Proteases of E. coli



Databases
ECCE   
Proteases of E. coli  
Maltose transporter
DNA sequences  
Software
Dana's tools  
Strategy

Gene expression in
E. coli


TEV NIa protease
as a tool




  Search all files of this site


© 2001 Webdesign by
Tilman Maier
74 peptidases/proteases are listed. The majority are metalloproteases, followed by Ser proteases, Cys proteases and Asp proteases. Proteases are listed according to their celluar localisation and in alphabetical order. MWs of periplasmic and outer membrane proteases are given for the unprocessed precursor proteins. Clicking on the protein name will open the latest SwissProt file.

The topology for each cytoplasmic membrane protein is predicted. Protein sequences are presented in lower case and the TMs in upper case.
To find out how it was done and to learn more about this topic click here



Proteases localised in the

Cytoplasm
Cytoplasmic membrane
Periplasm
Outer membrane




Cytoplasm

Aminobenzoyl-glutamate utilization protein A (abgA )
Peptidase familyM40 InterPro
Function 
Structure 
MW46588 Da
436 aa


Leucine aminopeptidase LAP (ampA )
Peptidase familyM17 InterPro
Function 
Structure 
MW54879 Da
503 aa


Methionine aminopeptidase (ampM )
Peptidase familyM24A InterPro
FunctionRemoves the N-terminal methionine from nascent proteins
StructurePDB
MW29331 Da
264 aa


Xaa-Pro aminopeptidase/AmpP (pepP )
Peptidase familyM24B InterPro
FunctionReleases any N-terminal amino acid preceding proline, even from short peptides
StructurePDB
MW49684 Da
440 aa


ATP-dependent Clp protease proteolytic subunit (clpP )
Peptidase familyS14 InterPro
FunctionHeat shock protein, chymotrypsin-like activity, major role in the degradation of misfolded proteins, interacts with chaperone subunits ClpA and X
Structure PDB
MW23186 Da
207 aa


Dipeptidyl carboxypeptidase (dcp )
Peptidase familyM3 InterPro
FunctionRemoves dipeptides from the c-termini of oligopeptides, broad specificity, does not hydrolyse bonds in which p1' is Pro, or both p1 and p1' are Gly
Structure 
MW77384 Da
680 aa


D-alanyl-D-alanine dipeptidase (ddpX/vanX )
Peptidase familyM45 InterPro
FunctionHydrolyses Ala-Ala
Structure 
MW21213 Da
193 aa

ElaD protein (elaD )
Peptidase familySUMO/Ulp1_C InterPro
FunctionCys protease?
Structure 
MW45947 Da
402 aa

Putative frv operon protein FrvX (frvX )
Peptidase familyM42/Glutamyl aminopeptidase (Lactococcus)
FunctionUnclear, homologous to SgcX of ECOLI
Structure 
MW38733 Da
356 aa

Gcp Glycoprotease (gcp/b3064 )
Peptidase familyM22 InterPro
Function 
Structure 
MW36024 Da
337 aa

Heat shock protein HslV (hslV )
Peptidase familyT1B InterPro
FunctionThr-Protease subunit of HslUV complex, interacts with chaperone subunit HslU
Structure PDB
MW18961 Da
175 aa

Heat shock protein 31 (hchA / b1967 )
Peptidase familyCys protease? InterPro
FunctionCrystal structure reveals a His Asp Cys catalytic triad. Hsp31 was previously characterised as a chaperone.
Structure PDB
MW31059 Da
282 aa

Hydrogenase 1 maturation protease (hyaD )
Peptidase familyM52 InterPro
FunctionInvolved in maturation (C-terminal processing) of HyaB, the subunit of hydrogenase 1
Structure 
MW21546 Da
195 aa

Hydrogenase 2 maturation protease (hybD )
Peptidase familyM52 InterPro
FunctionInvolved in maturation (C-terminal processing) of HybB, the subunit of hydrogenase 2
Structure PDB
MW17751 Da
164 aa

Formate hydrogenlyase maturation protein HycH (hycH )
Peptidase family 
FunctionInvolved in maturation of the large subunit of hydrogenlyase HycE
Structure 
MW15465 Da
136 aa

Hydrogenase 3 maturation protease (hycI )
Peptidase familyM52 InterPro
FunctionInvolved in maturation (C-terminal processing) of HycE, the large subunit of hydrogenase 3
Structure 
MW16925 Da
155 aa

Isoaspartyl dipeptidase IadA (iadA )
Peptidase familyM38
FunctionHydrolyses l-isoaspartyl (l-beta-aspartyl) dipeptides, to degrade proteins damaged by l-isoaspartyl residue formation
Structure PDB
MW41084 Da
390 aa

Muramoyltetrapeptide carboxypeptidase (LdcA )
Peptidase familyunknown
FunctionConverts cytosolic UDP-MurNac-Tetrapeptides to Tripeptides, essential for viability during stationary phase
Structure 
MW33567 Da
304 aa

Lon protease homolog (ycbZ )
Peptidase familyS16
FunctionLacks ATP ase domain of Lon
Structure 
MW65818 Da
586 aa

Protease Lon (lon )
Peptidase familyS16 InterPro
FunctionHeat shock protein, ATP-dependent Ser protease, broad substrate specificity
Structure PDB
MW87438 Da
784 aa

Aminoacyl-histidine dipeptidase/Peptidase D (pepD )
Peptidase familyM25 InterPro
FunctionXaa-His dipeptidase, has specificity for the unusual dipeptide beta-alanyl-l-histidine.
Structure 
MW52784 Da
484 aa

Alpha-aspartyl dipeptidase /Peptidase E (pepE )
Peptidase familyserine (according to MEROPS)
FunctionHydrolyses dipeptides containing n-terminal aspartate residues
Structure 
MW24570 Da
229 aa

X-Pro dipeptidase/Peptidase Q (pepQ )
Peptidase familyM24B InterPro
FunctionHydrolysis of Xaa-|-Pro dipeptides, but not on Pro-|-Pro
Structure 
MW50176 Da
443 aa

Aminotripeptidase/Peptidase T (pepT )
Peptidase familyM20A InterPro
FunctionHydrolyzes a tripeptides containing n-terminal Met, Leu, or Phe
Structure PDB
MW44923 Da
408 aa

Hypothetical protease PmbA (pmbA or tldE or b4235 )
Peptidase familyunknown
Functionrequired for the production of the antibiotic peptide MccB17
Structure 
MW48369 Da
450 aa

Probable zinc protease PqqL (pqqL/b1494 )
Peptidase familyM16 InterPro
Function 
Structure 
MW104656 Da
931 aa

Oligopeptidase A (prlC )
Peptidase familyM3 InterPro
Function 
Structure 
MW77167 Da
680 aa

Protease II (ptrB )
Peptidase familyS9A InterPro
FunctionCleaves after Lys and Arg residues
Structure 
MW79490 Da
686 aa

Putative sgc operon protein SgcX (sgcX )
Peptidase familyM42/Glutamyl aminopeptidase (Lactococcus)
FunctionUnclear, homolog of FrvX of E. coli
Structure 
MW41729 Da
383 aa

SprT Protein (sprT )
Peptidase familyZn MTpeptdseInterPro
Function 
Structure 
MW19348 Da
165 aa

Hypothetical protease TldD (tldD or b3244 )
Peptidase familyunknown
Function 
Structure 
MW51364 Da
481 aa

Putative metalloprotease YcaL (ycaL )
Peptidase familyM48InterPro
FunctionHomolog of YggG of E. coli
Structure 
MW26740 Da
254 aa

Hypothetical protease YeaZ (yeaZ )
Peptidase familyM22InterPro
Function 
Structure 
MW25181 Da
231 aa

Putative protease YegQ (yegQ )
Peptidase familyU32InterPro
Function 
Structure 
MW51193 Da
453 aa

Hypothetical protein YgeY (ygeY )
Peptidase familyM20AInterPro
Function 
Structure 
MW44804 Da
403 aa

Putative metalloprotease YggG (yggG )
Peptidase familyM48InterPro
FunctionHomolog of YcaL of E. coli
Structure 
MW26842 Da
252 aa

Putative Cys protease YhbO (yhbO )
Peptidase familyC40
Function 
Structure 
MW18858 Da
172 aa

Hypothetical protein YibP (yibG )
Peptidase familyM37InterPro
Function 
Structure 
MW46594 Da
419 aa

Hypothetical protein YpdF (ypdF )
Peptidase familyM24InterPro
Function 
Structure 
MW39624 Da
361 aa



Cytoplasmic membrane

Protease DegS (degS )
Peptidase familyS2C InterPro
FunctionEssential serine protease, Cleaves RseA to induce sigma E cascade
StructurePDB

transmembrane domains: 1 (N-in)

TMHMM gives 5-27
SP gives signal seq.

mfvkllrsVA IGLIVGAILL VAMPSLrsln plstpqfdst detpasynla vrraapavvn
vynrglntns hnqleirtlg sgvimdqrgy iitnkhvind adqiivalqd grvfeallvg
sdsltdlavl kinatgglpt ipinarrvph igdvvlaign pynlgqtitq giisatgrig
lnptgrqnfl qtdasinhgn sggalvnslg elmgintlsf dksndgetpe gigfaipfql
atkimdklir dgrvirgyig iggreiaplh aqgggidqlq givvnevspd gpaanagiqv
ndliisvdnk paisaletmd qvaeirpgsv ipvvvmrddk qltlqvtiqe ypatn

MW37581 Da
355 aa


FtsH (ftsH/hflB )
Peptidase familyM41/AAA Protease InterPro
Functionessential ATP-dependent zinc metalloprotease, cleaves soluble and integral membrane proteins
Structure PDB

transmembrane 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

GlpG (glpG )
Peptidase familyS54 InterPro
Function 
Structuretransmembrane domains: 6 (potential)

Phobius gives 96-115 135-160 172-188 194-212 224-242 248-267
SP gives none

mlmitsfanp rvaqafvdym atqgviltiq qhnqsdvwla desqaervra
Elarflenpa dprylaaswq aghtgsglhy rrypffaalr eragpVTWVM
MIACVVVFIA MQILGdqevm lwlawpfdpt lkfeFWRYFT HALMHFSLMH
ILFNLLWWWY LGGAVekrlg sgkLIVITLI SALLSGYVQQ kfsgpWFGGL
SGVVYALMGY VWLrgerdpq sgIYLQRGLI IFALIWIVAG WFdlfGMSMA
NGAHIAGLAV GLAMAFVdsl narkrk

MW31307 Da
276 aa

Heat shock protein HtpX (htpX )
Peptidase familyM48 InterPro
Function 
Structuretransmembrane 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

Leader peptidase Lep4/Prepilin-like protein (hofD/hopD )
Peptidase familyA24 InterPro
FunctionLeader peptidase, cleaves type-4 fimbrial leader sequence
Structuretransmembrane 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

Leader peptidase I (LepB )
Peptidase familyS26 InterPro
FunctionGeneral leader peptidase
StructurePDB

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

Lipoprotein signa l peptidase (lspA )
Peptidase familyA8 InterPro
FunctionLeader peptidase, removes signal peptides from lipoproteins
Structuretransmemebrane 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
MW18156 Da
164 aa

Leader peptidase PppA (pppA )
Peptidase familyA24 InterPro
FunctionLeader peptidase, removes signal peptides from lipoproteins
Structuretransmemebrane 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

MW29466 Da
269 aa

Possible Ser protease SohB (sohB )
Peptidase familyS49 InterPro
FunctionSuppressor of degP(htrA) null mutation
Structuretransmembrane 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

Signal peptide peptidase/Protease IV (sppA )
Peptidase familyS49 InterPro
FunctionDegrades cleaved signal peptides
Structuretransmembrane 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

YaeL (yaeL )
Peptidase familyM50B InterPro
FunctionRIP protease, degrades the antisigma factor RseA
Structuretransmembrane 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

YfbL (yfbL )
Peptidase familyM28A
Function 
Structuretransmembrane domains: 1 (potential)

TMHMM gives 5-27
SP gives 4-24

mkkIIFAFII LFVFLLPMII FYQPWVnalp stprhaspeq lektvryltq
tvhprsadni dnlnrsaeyi kevfvssgar vtsqdvpitg gpyknivady
gpadgpliii gahydsassy endqltytpg addnasgvag llelarllhq
qvpktgvqlv ayaseeppff rsdemgsavh aaslerpvkl mialemigyy 200
dsapgsqnyp ypamswlypd rgdfiavvgr iqdinavrqv kaallssqdl
svysmntpgf ipgidfsdhl nywqhdipai mitdtafyrn kqyhlpgdta
drlnyqkmaq vvdgvitlly nsk

MW35931 Da
323 aa



Periplasm

PBP-5, D-alanyl-D-alanine carboxypeptidase fraction A (dacA )
Peptidase familyS11InterPro
FunctionCell wall formation
Structure PDB
MW44444 Da
403 aa (1-29 signal pept.)

PBP-4, D-alanyl-D-alanine carboxypeptidase (dacB )
Peptidase familyS13InterPro
FunctionCell wall formation
Structure 
MW51798 Da
477 aa (1-20 signal pept.)

PBP-6, D-alanyl-D-alanine carboxypeptidase fraction C (dacC )
Peptidase familyS11InterPro
FunctionCell wall formation
Structure 
MW43609 Da
400 aa (1-27 signal pept.)

PBP-6B, D-alanyl-D-alanine carboxypeptidase (dacD )
Peptidase familyS11InterPro
FunctionCell wall formation
Structure 
MW43346 Da
388 aa (1-21 signal pept.)

Protease Do (degP/htrA )
Peptidase familyS2C InterPro
FunctionHeat shock protein, serine protease and chaperone ectivities, required at high temperature, virulence factor, involved in refolding and degradation of damaged proteins
StructurePDB
MW49439 Da
474 aa (1-26 signal pept.)


Protease DegQ (degQ )
Peptidase familyS2C InterPro
FunctionSerine protease
Structure 2 PDZ domains
MW47205 Da
455 aa (1-27 signal pept.)


Alkaline phosphatase isozyme conversion protein IAP (iap or b2753 )
Peptidase familyM28C
Function 
Structure 
MW37920 Da
345 aa (1-24 signal pept.)


Penicillin-insensitive D-alanyl-D-alanine-endopeptidase (mepA )
Peptidase familyUnknown
FunctionCell wall formation
Structure 
MW30136 Da
274 aa (1-19 signal pept.)

Putative Cys protease NlpC (nlpC )
Peptidase familyC40
Function 
Structurepotential lipoprotein
MW17283 Da
154 aa (1-15 signal pept.)

PBP-7, D-alanyl-D-alanine-endopeptidase (pbpG or b2134 )
Peptidase familyS11InterPro
FunctionCell wall formation
Structure 
MW34245 Da
313 aa (1-28 signal pept.)

Tail-specific protease Prc/Tsp (tsp )
Peptidase familyS41 InterPro
FunctionDegrades proteins containing a 11 residue C-term. ssrA degradation tag
Structure1 PDZ domain
MW76663 Da
682 aa (1-22 signal pept.)


Protease III (ptrA )
Peptidase familyM16 InterPro
FunctionEndopeptidase, may have preference for small peptides
Structure 
MW107708 Da
962 aa (1-23 signal pept.)


Protease I (tesA )
Peptidase familyLipase InterPro
FunctionHydrolyzes only long chain acyl thioesters (C12-C18), similar to chymotrypsin
Structure PDB
MW23622 Da
208 aa (1-26 signal pept.)


UmuD (umuD )
Peptidase familyS24 InterPro
Function 
Structure PDB
MW15063 Da
139 aa (1-24 signal pept.)


Putative Cys protease YafL (yafL )
Peptidase familyC40
Function 
Structurepotential lipoprotein
MW28785 Da
249 aa (1-17 signal pept.)

Putative protease YdcP (ydcP )
Peptidase familyU32 InterPro
Function 
Structure 
MW72701 Da
653 aa (1-20 signal pept.)


Putative protease YdgD (ydgD )
Peptidase familyS2B InterPro
Function 
Structure 
MW29277 Da
273 aa (1-21 signal pept.)


Putative Cys protease YdhO (ydhO )
Peptidase familyC40
Function 
Structure 
MW29916 Da
271 aa (1-27 signal pept.)

Hypothetical protein YebA (yebA )
Peptidase familyM37 InterPro
Function 
Structure 
MW49057 Da
440 aa (1-34 signal pept.)


Putative protease YhbU (yhbU )
Peptidase familyU32 InterPro
Function 
Structure 
MW37047 Da
331 aa (1-15 signal pept.)


Protein YhjJ (yhjJ )
Peptidase familyM16 InterPro
Function 
Structure 
MW55527 Da
498 aa (1-24 signal pept.)




Outer membrane

Lipoprotein NlpD (nlpD )
Peptidase familyM37 InterPro
Function 
Structure 
MW40149 Da
379 aa (1-25 Signal peptide)

OmpT/ProteaseVII (ompT )
Peptidase familyS18 InterPro
FunctionThe 3D structure questions that OmpT is a ser protease.
StructurePDB
MW35562 Da
317 aa (1-20 Signal peptide)