 reduced ferredoxin + 2 H+ = 2 oxidized ferredoxin + H2
interaction 
cofactors 
regulation 
topologytransmembrane domains: 2, SP has 0

TMHMM gives 20-39 326-348

mnneetfyqa mrrqgvtrrs FLKYCSLAAT SLGLGAGMAp kiawalenkp
ripvvwihgl ectcctesfi rsahplakdv ilslisldyd dtlmaaagtq
aeevfediit qyngkyilav egnpplgeqg mfcissgrpf ieklkraaag
asaiiawgtc aswgcvqaar pnptqatpid kvitdkpiik vpgcppipdv 200
msaiitymvt fdrlpdvdrm grplmfygqr ihdkcyrrah fdagefvqsw
dddaarkgyc lykmgckgpt tynacsstrw ndgvsfpiqs ghgclgcaen
gfwdrgsfys rvvdipqmgt hstadTVGLT ALGVVAAAVG VHAVASAVdq
rrrhnqqpte tehqpgnedk qa

MW40681 Da; 372 aa


Formate hydrogenlyase subunit 3 (hycC )
functionnon energy conserving pathway, hydrogen and carbodioxide are released
interaction 
cofactors 
regulation 
topologytransmembrane domains: 14 (potential), SP has 12

TMHMM gives 5-27 47-69 76-98 113-134 155-177 197-219 226-248 258-280 287-309 324-346 367-389 415-437 457-479 499-521
SP gives 10-26 44-67 76-93 116-140 153-173 197-218 229-251 258-280 296-312 416-440 453-476 502-521

msaiSLINSG VAWFVAAAVL AFLFSFQkal sgwiagigga vgslytAAAG
FTVLTGAVGV SGALSLVSYd vqispLNAIW LITLGLCGLF VSLYNIDWhr
haqvkcnglq inMLMAAAVC AVIASNLGMF VVMAeimalc avfltsnske
gklwFALGRL GTLLLAIACW LLWQRYGtld lrlldmrmqq lplgsdIWLL 200
GVIGFGLLAG IIPLHGWVPq ahanaSAPAA ALFSTVVMKI GLLGILTLsl
lggnaplWWG IALLVLGMIT AFVGGLYALV ehniqrLLAY HTLENIGIIL
LGLGAGVTGi aleqpalial glvGGLYHLL NHSLFKSVLF LGAGSVwfrt
ghrdieklgg igkkmpVISI AMLVGLMAMA ALPPLNGFAg ewviyqsffk 400
lsnsgafvar llgpLLAVGL AITGALAVMC MAKVYGVtfl gaprtkeaen
atcaplLMSV SVVALAICCV IGGVAAPWLl pmlsaavplp lepanttvSQ
PMITLLLIAC PLLPFIIMAI Ckgdrlpsrs rgaawvcgyd heksmvitah
gfampvkqaf apvlklrkwl npvslvpgwq cegsallfrr malvelavlv 600
viivsrga

MW6407 Da; 608 aa


Formate hydrogenlyase subunit 4 (hycD )
functionnon energy conserving pathway, hydrogen and carbodioxide are released
interaction 
cofactors 
regulation 
topologytransmembrane domains: 8 (potential)

TMHMM gives 7-29 69-91 98-116 131-153 166-188 218-240 252-274 289-306
SP gives 3-23 68-88 94-114 132-152 168-188 222-242 254-274 285-305

msvlypLIQA LVLFAVAPLL SGITRVARAr lhnrrgpgvl qeyrdiikll
grqsvgpdas gwvfrltpYV MVGVMLTIAT ALPVVTVGSP LpqlgdlITL
LYLFAIARFF FAISGLdtgs pftaigasre AMLGVLVEPM LLLGLWVAAQ
VAGstnisni tdtvyHWPLS QSIPLVLALC ACAFATFIem gklpfdlaea 200
eqelqegpls eysgsgfGVM KWGISLKQLV VLQMFVGVFI pwgqmetfta
gGLLLALVIA IVKLVVGVLV IALFensmar lrlditprIT WAGFGFAFLA
FVSLLAa

MW33029 Da; 307 aa


Hydrogenase-4 component B (hyfB )
function 
interaction 
cofactors 
regulation 
topologytransmembrane domains: 16 (potential)

TMHMM gives 5-27 40-62 82-101 108-130 134-153 165-187 202-224 237-259 274-296 303-325 340-362 383-405 431-453 474-496 529-551 654-671
SP gives 6-26 31-51 80-100 120-140 165-185 200-220 243-263 273-293 312-332 343-363 385-405 428-448 475-495 505-525 532-552 652-672

mdalQLLTWS LILYLFASLA SLFLLGLdrl aiklsgitsL VGGVIGIISG
ITQLHAGVTL VArfappfef adltlrmdsl sAFMVLVISL LVVVCSLYSL
TymreyeGKG AAAMGFFMNI FIASMVALLV mdnAFWFIVL FEMMSLSSWF
LVIarqdkts inagMLYFFI AHAGSVLIMI AFLLMGResg sldfasfrtl 200
sLSPGLASAV FLLAFFGFGA KAGMmplhsw lprahpAAPS HASALMSGVM
VKIGIFGILk vamdllaqtg lplWWGILVM AIGAISALLG VLYALAeqdi
krLLAWSTVE NVGIILLAVG VAMVGlslhd plltvvgllG ALFHLLNHAL
FKGLLFLGAG AIisrlhthd mekmgalakr mpWTAAACLI GCLAISAIPP 400
LNGFIsewyt wqslfslsrv eavalqlagp IAMVMLAVTG GLAVMCFVKM
YGItfcgapr sthaeeaqev pntMIVAMLL LAALCVLIAL SASWLApkim
hiahaftntp patvasgial vpgtfhtqVT PSLLLLLLLA MPLLPGLYWL
Wcrsrraafr rtgdawacgy gwenamapsg ngvmqplrvv fsalfrlrqq 600
ldptlrlnkg lahvtaraqs tepfwdervi rpivsatqrl akeiqhlqsg
dfrLYCLYVV AALVVLLIAI Av

MW72582 Da; 672 aa


Hydrogenase-4 component C (hyfC )
function 
interaction 
cofactors 
regulation 
topologytransmembrane domains: 8 (potential)

TMHMM gives 10-32 74-96 106-128 141-163 173-195 229-251 255-277 290-312
SP gives 11-31 74-94 99-119 141-161 182-202 229-249 257-277 290-310

mrqtlcdgyL VIFALAQAVI LLMLTPLFTG ISrqirarmh srrgpgiwqd
yrdihklfkr qevaptssgl mfrLMPWVLI SSMLVLAMAL PLFITVspfa
gggdlITLIY LLALFRFFFA LSGLDTGSpf agvgasrelt LGILVEPMLI
LSLLVLALIA GSThiemisn tlAMGWNSPL TTVLALLACG FACFIemgki 200
pfdvaeaeqe lqegplteys gaglalakWG LGLKQVVMAS LFVALFLPFG
RaqeLSLACL LTSLVVTLLK VLLIFVLasi aentlargrF LLIHHVTWLG
FSLAALAWVF WLtgl

MW34359 Da; 315 aa


Hydrogenase-4 component D (hyfD)
function 
interaction 
cofactors 
regulation 
topologytransmembrane domains: 12 (potential), SP has 15

TMHMM gives 4-23 30-52 72-94 115-134 139-156 169-191 269-291 298-320 330-352 364-386 409-431 458-477
SP gives 3-23 30-50 55-75 80-100 117-137 168-188 208-228 238-258 270-290 300-320 330-350 369-389 390-410 411-431 458-478

menLALTTLL LPFIGALVVS FSPqrraaeW GVLFAALTTL CMLSLISAFY
QAdkvavtlt lvnvgdvalf gLVIDRVSTL ILFVVVFLGL LVTIystgyl
tdknrehphn gtnrYYAFLL VFIGAMAGLV LSSTllgqLL FFEITGGCSW
ALISYYqsdk aqrsalkaLL ITHIGSLGLY LAAATLFLQT Gtfalsamse 200
lhgdarylvy ggilfaawgk saqlpmqawl pdameaptpi saylhaasmv
kvgvyifara iidggnipHV IGGVGMVMAL VTILYGFLMY LpqqdmkRLL
AWSTITQLGW MFFGLSLSIF gsrlalegsI AYIVNHAFAK SLFFLVAGAL
SYscgtrllp rlrGVLHTLP LPGVGFCVAA LAITGVppfn gffskfplfa 400
agfalsveYW ILLPAMILLM IESVASFAWF Irwfgrvvpg kpseavadaa
plpgsmrLVL IVLIVMSLIS SVIAATWlq

MW51754 Da; 479 aa


Hydrogenase-4 component E (hyfE )
function 
interaction 
cofactors 
regulation 
topologytransmembrane domains: 7 (potential)

TMHMM gives 5-24 31-53 57-79 91-113 128-145 152-171 176-195
SP gives 4-24 39-59 60-80 93-113 123-143 151-171 176-196

mtgsMIVNNL AGLMMLTSLF VISVksyrls CGFYACQSLV LVSIFATLSC
LFAaeqLLIW SASAFITKVL LVPLIMTYAa rnipqnipek ALFGPAMMAL
LAALIVLLCA FVVqpvklpm atglkpaLAV ALGHFLLGLL CIVSQrnilr
qIFGYCLMEN GSHLVLALLA WrapeLVEIG IATDAIFAVI VMVLLarkiw 200
rthgtldvnn ltalkg

MW23361 Da; 216 aa


Hydrogenase-4 component F (hyfF )
function 
interaction 
cofactors 
regulation 
topologytransmembrane domains: 12 (potential)

TMHMM gives 5-24 37-55 75-97 118-140 168-190 216-238 253-275 288-307 322-344 372-394 414-436 457-479
SP gives 4-24 34-54 75-95 122-142 168-188 217-237 256-276 286-306 322-342 384-404 417-437 457-477

msysVMFALL LLTPLLFSLL CFACrkrrls atrtvtVLHS LGITLLLILA
LWVVQtaada geifaaglwl hidgLGGLFL AILGVIGFLT GIYSIGYmrh
evahgelspv tlcdyygFFH LFLFTMLLVV TSNNLIVMWA aieattlssa
flvgiygqrs sleaawkYII ICTVGVAFGL FGTVLVYANA asvmpqaema 200
ifwsevlkqs slldpTLMLL AFVFLLIGFG TKTGLFPMha wlpdahseap
spVSALLSAV LLNCALLVLI RYYIIicqai gsdfpnrLLL IFGMLSVAVA
AFFILVQrdi krllayssve nMGLVAVELG IGGPLGIFAA LLHIlnhsla
ktllfcgsgn vllkygtrdl nVVCGMLKIM PFTAVLFGGG ALALagmppf 400
niflsefmti tagLARNHLL IIVLLLLLLT LVLAGLvrma arvlmakppq
avnrgdLGWL TTSPMVILLV MMLAMGTHIp qpvirilaga stivlsgthd
lpaqrstwhd flpsgtasvs ekhser

MW56767 Da; 526 aa


Oxidoreductases Acting on the CH-OH Group of Donors

Glucose dehydrogenase (gcd )
functionenergy conserving rather than sugar metabolism
interaction 
cofactorsPQQ (2,7,9-tricarboxy-1H-pyrrolo-(2,3f)-quinoline quinone)
regulation 
topologytransmembrane domains: 5 (potential)

TMHMM gives 13-35 40-57 64-81 96-114 121-140
SP gives 11-37 41-58 63-81 96-110 119-141

mainntgsrr LLVTLTALFA ALCGLYLLIG GGWLVaiggS WYYPIAGLVM
LGVAWMLwrs kraALWLYAA LLLGTMIWGV Wevgfdfwal tprsdILVFF
GIWLILPFVW RRLVIpasga VAALVVALLI SGGILTWAGF ndpqeingtl
sadatpaeai spvadqdwpa ygrnqegqrf splkqinadn vhnlkeawvf 200
rtgdvkqpnd pgeitnevtp ikvgdtlylc tahqrlfald aasgkekwhy
dpelktnesf qhvtcrgvsy heakaetasp evmadcprri ilpvndgrli
ainaengklc etfankgvln lqsnmpdtkp glyeptsppi itdktivmag
svtdnfstre tsgvirgfdv ntgellwafd pgakdpnaip sdehtftfns 400
pnswapaayd akldlvylpm gvttpdiwgg nrtpeqerya ssilalnatt
gklawsyqtv hhdlwdmdlp aqptladitv ngqkvpviya paktgnifvl
drrngelvvp apekpvpqga akgdyvtptq pfselsfrpt kdlsgadmwg
atmfdqlvcr vmfhqmryeg iftppseqgt lvfpgnlgmf ewggisvdpn 600
revaianpma lpfvsklipr gpgnpmeqpk dakgtgtesg iqpqygvpyg
vtlnpflspf glpckqpawg yisaldlktn evvwkkrigt pqdsmpfpmp
vpvpfnmgmp mlggpistag nvlfiaatad nylraynmsn geklwqgrlp
aggqatpmty evngkqyvvi sagghgsfgt kmgdyivaya lpddvk


MW86747 Da; 796 aa


Oxidoreductases Acting on the CH-NH2 Group of Donors

D-amino acid dehydrogenase small subunit (dadA )
functionoxidative deamination of d-amino acids, alanine metabolism
interaction 
cofactorsFAD flavoprotein and nonheme iron
regulationinduction: by alanine
topologyheterodimer of a small and a large subunit
inner membrane-bound
MW47607 Da; 432 aa


Oxidoreductases Acting on NADH or NADPH with NAD+ or NADP+ as Acceptor

NAD(P) transhydrogenase subunit alpha (pntA )
functiontranshydrogenation between NAD(P) and NAD(P)H is coupled to respiration and ATP hydrolysis, functions as a proton pump across the membrane
heterodimer of an alpha and a beta chain
interaction 
cofactors 
regulation 
topologytransmembrane domains: 5 (potential), SP has 4

TMHMM gives 169-191 403-420 424-446 453-472 477-499
SP gives 402-422 423-443 453-473 477-497

mrigiprerl tnetrvaatp ktveqllklg ftvavesgag qlasfddkaf
vqagaeiveg nsvwqseiil kvnaplddei allnpgttlv sfiwpaqnpe
lmqklaernv tvmamdsvpr israqsldal ssmaniagyr aiveaahefg
rfftgqitaa gkvppakVMV IGAGVAGLAA IGAANSLGAI Vrafdtrpev 200
keqvqsmgae fleldfkeea gsgdgyakvm sdafikaeme lfaaqakevd
iivttalipg kpapklitre mvdsmkagsv ivdlaaqngg nceytvpgei
fttengvkvi gytdlpgrlp tqssqlygtn lvnllkllck ekdgnitvdf
ddvvirgvtv irageitwpa ppiqvsaqpq aaqkaapevk teekctcspw 400
rkYALMALAI ILFGWMASVA pkeFLGHFTV FALACVVGYY VVWNVShalh
tpLMSVTNAI SGIIVVGALL QIgqggWVSF LSFIAVLIAS INIFGGFTVt
qrmlkmfrkn

MW54623 Da; 510 aa


Transhydrogenase subunit beta (pntB )
functiontranshydrogenation between NAD(P) and NAD(P)H is coupled to respiration and ATP hydrolysis, functions as a proton pump across the membrane
heterodimer of an alpha and a beta chain
interaction 
cofactors 
regulation 
topologytransmembrane domains: 9 (potential)

TMHMM gives 5-24 33-52 57-75 88-107 122-144 164-181 185-207 214-236 240-259
SP gives 4-24 46-66 83-103 116-136 165-185 189-209 216-236 240-260 309-329

msggLVTAAY IVAAILFIFS LAGLskhets rqGNNFGIAG MAIALIATIF
GPdtgnVGWI LLAMVIGGAI GIRLAkkvem tempelvAIL HSFVGLAAVL
VGFNSYLhhd agmapilvni hLTEVFLGIF IGAVTFTGSV VAFGklcgki
sskplmlpnr hkmNLAALVV SFLLLIVFVR TdsvGLQVLA LLIMTAIALV 200
FGWHLVAsig gadMPVVVSM LNSYSGWAAA AAGFMLsndL LIVTGALVGS
SGAILSYIMc kamnrsfisv iaggfgtdgs stgddqevge hreitaeeta
ellknshsvi itpgygmava qaqypvaeit eklrarginv rfgihpvagr
lpghmnvlla eakvpydivl emdeinddfa dtdtvlviga ndtvnpaaqd 400
dpkspiagmp vlevwkaqnv ivfkrsmntg yagvqnplff kenthmlfgd
akasvdailk al

MW48723 Da; 462 aa


Oxidoreductases acting on NADH or NADPH with Quinone or Similar Compound as Acceptor


 Oxidoreductases Acting on Nitrogenous Compounds

Respiratory nitrate reductase 1 gamma chain (narI )
functionallows to use nitrate as electron acceptor during anaerobic growth; transferres electrons from quinones to beta subunit
tetramer of an alpha, a beta and two gamma chains (catalytic subunits: alpha and beta chains, gamma chains are involved in membrane binding)
interaction 
cofactors 
regulationinduction: nitrate
topology>transmembrane domains: 5 (potential)

TMHMM gives 4-26 47-69 89-108 127-149 184-206
SP gives 6-26 54-74 89-109 127-147 180-200

mqfLNMFFFD IYPYIAGAVF LIGSWLrydy gqytwraass qmldrkGMNL
ASNLFHIGIL GIFVGHFFGm ltphwmyeaw lpievkqkMA MFAGGASGVL
CLIGGVLLlk rrlfsprvra tttgadILIL SLLVIQCALG LLTIPFSAQh
mdgsemmklv gwaqsvvtfh ggasqhldgv afiFRLHLVL GMTLFLLFPF 200
SRLIHIwsvp veyltrkyql vrarh

MW25497 Da; 225 aa


Respiratory nitrate reductase 2 gamma chain (narV )
functioncan substitute for the Nra enzyme and allows to use nitrate as electron acceptor during anaerobic growth transferres electrons from quinones to beta subunit
tetramer of an alpha a beta and two gamma chains (catalytic subunits: alpha and beta chains, gamma chains are involved in membrane binding)
interaction 
cofactors 
regulation 
topologytransmembrane domains: 5 (potential)

TMHMM gives 10-29 50-69 89-111 128-150 185-207
SP gives 7-27 49-69 91-111 128-148 181-201

miqylnvffY DIYPYICATV FFLGSWLRYd ygqytwrass sqmldkrgmV
IWSNLFHIGI LGIFFGHLFg mltphwmyaw flpvaakqLM AMVLGGICGV
LTLIGGAGLL Wrrltnqrvr atsttpdIII MSILLIQCLL GLSTIPFSAQ
ypdgsemmkl vgwaqsivtf rggssemlng vafvFRLHLV LGMTIFLLFP 200
FTRLVHVwsa pfeyftrryq ivrsrr

MW26018 Da; 226 aa


Oxidoreductases Acting on Diphenols and Related Compounds with Oxygen as Acceptor


Transferases

3-Deoxy-D-manno-octulosonic-acid transferase (kdtA )
functionlipopolysaccharide core biosynthesis
interaction 
cofactors 
regulation 
topologytransmembrane domains: 1 (potential), TMHMM has 0 (if TM, N-term is out)

TMHMM gives 0
SP gives 1-20

mleLLYTALL YLIQPLIWIR LWVrgrkapa yrkrwgeryg fyrhplkpgg
imlhsvsvge tlaaiplvra lrhrypdlpi tvttmtptgs ervqsafgkd
vqhvylpydl pdalnrflnk vdpklvlime telwpnliaa lhkrkiplvi
anarlsarsa agyaklgkfv rrllrritli aaqneedgar fvalgaknnq 200
vtvtgslkfd isvtpqlaak avtlrrqwap hrpvwiatst hegeesvvia
ahqallqqfp nlllilvprh perfpdainl vrqaglsyit rssgevpsts
tqvvvgdtmg elmllygiad lafvggslve rgghnpleaa ahaipvlmgp
htfnfkdica rleqasglit vtdattlake vsslltdady rsfygrhave 400
vlyqnqgalq rllqllepyl ppkth

MW47291 Da; 425 aa


Transferases Transferring One-Carbon Groups

Acyltransferases

2-Acylglycerophosphoethanolamine acyltransferase (aas )
functionlysophospholipid acylation, regeneration of phosphatidylethanolamin
interaction 
cofactorsATP, Mg2+
regulation 
topologytransmembrane domains: 0 (potential), SP has 3

TMHMM gives 0
SP gives 37-57 258-278 409-429

mlfsffrnlc rvlyrvrvtg dtqalkgerv litpnhvsfi dgillglflp
vrpvfavyts isqqwymrwl ksfidfvpld ptqpmaikhl vrlveqgrpv
vifpegritt tgslmkiydg agfvaaksga tvipvriega elthfsrlkg
lvkrrlfpqi tlhilpptqv ampdaprard rrkiagemlh qimmearmav 200
rpretlyesl lsamyrfgag kkcvedvnft pdsyrklltk tlfvgrilek
ysvegerigl mlpnagisaa vifgaiarrr mpammnytag vkgltsaita
aeiktiftsr qfldkgklwh lpeqltqvrw vyledlkadv ttadkvwifa
hllmprlaqv kqqpeeeali lftsgseghp kgvvhshksi lanveqikti 400
adfttndrfm salplfhsfg ltvglftpll tgaevflyps plhyrivpel
vydrsctvlf gtstflghya rfanpydfyr lryvvagaek lqestkqlwq
dkfglrileg ygvtecapvv sinvpmaakp gtvgrilpgm darllsvpgi
eeggrlqlkg pnimngylrv ekpgvlevpt aenvrgemer gwydtgdivr 600
fdeqgfvqiq grakrfakia gemvslemve qlalgvspdk vhataiksda
skgealvlft tdneltrdkl qqyarehgvp elavprdiry lkqmpllgsg
kpdfvtlksw vdeaeqhde

MW80700 Da; 719 aa


Apolipoprotein N-acyltransferase (cutE )
functionlipoprotein biosynthesis
interaction 
cofactors 
regulation 
topologytransmembrane domains: 6 (potential)

TMHMM gives 12-34 54-76 89-111 166-188 195-213 489-507
SP gives 12-28 57-77 91-111 168-188 194-214 487-507

mafaslierq rirLLLALLF GACGTLAFSP YDVWpaaiis lmglqaltfn
rrpLQSAAIG FCWGFGLFGS GINWVYVsia tfggmpgpVN IFLVVLLAAY
LSLYTGLFAG VLsrlwpktt wlrvaiaapa lwqvteflrg wvltgfpwlq
fgysqidgpl kglapIMGVE AINFLLMMVS GLLALALVkr nwrpLVVAVV 200
LFALPFPLRY IQWftpqpek tiqvsmvqgd ipqslkwdeg qllntlkiyy
nataplmgks sliiwpesai tdleinqqpf lkaldgelrd kgsslvtgiv
darlnkqnry dtyntiitlg kgapysyesa drynknhlvp fgefvplesi
lrplapffdl pmssfsrgpy iqpplsangi eltaaicyei ilgeqvrdnf 400
rpdtdyllti sndawfgksi gpwqhfqmar mralelarpl lrstnngita
vigpqgeiqa mipqftrevl ttnvtpttgl tpyartgnWP LWVLTALFGF
AAVLMSLrqr rk

MW57065 Da; 512 aa


Ddg protein (ddg )
function 
interaction 
cofactors 
regulation 
topologytransmembrane domains: 1 (potential), SP has 2

TMHMM gives 20-42
SP gives 20-40 125-145

mfpqckfsre flhprywltW FGLGVLWLWV QLPYPVLCFL GTrigamarp
flkrresiar knlelcfpqh saeerekmia enfrslgmal vetgmawfwp
dsrvrkwfdv egldnlkraq mqnrgvmvvg vhfmslelgg rvmglcqpmm
atyrphnnql mewvqtrgrm rsnkamigrn nlrgivgalk kgeavwfapd 200
qdygrkgssf apffavenva ttngtyvlsr lsgaamltvt mvrkadysgy
rlfitpemeg yptdenqaaa ymnkiiekei mrapeqylwi hrrfktrpvg
esslyi

MW35493 Da; 306 aa


Lipid A biosynthesis lauroyl acyltransferase (htrB )
functionlipopolysaccharide core biosynthesis
interaction 
cofactors 
regulationinduction: at high temperatures, not heat shock induced!
topologytransmembrane domains: 1 (potential), SP has 2

TMHMM gives 16-38
SP gives 17-37 209-229

mtnlpkfsta llhprYWLTW LGIGVLWLVV QLPYPVIYrl gcglgklalr
fmkrrakivh rnlelcfpem seqerrkmvv knfesvgmgl metgmawfwp
drriarwtev igmehirdvq aqkrgillvg ihfltlelga rqfgmqepgi
gvyrpndnpl idwlqtwgrl rsnksmldrk dlkgmikalk kgevvwyapd 200
hdygprssvf vplfaveqaa tttgtwmlar msgaclvpfv prrkpdgkgy
qlimlppecs pplddaetta awmnkvvekc immapeqymw lhrrfktrpe
gvpsry

MW35407 Da; 306 aa


Lipid A biosynthesis Kdo2-(lauroyl)-lipid IVA acyltransferase (msbB )
functionlipopolysaccharide core biosynthesis
interaction 
cofactors 
regulation 
topologytransmembrane domains: 1 (potential), SP has 3

TMHMM gives 23-40
SP gives 23-43 85-105 133-153

metkknnsey ipefdksfrh prYWGAWLGV AAMAGIALTP pkfrdpilar
lgrfagrlgk ssrrralinl slcfpersea ereaivdemf atapqamamm
aelairgpek iqprvdwqgl eiieemrrnn ekviflvphg wavdipamlm
asqgqkmaam fhnqgnpvfd yvwntvrrrf ggrlharndg ikpfiqsvrq 200
gywgyylpdq dhgpehsefv dffatykatl paigrlmkvc rarvvplfpi
ydgkthrlti qvrppmddll eaddhtiarr mneeveifvg prpeqytwil
kllktrkpge iqpykrkdly pik

MW37410 Da; 323 aa


Glycosyltransferases

 Hexosyltransferases

Putative undecaprenyl-phosphate alpha-N-acelylglucosaminyltransferase (rfe )
functioninvolved in synthesis of enterobacterial common antigen (ECA), required for synthesis of lipopolysaccharide O-side chains
interaction 
cofactors 
regulation 
topologytransmembrane domains: 11 (potential)

TMHMM gives 5-24 45-66 70-89 105-127 131-153 160-179 184-206 213-232 242-261 294-311 321-338
SP gives 3-23 46-66 69-89 106-126 132-152 158-178 187-207 213-233 242-262 294-314 318-338

mnllTVSTDL ISIFLFTTLF LFFArkvakk vglvdkpnfr krhqGLIPLV
GGISVYAGIC FTFGIVdyyI PHASLYLACA GVLVFIGALd drfdisvkir
atiqAAVGIV MMVFGKLYLS SLGYIFGswe MVLGPFGYFL TLFAVWAAIN
AFNmvdgidG LLGGLSCVSF AAIGMILWFd gqtSLAIWCF AMIAAILPYI 200
MLNLGIlgrr ykVFMGDAGS TLIGFTVIWI LLettqgkth pISPVTALWI
IAIPLMDMVA Imyrrlrkgm spfspdrqhi hhlimragft srqAFVLITL
AAALLASIGV Laeyshfvpe WVMLVLFLLA FFLYGYCIkr awkvarfikr
vkrrlrrnrg gspnltk

MW40957 Da; 367 aa


Probable 4-alpha-l-fucosyltransferase (rffT )
functioninvolved in synthesis of enterobacterial common antigen (ECA), required for synthesis of lipopolysaccharide O-side chains
interaction 
cofactors 
regulation 
topologytransmembrane domains: 12 (potential)
MW51517 Da; 450 aa


 Pentosyltransferases

Monofunctional biosynthetic peptidoglycan transglycosylase (mtgA )
functioncell wall formation, final steps in peptidoglycan biosynthesis
interaction 
cofactors 
regulation 
topologytransmembrane domains: 1 (potential)

TMHMM gives 21-43
SP gives 19-39

msksrltvfs fvrrfllrlm VVLAVFWGGG IALFSVAPVP FSAvmverqv
sawlhgnfry vahsdwvsmd qispwmglav iaaedqkfpe hwgfdvasie
kalahnerne nrirgastis qqtaknlflw dgrswvrkgl eagltlgiet
vwskkriltv ylniaefgdg vfgveaaaqr yfhkpasklt rseaallaav 200
lpnplrfkvs spsgyvrsrq awilrqmyql ggepfmqqhq ld

MW27341 Da; 242 aa


Glycosyltransferases Transferring Other Glycosyl Groups

Prolipoprotein diacylglyceryl transferase (lgt )
functionfirst step in lipoprotein biosynthesis
interaction 
cofactors 
regulation 
topologytransmembrane domains: 5 (potential), SP has 7

TMHMM gives 15-37 58-80 95-117 223-245 260-282
SP gives 22-42 60-80 96-116 130-150 198-218 225-245 260-280

mtssylhfpe fdpvIFSIGP VALHWYGLMY LVGFIFAmwl atrranrpgs
gwtknevENL LYAGFLGVFL GGRIGYVLFY nfpqfmadpl ylfrVWDGGM
SFHGGLIGVI VVMIIFArrt krsffqvsdf iaplipfglg agrlgnfing
elwgrvdpnf pfamlfpgsr tedilllqtn pqwqsifdty gvlprhpsql 200
yelllegvvl fiilnlyirk prPMGAVSGL FLIGYGAFRI IVEFFrqpda
qftgawvqyI SMGQILSIPM IVAGVIMMVW AYrrspqqhv s

MW33108 Da; 291 aa


Glucans biosynthesis protein MdoC (mdoC/ymdD )
functionrequired for the succinyl substitution of periplasmic glucans
interaction 
regulation 
topologytransmembrane domains: 10 (potential)

TMHMM gives 17-39 54-76 88-110 136-158 179-198 213-235 242-261 276-295 308-330 334-356
SP gives 17-37 60-80 91-111 137-157 173-193 213-233 239-259 274-294 311-331 338-358

mnpvpaqrey fldsirAWLM LLGIPFHISL IYSSHTWHVn saesslwltl
fndFIHSFRM QVFFVISGYF SYMLFLrypl kkwwkvrver VGIPMLTAIP
LLTLPQFIML qyvkgkaesw pglslydkyn tlaweLISHL WFLLVLVVMT
TLCVWIFkri rnnlensdkt nkkfsmvkLS VIFLCLGIGY AVIRRTIFiv 200
yppilsngmf nFIVMQTLFY LPFFILGALA FIFphlkalf tTPSRGCTLA
AALAFVAYLL Nqrygsgdaw myeteSVITM VLGLWMVNVV FSFGHrllnf
qsarvtYFVN ASLFIYLVHH PLTLFFGAYI tphITSNWLG FLCGLIFVVG
IAIILYeihl ripllkflfs gkpvvkrend kapar

MW44690 Da; 385 aa


Transferases Transferring Alkyl or Aryl Groups, Other than Methyl Groups

1,4-Dihydroxy-2-naphtoate octaprenyltransferase (menA )
functionmenaquinone biosynthesis
interaction 
cofactors 
regulation 
topologytransmembrane domains: 9 (potential), SP has 8

TMHMM gives 21-40 44-63 98-117 121-143 150-172 177-199 228-247 251-270 290-307
SP gives 21-41 43-63 98-118 124-144 149-169 177-197 238-258 287-307

mteqqisrtq awleslrpkt LPLAFAAIIV GTALAWWQGH fdpLVALLAL
ITAGLLQILS NLAndygdav kgsdkpdrig plrgmqkgvi tqqemkrALI
ITVVLICLSG LALVAVAcht LADFVGFLIL GGLSIIAAIT YTVgnrpygY
IGLGDISVLV FFGWLSVMGS WYlqahTLIP ALILPATACG LLATAVLNIn 200
nlrdinsdre ngkntlvvrl gevnarrYHA CLLMGSLVCL ALFNLFSlhs
LWGWLFLLAA PLLVKQARYV mremdpvamr pmlertvkgA LLTNLLFVLG
IFLSQWAa

MW33594 Da; 308 aa


4-Hydroxybenzoate octaprenyltransferase (ubiA )
functionsecond step in ubiquinone biosynthesis
interaction 
cofactorsmagnesium
regulation 
topologytransmembrane domains: 8 (potential), TMHMM has 7

TMHMM gives 23-40 45-67 99-132 160-182 213-230 235-252 272-289
SP gives 23-43 46-66 100-120 141-161 163-183 213-233 234-254 268-288

mewsltqnkl lafhrlmrtd kpIGALLLLW PTLWALWVAT pgvpqLWILA
VFVAGVWLMR AAGCVVndya drkfdghvkr tanrplpsga vtekearaLF
VVLVLISFLL VLTLNTMTIL LSIAALALAW VYpfmkryth LPQVVLGAAF
GWSIPMAFaa VSESVPLSCW LMFLANILWA VAYdtqyamv drdddvkigi 200
kstailfgqy dkLIIGILQI GVLALMAIIG elngLGWGYY WSILVAGALF
VYqqklianr ereacfkafm nnnYVGLVLF LGLAMSYWhf

MW32511 Da; 290 aa


Transferases Transferring Phosphorous-Containing Groups

 Phosphotransferases with an Alcohol Group as Acceptor

Bacitracin resistance protein (bacA )
functionconfers resistance to bacitracin, probably by phosphorylation of undecaprenol
interaction 
cofactors 
regulation 
topologytransmembrane domains: 7 (potential)

TMHMM gives 13-35 50-69 90-109 119-136 187-209 224-246 253-272
SP gives 7-27 45-65 90-110 116-136 157-177 222-242 252-272

msdmhsllia aiLGVVEGLT EFLPVSSTGH MIIVGhllgf egdtaktfeV
VIQLGSILAV VVMFWRRLFg ligihfgrpl qhegeskgrL TLIHILLGMI
PAVVLGLLFh dtikslfnPI NVMYALVVGG LLLIAAeclk pkeprapgld
dmtyrqafmi gcfqclalwp gfsrsgatis ggmlmgVSRY AASEFSFLLA 200
VPMMMGATAl dlykswgflt sgdIPMFAVG FITAFVVALI AIKTFLqlik
riSFIPFAIY RFIVAAAVYV VFf

MW29758 Da; 273 aa


Diacylglycerol kinase (dgkA )
functionrecycling of diacylglycerol produced during the turnover of membrane phospholipid
interaction 
cofactors 
regulation 
topologytransmembrane domains: 2 (potential), SP has 3

TMHMM gives 56-78 98-120
SP gives 33-48 52-68 95-118

annttgftri ikaagyswkg lraawineaa frqegvavll avviacwldv
daitrVLLIS SVMLVMIVEI LNSAIEAVvd rigseyhels grakdmgSAA
VLIAIIVAVI TWCILLWSHF

MW13113 Da; 121 aa


Phosphotransferases with a Nitrogenous Group as Acceptor
(Sensor Proteins of Two-Component Regulatory Systems)

Nucleotidyltransferases

Phosphatidate cytidylyltransferase (cdsA )
functionphospholipid biosynthesis
interaction 
cofactors 
regulation 
topologytransmembrane domains: 7 (potential), TMHMM has 6

TMHMM gives 20-37 47-69 82-104 114-136 156-175 179-198
SP gives 20-40 57-77 85-105 115-135 154-174 177-197 228-248

mlaawewgql sgfttrsqrV WLAVLCGLLL ALMLFLLpey hrnihqPLVE
ISLWASLGWW IVALLLVLFy pgsaaiwrns kTLRLIFGVL TIVPFFWGML
ALRAwhyden hysGAIWLLY VMILVWGADS GAYMFGklfg khklapkvsp
gktwqGFIGG LATAAVISWG YGMWAnldVA PVTLLICSIV AALASVLGdl 200
tesmfkreag ikdsghlipg hggildridS LTAAVPVFAC LLLLVFrtl

MW27571 Da; 249 aa


Transferases for Other Substituted Phosphate Groups

Cardioplipin synthetase (cls )
functionaffects resistance to gyrase inhibitor novobiocin, condensation of two molecules of phosphatidylglycerol
interaction 
cofactors 
regulation 
topologytransmembrane domains: 2 (potential)

TMHMM gives 10-29 36-58
SP gives 7-25 37-58

mttvytLVSW LAILGYWLLI AGVTLRILMk rravpSAMAW LLIIYILPLV
GIIAYLAVge lhlgkrraer aramwpstak wlndlkackh ifaeenssva
aplfklcerr qgiagvkgnq lqlmtesddv mqalirdiql arhniemvfy
iwqpggmadq vaeslmaaar rgihcrlmld sagsvaffrs pwpelmrnag 200
ievvealkvn lmrvflrrmd lrqhrkmimi dnyiaytgsm nmvdpryfkq
dagvgqwidl marmegpiat amgiiyscdw eietgkrilp pppdvnimpf
eqasghtiht iasgpgfped lihqalltaa ysareylimt tpyfvpsddl
lhaictaaqr gvdvsiilpr kndsmlvgwa srafftella agvkiyqfeg 400
gllhtksvlv dgelslvgtv nldmrslwln feitlaiddk gfgadlaavq
ddyisrsrll darlwlkrpl wqrvaerlfy ffspll

MW54822 Da; 486 aa


CDP-diaglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (pgsA )
functionbiosynthesis of acidic phospholipids
interaction 
cofactors 
regulation 
topologytransmembrane domains: 4 (potential)

TMHMM gives 7-29 33-52 120-142 146-168
SP gives 13-37 61-81 87-107 146-168

qfniptLLTL FRVILIPFFV LVFYLPVTWs pfAAALIFCV AAVTDWFDGF
LArrwnqstr fgafldpvad kvlvaiamvl vtehyhswwv tlpaatmiar
eiiisalrew maelgkrssV AVSWIGKVKT TAQMVALAWL LWrpnIWVEY
AGIALFFVAA VLTLWSMLqy lsaaradlld q

MW20569 Da; 181 aa


Phospho-N-acetylmuramoyl-pentapeptid-transferase (mraY )
functionpeptidoglycan synthesis
interaction 
cofactors 
regulation 
topologytransmembrane domains: 10 (potential)

TMHMM gives 15-37 75-92 97-114 134-151 171-193 200-219 234-256 263-285 289-311 338-357
SP gives 19-45 77-90 97-113 134-156 174-188 200-220 239-251 271-284 288-299 342-357

mlvwlaehlv kyysGFNVFS YLTFRAIVSL LTALFISLWM gprmiahlqk
lsfgqvvrnd gpeshfskrg tptmGGIMIL TAIVISVLLW AYpsnpYVWC
VLVVLVGYGV IGFVddyrkv vrkdtkglia rwkYFWMSVI ALGVAFALYL
Agkdtpatql vvpffkdVMP QLGLFYILLA YFVIVGTGna vnltdgldgL 200
AIMPTVFVAG GFALVAWATg nmnfasylhi pylrhAGELV IVCTAIVGAG
LGFLWFntyp aqVFMGDVGS LALGGALGII AVLLrqefLL VIMGGVFVVE
TLSVILQVGS Fklrgqrifr mapihhhyel kgwpeprVIV RFWIISLMLV
LIGLATLkvr

MW39874 Da; 360 aa


Phosphoglycerol transferase I (mdoB )
functiontransferrs a phosphoglycerol residue from phosphatidylglycerol to MDO
interaction 
cofactors 
regulation 
topologytransmembrane domains: 4 (potential), TMHMM has 3

TMHMM gives 13-35 63-85 92-114
SP gives 13-33 64-84 95-115 197-217

mmsellsfalf lasv
liyawkagr ntWWFAATLT VLGLFVVLNI TLFASdyftg dgindavlyt
ltnsltgagv skYILPGIGI VLGLTAVFGA LGWILrrrrh hPHHFGYSLL
ALLLALGSVD ASPAfrqite lvksqsrdgd pdfaayykep sktipdpkln
lvyiygesle rtyfdneafp dltpelgalk negldfshtq qlpgtdYTIA
GMVASQCGIP LFAPFegnas asvssffpqn iclgdilkns gyqnyfvqga
nlrfagkdvf lkshgfdhly gseelksvva dphyrndwgf yddtvldeaw
kkfeelsrsg qrfslftltv dthhpdgfis rtcnrkkydf dgkpnqsfsa
vscsqeniat finkikaspw fkdtvivvss dhlamnntaw kylnkqdrnn
lffvirgdkp qqetlavkrn tmdngatvld ilggdnylgl grsslsgqsm
seiflnikek tlawkpdiir lwkfpkemke ftidqqknmi afsgshfrlp
lllrvsdkrv eplpeseysa plrfqladfa prdnfvwvdr cykmaqlwap
elalstdwcv sqgqlggqqi vqhvdkttwq gktafkdtvi dmarykgnvd
tlkivdndir ykadsfifnv agapeevkqf sgisrpeswg rwsnaqlgde
vkieykhplp kkfdlvitak aygnnasrpi pvrvgneeqt lvlgnevttt
tlhfdnptda dtlvivppep vstnegnilg hsprklgigm veikvvereg

MW85494 Da; 763 aa


Hydrolases

Hydrolases Acting on Ester Bonds

Carboxylic Monoester Hydrolases


Lysophospholipase L2 (pldB )
functionlipid synthesis
interaction 
cofactors 
regulation 
topologytransmembrane domains: 0 (potential)
MW38893 Da; 340 aa


Phosphoric Monoester Hydrolases

Phosphatidylglycerophosphatase A (pgpA )
functionphospholipid degradation
interaction 
cofactors 
regulation 
topologytransmembrane domains: 3 (potential)

TMHMM gives 21-43 53-75 141-163
SP gives 32-52 54-74 142-162

mtilprhkdv aksrlkmsnp WHLLAVGFGS GLSPIVPGTM GSLaaipfwy
lmTFLPWQLY SLVVMLGICI GVYLChqtak dmgvhdhgsi vwdefigmwi
tlmalptndw qwvaagfvif rildmwkpwp irwfdrnvhg GMGIMIDDIV
AGVISAGILY FIGhhwplgi ls

MW19418 Da; 172 aa


Phosphatidylglycerophosphatase B (pgpB )
functionphospholipid degradation (inner and outer membranes)
interaction 
cofactors 
regulation 
topologytransmembrane domains: 6 (potential)

TMHMM gives 7-29 49-68 75-92 159-179 186-208 212-229
SP gives 9-29 48-68 72-92 159-179 185-205 211-231

mrsiarrtaV GAALLLVMPV AVWISGWrwq pgeqswllka afwvtetVTQ
PWGVITHLIL FGWFLWCLrf rikaaFVLFA ILAAAILVGQ GVkswikdkv
qeprpfviwl ekthhipvde fytlkraerg nlvkeqlaee knipqylrsh
wqketgFAFP SGHTMFAASW ALLAVGLLWp rrrtLTIAIL LVWATGVMGS 200
RLLLGMHWpr dLVVATLISW ALVAVATWLa qricgpltpp aeenreiaqr
eqes

MW29021 Da; 254 aa


Hydrolases Acting on Peptide Bonds (Proteases)

Cell division protein FtsH (hflB )
functionessential ATP-dependent zinc metalloprotease, cleaves soluble and integral membrane proteins. Involved in the degradation of sigma-32
interaction 
cofactorsbinds and requires a zinc atom
regulation 
topologytransmembrane domains:2 (potential)

TMHMM gives 5-24 97-119
SP gives 5-24 96-120

maknLILWLV IAVVLMSVFQ SFgpsesngr kvdystflqe vnndqvrear
ingreinvtk kdsnryttyi pvqdpklldn lltknvkvvg eppeepSLLA
SIFISWFPML LLIGVWIFFm rqmqggggkg amsfgkskar mltedqiktt
fadvagcdea keevaelvey lrepsrfqkl ggkipkgvlm vgppgtgktl 200
lakaiageak vpfftisgsd fvemfvgvga srvrdmfeqa kkaapciifi
deidavgrqr gaglggghde reqtlnqmlv emdgfegneg iiviaatnrp
dvldpallrp grfdrqvvvg lpdvrgreqi lkvhmrrvpl apdidaaiia
rgtpgfsgad lanlvneaal faargnkrvv smvefekakd kimmgaerrs 400
mvmteaqkes tayheaghai igrlvpehdp vhkvtiiprg ralgvtfflp
egdaisasrq klesqistly ggrlaeeiiy gpehvstgas ndikvatnla
rnmvtqwgfs eklgpllyae eegevflgrs vakakhmsde tariidqevk
aliernynra rqlltdnmdi lhamkdalmk yetidapqid dlmarrdvrp 600
pagweepgas nnsgdngspk aprpvdeprt pnpgntmseq lgdk

MW70708 Da; 644 aa


HflC protein (hflC )
functionHflC and HflK govern the stability of phage lambda cII protein and have been proposed to encode or regulate a cII specific protease
interactionHflK and HflC may interact to form a multimeric complex
cofactors 
regulation 
topologytransmembrane domains: 1 (potential)

TMHMM gives 5-23
SP gives 3-23

mrksVIAIII IVLVVLYMSV FVVkegergi tlrfgkvlrd ddnkplvyep
glhfkipfie tvkmldariq tmdnqadrfv tkekkdlivd syikwrisdf
sryylatggg disqaevllk rkfsdrlrse igrldvkdiv tdsrgrltle
vrdalnsgsa gtedevttpa adnaiaeaae rvtaetkgkv pvinpnsmaa 200
lgievvdvri kqinlptevs eaiynrmrae reavarrhrs qgqeeaeklr
atadyevtrt laeaerqgri mrgegdaeaa klfadafskd pdfyafirsl
rayensfsgn qdvmvmspds dffrymktpt satr

MW37649 Da; 334 aa


Heat shock protein HtpX (htpX )
functionpotential metalloprotease
interaction 
cofactors 
regulationinduction: temperature upshift by the sigma 32 heat shock transcription factor
topologytransmembrane domains: 4 (potential)

TMHMM gives 5-27 32-54 158-180 195-217
SP gives 7-27 35-51 158-178 193-213

mmriALFLLT NLAVMVVFGL VLSLTGIqss sVQGLMIMAL LFGFGGSFVS
LLMSkwmalr svggevieqp rnererwlvn tvatqarqag iampqvaiyh
apdinafatg arrdaslvav stgllqnmsp deaeaviahe ishiangdmv
tmtliqgVVN TFVIFISRIL AQLAAGFMGG nrdegeesng npliYFAVAT 200
VLELVFGILA SIITMWFsrh refhadagsa klvgrekmia alqrlktsye
pqeatsmmal cingksksls elfmthppld kriealrtge ylk

MW31923 Da; 293 aa


Metalloprotease YaeL (yaeL )
functionRIP protease
interaction 
regulation 
topologytransmembrane domains: 4 (potential), SP has 3

TMHMM gives 2-21 98-120 376-398 426-445
SP gives 107-127 376-396 430-450

mLSFLWDLAS FIVALGVLIT Vhefghfwva rrcgvrverf sigfgkalwr
rtdklgteyv ialiplggyv kmlderaepv vpelrhhafn nksvgqrAAI
IAAGPVANFI FAIFAYWLVF iigvpgvrpv vgeiaansia aeaqiapgte
lkavdgietp dwdavrlqlv dkigdestti tvapfgsdqr rdvkldlrhw 200
afepdkedpv sslgirprgp qiepvlenvq pnsaaskagl qagdrivkvd
gqpltqwvtf vmlvrdnpgk slaleierqg splsltlipe skpgngkaig
fvgiepkvip lpdeykvvrq ygpfnaivea tdktwqlmkl tvsmlgklit
gdvklnnlsg pisiakgagm taelgVVYYL PFLALISVNL GIINLFPLpv 400
ldgghllfla iekikggpvs ervqdFCYRI GSILLVLLMG LALFNdfsrl

MW49071 Da; 450 aa


Serine Endopeptidases

Signal peptidase I (lepB )
functionserine protease, cleavage of N-terminal leader sequences of secreted and periplasmic protein precursors
interaction 
cofactors 
regulation 
topologyPDB

transmembrane domains: 2 (N-out)

TMHMM gives 5-27 60-82
SP gives 4-22 59-77

manmFALILV IATLVTGILW CVDKFFFapk rrerqaaaqa aagdsldkat
lkkvapkpgW LETGASVFPV LAIVLIVRSF IYepfqipsg smmptlligd
filvekfayg ikdpiyqktl ietghpkrgd ivvfkypedp kldyikravg
lpgdkvtydp vskeltiqpg cssgqacena lpvtysnvep sdfvqtfsrr 200
nggeatsgff evpknetken girlserket lgdvthrilt vpiaqdqvgm
yyqqpgqqla twivppgqyf mmgdnrdnsa dsrywgfvpe anlvgratai
wmsfdkqege wptglrlsri ggih

MW35960 Da; 324 aa


Protease IV (sppA )
functionserine protease involved in digestion of the cleaved signal peptides
homotetramer
interaction 
cofactors 
regulation 
topologytransmembrane domains: 3 (potential), TMHMM has 1

TMHMM gives 21-43
SP gives 29-45 398-414 421-441

mrtlwrfiag ffkwtwrlln FVREMVLNLF FIFLVLVGVG IWMqvsggds
ketasrgall ldisgvivdk pdssqrfskl srqllgassd rlqenslfdi
vntirqakdd rnitgivmdl knfaggdqps mqyigkalke frdsgkpvya
vgenysqgqy ylasfankiw lspqgvvdlh gfatnglyyk slldklkvst 200
hvfrvgtyks avepfirddm spaareadsr wigelwqnyl ntvaanrqip
aeqvfpgaqg llegltktgg dtakyalenk lvdalassae iekaltkefg
wsktdknyra isyydyalkt padtgdsigv vfangaimdg eetqgnvggd
ttaaqirdar ldpkvkaivl rvnspggtvt aseviraela aaraagkpVV 400
VSMGGMAASG GYWIstpanY IVANPSTLTG SIGIFGVITT Vensldsigv
htdgvstspl advsitralp peaqlmmqls iengykrfit lvadarhstp
eqidkiaqgh vwtgqdakan glvdslgdfd davakaaela kvkqwhleyy
vdeptffdkv mdnmsgsvra mlpdafqaml paplasvast vksesdklaa 600
fndpqnryaf cltcanmr

MW67233 Da; 618 aa


Possible protease SohB (sohB )
functionSerine protease, suppressor of degP(htrA) null mutation
interaction 
cofactors 
regulation 
topologytransmembrane domains: 1 (potential), TMHMM has 2

TMHMM gives 10-32 190-207
SP gives 9-29

mellseyglF LAKIVTVVLA IAAIAAIIVN VAqrnkrqrg elrvnnlseq
ykemkeelaa almdshqqkq whkaqkkkhk qeakaakaka klgevatdsk
prvwvldfkg smdahevnsl reeitavlaa fkpqdqvvlr lespggmvhg
yglaasqlqr lrdknipltv tvdkvaasgg ymmacvadki vsapfaivgs 200
igvvaqmpnf nrflkskdid ielhtagqyk rtltllgent eegrekfree
lnethqlfkd fvkrmrpsld ieqvatgehw ygqqavekgl vdeintsdev
ilslmegrev vnvrymqrkr lidrftgsaa esadrlllrw wqrgqkplm

MW39366 Da; 349 aa


Aspartic Endopeptidases

Lipoprotein signal peptidase (lspA )
functionspecifically catalyses the removal of N-terminal leader sequences from membrane prolipoproteins
interaction 
cofactors 
regulation 
topologytransmemebrane domains: 4 (potential)

TMHMM gives 13-35 67-86 99-121 136-158
SP gives 12-26 70-88 96-113 142-159

msqsicstgl rwLWLVVVVL IIDLGSKYLI LQNFAlgdtv plfpslnlhy
arnygaafsf ladsggWQRW FFAGIAIGIS VILAVMMYrs katqklnnIA
YALIIGGALG NLFDRLWHGF Vvdmidfyvg dwhfaTFNLA DTAICVGAAL
IVLEGFLPsr akkq

MW18156 Da; 164 aa


Leader peptidase PppA (pppA )
functionpotential leader peptidase
interaction 
cofactors 
regulation 
topologytransmemebrane domains: 7 (potential)

TMHMM gives 15-37 102-120 124-141 148-167 177-196 209-231 246-268
SP gives 0

mlfdvfqqyp tampVLATVG GLIIGSFLNV VIWrypimlr qqmaefhgem
ssaqskisla lprshcphcq qtirirdnip lfswlmlkgr crdcqakisk
rYPLVELLTA LAFLLASLVW pesgWGLAVM ILSAWLIAAS VIdldhqWLP
DVFTQGVLWT GLIAAWAqqs pltlqdAVTG VLVGFITFYS LRWIAGIVLr 200
kealgmgdVL LFAALGGWVG ALSLPNVALI Asccgliyav itkrgstTLP
FGPCLSLGGI ATLYLQALF
IVLEGFLPsr akkq

MW29466 Da; 269 aa


Endopeptidase of Unknown Catalytic Mechanism

Type-4 prepilin-like protein specific leader peptidase (hopD )
functionpotential aspartic protease, cleaves type-4 fimbrial leader sequence and methylates the N-terminal (generally phe) residue
interaction 
cofactors 
regulation 
topologytransmembrane domains: 7 (potential), SP has 6

TMHMM gives 7-29 49-71 78-100 104-122 127-149 169-191 204-223
SP gives 3-23 68-88 104-124 128-148 175-195 203-223

mtMLLPLFIL VGFIADYFVN AIAYhlsple dktaltfrqv lvhfrqkkYA
WHDTVPLILC VAAAIACALA PFtpIVTGAL FLYFCFVLTL SVIdfrtqll
pdkLTLPLLW LGLVFNAQYG LIdlhdaVYG AVAGYGVLWC VYWGVWLVCh
keglgygdfk llaaagaWCG WQTLPMILLI ASLGGIGYAI Vsqllqrrti 200
ttIAFGPWLA LGSMINLGYL AWIsy

MW24957 Da; 225 aa


Hydrolases Acting on Acid Anhydrides in Phosphorous-Containing Anhydrides


Ligases
 Forming Carbon-Nitrogen Bonds

 Acid Amino-Acid Ligases (Peptide Synthases)


Probable crotonobetaine/carnitine-CoA ligase (caiC )
functioncarnitine metabolism
interaction 
cofactors 
regulation 
topologytransmembrane domains: 0 (potential), SP has 2

TMHMM gives 0
SP gives 77-97 231-251

mdrgamdiig gqhlrqmwdd ladvyghkta licessggvv nrysylelnq
einrtanlfy tlgirkgdkv alhldncpef ifcwfglaki gaimvpinar
llceesawil qnsqacllvt saqfypmyqq iqqedatqlr hicltdvalp
addgvssftq lknqqpatlc yapplstddt aeilftsgtt srpkgvvith 200
ynlrfagyys awqcalrddd vyltvmpafh idcqctaama afsagatfvl
vekysarafw gqvqkyratv tecipmmirt lmvqppsand qqhrlrevmf
ylnlseqekd afcerfgvrl ltsygmteti vgiigdrpgd krrwpsigrv
gfcyeaeird dhnrplpage igeicikgip gktifkeyfl npqatakvle 400
adgwlhtgdt gyrdeedffy fvdrrcnmik rggenvscve leniiaahpk
iqdivvvgik dsirdeaika fvvlnegetl seeeffrfce qnmakfkvps
yleirkdlpr ncsgkiirkn lk

MW59089 Da; 522 aa


2,3-Dihydroxybenzoate-AMP ligase (entE )
functionenterobactin (iron chelating compound) biosynthesis
EntD, EntE, EntF and EntG form a multienzyme complex called enterochelin synthase
interaction 
cofactors 
regulation 
topologytransmembrane domains: 0 (potential), SP has 2

TMHMM gives 0
SP gives 86-105 244-268

msipftrwpe efarryrekg ywqdlpltdi ltrhaasdsi avidgerqls
yrelnqaadn lacslrrqgi kpgetalvql gnvaelyitf fallklgvap
vlalfshqrs elnayasqie palliadrqh alfsgddfln tfvtehssir
vvqllndsge hnlqdainhp aedftatpsp adevayfqls ggttgtpkli 200
prthndyyys vrrsveicqf tqqtrylcai paahnyamss pgslgvflag
gtvvlaadps atlcfpliek hqvnvtalvp pavslwlqal iegesraqla
slkllqvgga rlsatlaari paeigcqlqq vfgmaeglvn ytrlddsaek
iihtqgypmc pddevwvada egnplpqgev grlmtrgpyt frgyykspqh 400
nasafdangf ycsgdlisid pegyitvqgr ekdqinrgge kiaaeeienl
llrhpaviya alvsmedelm gekscaylvv keplravqvr rflreqgiae
fklpdrvecv dslpltavgk vdkkqlrqwl asrasa

MW59112 Da; 536 aa


Enterobactin synthetase component F (entF )
functionenterobactin (iron chelating compound) biosynthesis
EntD, EntE, EntF and EntG form a multienzyme complex called enterochelin synthase
interaction 
cofactorscontains a covalently bound phosphopantethein
regulation 
topologytransmembrane domains: 0 (potential)
MW141990 Da; 1293 aa


O-antigen ligase (rfaL )
functionlipopolysaccharide core biosynthesis
interaction 
cofactors 
regulation 
topologytransmembrane domains: 10 (potential), SP has 11

TMHMM gives 20-37 41-60 72-91 106-128 135-157 167-189 240-258 349-368 373-392 396-413
SP gives 18-38 40-60 72-92 106-126 136-156 169-189 242-262 289-309 347-367 370-390 391-411

mltsfklhsl kpytlkssmI LEIITYILCF FSMIIAFvdn TFSIKIYNIT
AIVCLLSLIL rgrqenynik nLILPLSIFL IGLLDLIWYS Afkvdnspfr
atyhsYLNTA KIFIFGSFIV FLTLTSQLks kkesVLYTLY SLSFLIAGYA
MYINSIHend risfgvGTAT GAAYSTMLIG IVSGVAILYt kknhpflfll 200
nscagtlcsg antnqsnptp vpyncvaali ayynkspkkF TSSIVLLIAI
LASIVIIFnk piqnryneal ndlnsytnan svtslgarla myeiglnifi
kspfsftsae sraesmnllv aehnrlrgal efsnvhlhne iiergslkGL
MGIFSTLFLY FSLFYIAYkk raLGLLILTL GIVGIGLSDV IIwarSIPII 400
IISAIVLLLV INNrnntin

MW46683 Da; 419 aa


Disulfide Bond Formation

Disulfide bond formation protein B (dsbB )
functionoxidizes DsbA protein
interaction 
cofactors 
regulation 
topologytransmembrane domains: 4

TMHMM gives 13-32 42-64 71-89 145-162
SP gives 15-31 50-65 72-89 145-163

mlrflnqcsq grGAWLLMAF TALALELTAL WFqhvmllkp cVLCIYERCA
LFGVLGAALI GAIApktplr YVAMVIWLYS AFRGVQLTYe htmlqlypsp
fatcdfmvrf pewlpldkwv pqvfvasgdc aerqwdflgl empqWLLGIF
IAYLIVAVLV VIsqpfkakk rdlfgr

MW20142 Da; 176 aa


Thiol:disulfide interchange protein DsbD (dsbD )
functionreduces DsbC protein
interaction 
cofactors 
regulation 
topologytransmembrane domains: 7 (potential)

TMHMM gives 88-110 130-152 165-187 217-239 246-268 283-300 307-329
SP gives 94-118 130-154 166-188 213-237 246-270 284-300 312-329

maqriftlil llcstsvfag lfdapgrsqf vpadqafafd fqqnqhdlnl
twqikdgyyl yrkqiritpe hakiadvqlp qgvwhedefy gkseiyrdrl
tlpvtinqas agatltvtyq gcadagfcyp petktvplse vvannaapqp
vsvpqqeqpt aqlpFSALWA LLIGIGIAFT PCVLPMYpli sgivlggkqr 200
lstaraLLLT FIYVQGMALT YTALGLVVAa aglqfqaalq hPYVLIGLAI
VFTLLAMSMF GLFTlqlpss lqtrltlmsn rqqggspggv fvmGAIAGLI
CSPCTTAPLS AILLYIaqsg nmWLGGGTLY LYALGMGLPL MLITVfgnrl
lpksgpwmeQ VKTAFGFVIL ALPVFLLerv igdVWGLRLW SALGVAFFGW 400
AFITSLqakr gwmrivqiil laaalvsvrp lqdwafgath taqtqthlnf
tqiktvdeln qalveakgkp vmldlyadwc vackefekyt fsdpqvqkal
adtvllqanv tandaqdval lkhlnvlglp tilffdgqgq ehpqarvtgf
mdaetfsahl rdrqp

MW61795 Da; 565 aa