E. coli Proteases - Serine Proteases
Proteases of E. coli Serine 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.
Serine proteases localised in the
Cytoplasm
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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
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Lon protease homolog (ycbZ)
Peptidase family s16 Function Lacks ATP ase domain of Lon Structure MW 65818 Da
586 aa
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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
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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
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Protease II (ptrB)
Peptidase family s9A InterPro Function Cleaves after Lys and Arg residues Structure MW 79490 Da
686 aa
Cytoplasmic membrane
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Protease DegS (degS)
Peptidase family S2C InterPro Function Essential serine protease, Cleaves RseA to induce sigma E cascade Structure PDB MW 37581 Da
355 aa
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GlpG (glpG)
Peptidase family s54 InterPro Function Structure transmembrane domains: 6 (potential) MW 31307 Da
276 aa
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Leader peptidase I (LepB)
Peptidase family s26 InterPro Function General leader peptidase Structure PDB
2 TM, periplasmic N-and C-terminiMW 35960 Da
324 aa
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Possible Ser protease SohB (sohB)
Peptidase family s49 InterPro Function Suppressor of degP(htrA) null mutation Structure 1 TM? MW 39366 Da
349 aa
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Signal peptide peptidase/Protease IV (sppA)
Peptidase family s49 InterPro Function Degrades cleaved signal peptides Structure 3 TM? MW 67233 Da
618 aa
Periplasm
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PBP-5, D-alanyl-D-alanine carboxypeptidase fraction A (dacA)
Peptidase family s11 Function Cell wall formation Structure MW 44444 Da
403 aa (1-29 signal pept.)
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PBP-4, D-alanyl-D-alanine carboxypeptidase (dacB)
Peptidase family s13 InterPro Function RIP protease, degrades the antisigma factor RseA Structure MW 51798 Da
477 aa (1-20 signal pept.)
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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.)
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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.)
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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.)
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Protease DegQ (degQ)
Peptidase family s2c Function Serine protease Structure 2 PDZ domains MW 47205 Da
455 aa (1-27 signal pept.)
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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.)
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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.)
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UmuD (umuD)
Peptidase family S24 Function Structure MW 15063 Da
139 aa (1-24 signal pept.)
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Putative protease YdgD (ydgD)
Peptidase family S2B Function Structure MW 29277 Da
273 aa (1-21 signal pept.)
Outer membrane
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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.)