E. coli Proteases

E. coli Proteases

The E. coli K12 genome encodes at least 74 peptidases/proteases.

Proteases were classified according to their celluar localisation.
View all proteases.

View lists of

Note that some proteases have not yet been classified. Several proteases are not seperately listed because there are only few family members. Also, proteases encoded on plasmids, phages or by pathogenic E. coli are not included in these lists.

All Proteases of E. coli

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 UniProt file.

The topology for each cytoplasmic membrane protein is predicted. Protein sequences are presented in lower case and the TMs in upper case.

Proteases localised in the

Cytoplasm
Cytoplasmic membrane
Periplasm
Outer membrane

Cytoplasm

Aminobenzoyl-glutamate utilization protein A (abgA)

Peptidase family M40 InterPro

Function

Structure

MW 46588 Da
436 aa
Leucine aminopeptidase LAP (ampA)

Peptidase family M17 InterPro

Function

Structure

MW 54879 Da
503 aa
Methionine aminopeptidase (ampM)

Peptidase family M24A InterPro

Function Removes the N-terminal methionine from nascent proteins

Structure PDB

MW 29331 Da
264 aa
Xaa-Pro aminopeptidase/AmpP (pepP)

Peptidase family M24B InterPro

Function Releases any N-terminal amino acid preceding proline, even from short peptides

Structure PDB

MW 49684 Da
440 aa

ATP-dependent Clp protease proteolytic subunit (clpP)

Peptidase family	S14 InterPro
Function	Heat shock protein, chymotrypsin-like activity, major role in the degradation of misfolded proteins, interacts with chaperone subunits ClpA and X
Structure	PDB
MW	23186 Da 207 aa

Dipeptidyl carboxypeptidase (dcp)

Peptidase family	M3
Function	Removes 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
MW	77384 Da 680 aa

D-alanyl-D-alanine dipeptidase (ddpX/vanX)

Peptidase family M45 InterPro

Function Hydrolyses Ala-Ala

Structure

MW 21213 Da
4002 aa
ElaD protein (elaD)

Peptidase family SUMO/Ulp1_C InterPro

Function Cys protease?

Structure

MW 45947 Da
402 aa
Putative frv operon protein FrvX (frvX)

Peptidase family M42/Glutamyl aminopeptidase (Lactococcus)

Function Unclear, homologous to SgcX of ECOLI

Structure

MW 38733 Da
356 aa
Gcp Glycoprotease (gcp/b3064)

Peptidase family M22 InterPro

Function

Structure

MW 36024 Da
356 aa
Heat shock protein HslV (hslV)

Peptidase family T1B InterPro

Function Thr-Protease subunit of HslUV complex, interacts with chaperone subunit HslU

Structure PDB

MW 18961 Da
175 aa

Heat shock protein 31 (hchA / b1967)

Peptidase family	Cys protease? InterPro
Function	Crystal structure reveals a His Asp Cys catalytic triad. Hsp31 was previously characterised as a chaperone.
Structure	PDB
MW	31059 Da 282 aa

Hydrogenase 1 maturation protease (hyaD)

Peptidase family M52 InterPro

Function Involved in maturation (C-terminal processing) of HyaB, the subunit of hydrogenase 1

Structure

MW 21546 Da
195 aa
Hydrogenase 2 maturation protease (hybD)

Peptidase family M52 InterPro

Function Involved in maturation (C-terminal processing) of HybB, the subunit of hydrogenase 2

Structure PDB

MW 17751 Da
164 aa
Formate hydrogenlyase maturation protein HycH (hycH)

Peptidase family

Function Involved in maturation of the large subunit of hydrogenlyase HycE

Structure

MW 15465 Da
136 aa
Hydrogenase 3 maturation protease (hycI)

Peptidase family M52 InterPro

Function Involved in maturation of the large subunit of hydrogenlyase HycE

Structure

MW 16925 Da
155 aa
Isoaspartyl dipeptidase IadA (iadA)

Peptidase family M38

Function Hydrolyses l-isoaspartyl (l-beta-aspartyl) dipeptides, to degrade proteins damaged by l-isoaspartyl residue formation

Structure PDB

MW 41084 Da
390 aa
Muramoyltetrapeptide carboxypeptidase (LdcA)

Peptidase family unknown

Function Converts cytosolic UDP-MurNac-Tetrapeptides to Tripeptides, essential for viability during stationary phase

Structure

MW 33567 Da
304 aa
Lon protease homolog (ycbZ)

Peptidase family s16

Function Lacks ATP ase domain of Lon

Structure

MW 65818 Da
586 aa
Protease Lon (lon)

Peptidase family s16 InterPro

Function Heat shock protein, ATP-dependent Ser protease, broad substrate specificity

Structure PDB

MW 87438 Da
784 aa
Aminoacyl-histidine dipeptidase/Peptidase D (pepD)

Peptidase family M25 InterPro

Function Xaa-His dipeptidase, has specificity for the unusual dipeptide beta-alanyl-l-histidine

Structure

MW 52784 Da
484 aa
Alpha-aspartyl dipeptidase /Peptidase E (pepE)

Peptidase family serine (according to MEROPS)

Function Hydrolyses dipeptides containing n-terminal aspartate residues

Structure

MW 24570 Da
229 aa
X-Pro dipeptidase/Peptidase Q (pepQ)

Peptidase family M24B InterPro

Function Hydrolysis of Xaa-|-Pro dipeptides, but not on Pro-|-Pro

Structure

MW 50176 Da
443 aa
Aminotripeptidase/Peptidase T (pepT)

Peptidase family M20A InterPro

Function Hydrolyzes a tripeptides containing n-terminal Met, Leu, or Phe

Structure PDB

MW 44923 Da
408 aa
Hypothetical protease PmbA (pmbA or tldE or b4235)

Peptidase family unknown

Function required for the production of the antibiotic peptide MccB17

Structure

MW 48369 Da
450 aa
Probable zinc protease PqqL (pqqL/b1494)

Peptidase family M16 InterPro

Function

Structure

MW 104656 Da
931 aa
Oligopeptidase A (prlC)

Peptidase family M3 InterPro

Function

Structure

MW 77167 Da
680 aa
Protease II (ptrB)

Peptidase family s9A InterPro

Function Cleaves after Lys and Arg residues

Structure

MW 79490 Da
686 aa
SprT Protein (sprT)

Peptidase family Zn MTpeptdse InterPro

Function

Structure

MW 19348 Da
165 aa
Hypothetical protease TldD (tldD or b3244)

Peptidase family unknown

Function

Structure

MW 51364 Da
481 aa
Putative metalloprotease YcaL (ycaL)

Peptidase family M48 InterPro

Function Homolog of YggG of E. coli

Structure

MW 26740 Da
254 aa
Hypothetical protease YeaZ (yeaZ)

Peptidase family M22 InterPro

Function

Structure

MW 25181 Da
231 aa
Putative protease YegQ (yegQ)

Peptidase family U32 InterPro

Function

Structure

MW 51193 Da
453 aa
Hypothetical protein YgeY (ygeY)

Peptidase family M20A InterPro

Function

Structure

MW 44804 Da
403 aa
Putative metalloprotease YggG (yggG)

Peptidase family M48 InterPro

Function Homolog of YcaL of E. coli

Structure

MW 26842 Da
252 aa
Putative Cys protease YhbO (yhbO)

Peptidase family c40

Function

Structure

MW 18858 Da
172 aa
Hypothetical protein YibP (yibG)

Peptidase family M37 InterPro

Function

Structure

MW 46594 Da
419 aa
Hypothetical protein YpdF (ypdF)

Peptidase family M24 InterPro

Function

Structure

MW 39624 Da
361 aa

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Cytoplasmic membrane

Protease DegS (degS)

Peptidase family	S2C InterPro
Function	Essential serine protease, Cleaves RseA to induce sigma E cascade
Structure	PDB 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
MW	37581 Da 355 aa

FtsH (ftsH/hflB)

Peptidase family	M41/AAA Protease InterPro
Function	essential 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
MW	70708 Da 644 aa

GlpG (glpG)

Peptidase family	s54 InterPro
Function
Structure	transmembrane 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 kfsgpWFGG SGVVYALMGY VWLrgerdpq sgIYLQRGLI IFALIWIVAG WFdlfGMSMA NGAHIAGLAV GLAMAFVdsl narkrk
MW	31307 Da 276 aa

Heat shock protein HtpX (htpX)

Peptidase family	M48 InterPro
Function
Structure	transmembrane 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
MW	31923 Da 293 aa

Leader peptidase Lep4/Prepilin-like protein (hofD/hopD)

Peptidase family	A24 InterPro
Function	Leader peptidase, cleaves type-4 fimbrial leader sequence
Structure	transmembrane 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
MW	24957 Da 225 aa

Leader peptidase I (LepB)

Peptidase family	s26 InterPro
Function	General leader peptidase
Structure	PDB 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
MW	35960 Da 324 aa

Lipoprotein signa l peptidase (lspA)

Peptidase family	A8 InterPro
Function	Leader peptidase, removes signal peptides from lipoproteins
Structure	transmemebrane 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
MW	18156 Da 164 aa

Leader peptidase PppA (pppA)

Peptidase family	A24 InterPro
Function	Leader peptidase, removes signal peptides from lipoproteins
Structure	transmemebrane 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
MW	29466 Da 269 aa

Possible Ser protease SohB (sohB)

Peptidase family	s49 InterPro
Function	Suppressor of degP(htrA) null mutation
Structure	transmembrane 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
MW	39366 Da 349 aa

Signal peptide peptidase/Protease IV (sppA)

Peptidase family	s49 InterPro
Function	Degrades cleaved signal peptides
Structure	transmembrane 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
MW	67233 Da 618 aa

rseP (YaeL)

Peptidase family	M50B
Function	RIP protease, degrades the antisigma factor RseA
Structure	transmembrane 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
MW	49071 Da 450 aa

YfbL (yfbL)

Peptidase family	M28A
Function
Structure	transmembrane 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
MW	35931 Da 323 aa

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Periplasm

PBP-5, D-alanyl-D-alanine carboxypeptidase fraction A (dacA)

Peptidase family s11

Function Cell wall formation

Structure PDB

MW 44444 Da
403 aa (1-29 signal pept.)
PBP-4, D-alanyl-D-alanine carboxypeptidase (dacB)

Peptidase family s13

Function RIP protease, degrades the antisigma factor RseA

Structure

MW 51798 Da
477 aa (1-20 signal pept.)
PBP-6, D-alanyl-D-alanine carboxypeptidase fraction C (dacC)

Peptidase family s11

Function Cell wall formation

Structure

MW 43609 Da
400 aa (1-27 signal pept.)
PBP-6B, D-alanyl-D-alanine carboxypeptidase (dacD )

Peptidase family s11

Function Cell wall formation

Structure

MW 43346 Da
388 aa (1-21 signal pept.)

Protease Do (degP/htrA)

Peptidase family	S2C
Function	Heat shock protein, serine protease and chaperone ectivities, required at high temperature, virulence factor, involved in refolding and degradation of damaged proteins
Structure	PDB
MW	49439 Da 474 aa (1-26 signal pept.)

Protease DegQ (degQ)

Peptidase family s2c

Function Serine protease

Structure 2 PDZ domains

MW 47205 Da
455 aa (1-27 signal pept.)
Alkaline phosphatase isozyme conversion protein IAP (iap or b2753)

Peptidase family M28C

Function

Structure

MW 37920 Da
345 aa (1-24 signal pept.)
Penicillin-insensitive D-alanyl-D-alanine-endopeptidase (mepA)

Peptidase family Unknown

Function Cell wall formation

Structure

MW 30136 Da
274 aa (1-19 signal pept.)
Putative Cys protease NlpC (nlpC)

Peptidase family Unknown

Function

Structure potential lipoprotein

MW 17283 Da
154 aa (1-15 signal pept.)
PBP-7, D-alanyl-D-alanine-endopeptidase (pbpG or b2134)

Peptidase family Unknown

Function Cell wall formation

Structure

MW 34245 Da
313 aa (1-28 signal pept.)
Tail-specific protease Prc/Tsp (tsp)

Peptidase family s41

Function Degrades proteins containing a 11 residue C-term. ssrA degradation tag

Structure 1 PDZ domain

MW 76663 Da
682 aa (1-22 signal pept.)
Protease III (ptrA)

Peptidase family M16

Function Endopeptidase, may have preference for small peptides

Structure

MW 107708 Da
962 aa (1-23 signal pept.)
Protease I (tesA)

Peptidase family Lipase

Function Hydrolyzes only long chain acyl thioesters (C12-C18), similar to chymotrypsin

Structure PDB

MW 23622 Da
208 aa (1-26 signal pept.)
UmuD (umuD)

Peptidase family S24

Function

Structure PDB

MW 15063 Da
139 aa (1-24 signal pept.)
Putative Cys protease YafL (yafL)

Peptidase family C40

Function

Structure potential lipoprotein

MW 28785 Da
249 aa (1-17 signal pept.)
Putative protease YdcP (ydcP)

Peptidase family U32

Function

Structure

MW 72701 Da
653 aa (1-20 signal pept.)
Putative protease YdgD (ydgD)

Peptidase family S2B

Function

Structure

MW 29277 Da
273 aa (1-21 signal pept.)
Putative Cys protease YdhO (ydhO)

Peptidase family C40

Function

Structure

MW 29916 Da
271 aa (1-27 signal pept.)
Hypothetical protein YebA (yebA)

Peptidase family M37

Function

Structure

MW 49057 Da
440 aa (1-34 signal pept.)
Putative protease YhbU (yhbU)

Peptidase family U32

Function

Structure

MW 37047 Da
331 aa (1-15 signal pept.)
Protein YhjJ (yhjJ)

Peptidase family M16

Function

Structure

MW 55527 Da
498 aa (1-24 signal pept.)

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Outer membrane

Lipoprotein NlpD (nlpD)

Peptidase family M37

Function

Structure

MW 40149 Da
379 aa (1-25 signal pept.)
OmpT/ProteaseVII (ompT)

Peptidase family S18

Function The 3D structure questions that OmpT is a ser protease.

Structure PDB

MW 35562 Da
317 aa (1-20 signal pept.)

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Peptidase family	M40 InterPro
Function
Structure
MW	46588 Da 436 aa

Peptidase family	M17 InterPro
Function
Structure
MW	54879 Da 503 aa

Peptidase family	M24A InterPro
Function	Removes the N-terminal methionine from nascent proteins
Structure	PDB
MW	29331 Da 264 aa

Peptidase family	M24B InterPro
Function	Releases any N-terminal amino acid preceding proline, even from short peptides
Structure	PDB
MW	49684 Da 440 aa

Peptidase family	M45 InterPro
Function	Hydrolyses Ala-Ala
Structure
MW	21213 Da 4002 aa

Peptidase family	SUMO/Ulp1_C InterPro
Function	Cys protease?
Structure
MW	45947 Da 402 aa

Peptidase family	M42/Glutamyl aminopeptidase (Lactococcus)
Function	Unclear, homologous to SgcX of ECOLI
Structure
MW	38733 Da 356 aa

Peptidase family	M22 InterPro
Function
Structure
MW	36024 Da 356 aa

Peptidase family	T1B InterPro
Function	Thr-Protease subunit of HslUV complex, interacts with chaperone subunit HslU
Structure	PDB
MW	18961 Da 175 aa

Peptidase family	M52 InterPro
Function	Involved in maturation (C-terminal processing) of HyaB, the subunit of hydrogenase 1
Structure
MW	21546 Da 195 aa

Peptidase family	M38
Function	Hydrolyses l-isoaspartyl (l-beta-aspartyl) dipeptides, to degrade proteins damaged by l-isoaspartyl residue formation
Structure	PDB
MW	41084 Da 390 aa

Peptidase family	unknown
Function	Converts cytosolic UDP-MurNac-Tetrapeptides to Tripeptides, essential for viability during stationary phase
Structure
MW	33567 Da 304 aa

Peptidase family	s16
Function	Lacks ATP ase domain of Lon
Structure
MW	65818 Da 586 aa

Peptidase family	M25 InterPro
Function	Xaa-His dipeptidase, has specificity for the unusual dipeptide beta-alanyl-l-histidine
Structure
MW	52784 Da 484 aa

Peptidase family
Function	Involved in maturation of the large subunit of hydrogenlyase HycE
Structure
MW	15465 Da 136 aa

Peptidase family	s16 InterPro
Function	Heat shock protein, ATP-dependent Ser protease, broad substrate specificity
Structure	PDB
MW	87438 Da 784 aa

Peptidase family	serine (according to MEROPS)
Function	Hydrolyses dipeptides containing n-terminal aspartate residues
Structure
MW	24570 Da 229 aa

Peptidase family	M20A InterPro
Function	Hydrolyzes a tripeptides containing n-terminal Met, Leu, or Phe
Structure	PDB
MW	44923 Da 408 aa

Peptidase family	M16 InterPro
Function
Structure
MW	104656 Da 931 aa

Peptidase family	M3 InterPro
Function
Structure
MW	77167 Da 680 aa

Peptidase family	s9A InterPro
Function	Cleaves after Lys and Arg residues
Structure
MW	79490 Da 686 aa

Peptidase family	Zn MTpeptdse InterPro
Function
Structure
MW	19348 Da 165 aa

Peptidase family	U32 InterPro
Function
Structure
MW	51193 Da 453 aa

Peptidase family	M37 InterPro
Function
Structure
MW	46594 Da 419 aa

Peptidase family	M24 InterPro
Function
Structure
MW	39624 Da 361 aa

Peptidase family	s11
Function	Cell wall formation
Structure	PDB
MW	44444 Da 403 aa (1-29 signal pept.)

Peptidase family	s2c
Function	Serine protease
Structure	2 PDZ domains
MW	47205 Da 455 aa (1-27 signal pept.)

Peptidase family	M28C
Function
Structure
MW	37920 Da 345 aa (1-24 signal pept.)

Peptidase family	s41
Function	Degrades proteins containing a 11 residue C-term. ssrA degradation tag
Structure	1 PDZ domain
MW	76663 Da 682 aa (1-22 signal pept.)

Peptidase family	M16
Function	Endopeptidase, may have preference for small peptides
Structure
MW	107708 Da 962 aa (1-23 signal pept.)

Peptidase family	Lipase
Function	Hydrolyzes only long chain acyl thioesters (C12-C18), similar to chymotrypsin
Structure	PDB
MW	23622 Da 208 aa (1-26 signal pept.)

Peptidase family	S18
Function	The 3D structure questions that OmpT is a ser protease.
Structure	PDB
MW	35562 Da 317 aa (1-20 signal pept.)