periplasmic protease YcaL [Escherichia coli str. K-12 substr. MG1655]
Protein Classification
M48 family metallopeptidase( domain architecture ID 11574521)
M48 family metallopeptidase is an integral membrane protein that proteolytically removes the C-terminal three residues of farnesylated proteins; contains a zinc-binding motif, HEXXH
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| M48C_loiP_like | cd07334 | Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase ... |
34-249 | 4.07e-111 | ||||
Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase M48 Ste24p protease loiP (formerly yggG)-like family are mostly uncharacterized proteins that include E. coli loiP and ycaLG, considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. LoiP has been shown to be a metallopeptidase that cleaves its targets preferentially between Phe-Phe residues. It is upregulated when bacteria are subjected to media of low osmolarity, thus yggG was named LoiP (low osmolarity induced protease). Proper membrane localization of LoiP may depend on YfgC, another putative metalloprotease in this subfamily. : Pssm-ID: 320693 [Multi-domain] Cd Length: 215 Bit Score: 318.37 E-value: 4.07e-111
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| Name | Accession | Description | Interval | E-value | |||||
| M48C_loiP_like | cd07334 | Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase ... |
34-249 | 4.07e-111 | |||||
Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase M48 Ste24p protease loiP (formerly yggG)-like family are mostly uncharacterized proteins that include E. coli loiP and ycaLG, considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. LoiP has been shown to be a metallopeptidase that cleaves its targets preferentially between Phe-Phe residues. It is upregulated when bacteria are subjected to media of low osmolarity, thus yggG was named LoiP (low osmolarity induced protease). Proper membrane localization of LoiP may depend on YfgC, another putative metalloprotease in this subfamily. Pssm-ID: 320693 [Multi-domain] Cd Length: 215 Bit Score: 318.37 E-value: 4.07e-111
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| Peptidase_M48 | pfam01435 | Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ... |
74-250 | 8.62e-25 | |||||
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX prenyl protease homologs such as Human FACE-1 protease. These are metallopeptidases, with the characteriztic HExxH motif giving the two histidine-zinc-ligands and an adjacent glutamate on the next helix being the third. The whole molecule folds to form a deep groove/cleft into which the substrate can fit. Pssm-ID: 426263 [Multi-domain] Cd Length: 201 Bit Score: 97.50 E-value: 8.62e-25
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| COG4784 | COG4784 | Putative Zn-dependent protease [General function prediction only]; |
7-244 | 7.66e-19 | |||||
Putative Zn-dependent protease [General function prediction only]; Pssm-ID: 443814 [Multi-domain] Cd Length: 488 Bit Score: 84.94 E-value: 7.66e-19
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| PRK05457 | PRK05457 | protease HtpX; |
97-242 | 4.25e-08 | |||||
protease HtpX; Pssm-ID: 235478 [Multi-domain] Cd Length: 284 Bit Score: 52.87 E-value: 4.25e-08
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| Name | Accession | Description | Interval | E-value | |||||
| M48C_loiP_like | cd07334 | Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase ... |
34-249 | 4.07e-111 | |||||
Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase M48 Ste24p protease loiP (formerly yggG)-like family are mostly uncharacterized proteins that include E. coli loiP and ycaLG, considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. LoiP has been shown to be a metallopeptidase that cleaves its targets preferentially between Phe-Phe residues. It is upregulated when bacteria are subjected to media of low osmolarity, thus yggG was named LoiP (low osmolarity induced protease). Proper membrane localization of LoiP may depend on YfgC, another putative metalloprotease in this subfamily. Pssm-ID: 320693 [Multi-domain] Cd Length: 215 Bit Score: 318.37 E-value: 4.07e-111
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| M48C_Oma1_like | cd07332 | Peptidase M48C Ste24p, integral membrane endopeptidase; This subfamily contains peptidase M48C ... |
41-248 | 1.37e-36 | |||||
Peptidase M48C Ste24p, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer. Pssm-ID: 320691 [Multi-domain] Cd Length: 222 Bit Score: 128.84 E-value: 1.37e-36
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| M48C_Oma1-like | cd07324 | Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 ... |
76-248 | 1.70e-31 | |||||
Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 subfamily C (also known as Oma1 peptidase or mitochondrial metalloendopeptidase OMA1), including similar peptidases containing tetratricopeptide (TPR) repeats, as well as uncharacterized proteins such as E. coli bepA (formerly yfgC), ycaL and loiP (formerly yggG), considered to be putative metallopeptidases. Oma1 peptidase is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Homologs of Oma1 are present in higher eukaryotes, eubacteria and archaebacteria, suggesting that Oma1 is the founding member of a conserved family of membrane-embedded metallopeptidases, all containing the zinc metalloprotease motif (HEXXH). M48 peptidases proteolytically remove the C-terminal three residues of farnesylated proteins. Pssm-ID: 320683 [Multi-domain] Cd Length: 142 Bit Score: 113.04 E-value: 1.70e-31
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| M48C_bepA_like | cd07333 | Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase ... |
74-252 | 5.27e-27 | |||||
Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase M48C Ste24p protease bepA (formerly yfgC)-like proteins considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Several members of this family also contain tetratricopeptide (TPR) repeat motifs, which are involved in a variety of functions including protein-protein interactions. BepA has been shown to possess protease activity and is responsible for the degradation of incorrectly folded LptD, an essential outer-membrane protein (OMP) involved in OM transport and assembly of lipopolysaccharide. Overexpression of the bepA protease causes abnormal biofilm architecture. Pssm-ID: 320692 [Multi-domain] Cd Length: 174 Bit Score: 102.57 E-value: 5.27e-27
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| Peptidase_M48 | pfam01435 | Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ... |
74-250 | 8.62e-25 | |||||
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX prenyl protease homologs such as Human FACE-1 protease. These are metallopeptidases, with the characteriztic HExxH motif giving the two histidine-zinc-ligands and an adjacent glutamate on the next helix being the third. The whole molecule folds to form a deep groove/cleft into which the substrate can fit. Pssm-ID: 426263 [Multi-domain] Cd Length: 201 Bit Score: 97.50 E-value: 8.62e-25
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| M48C_Oma1_like | cd07331 | Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ... |
74-251 | 5.22e-23 | |||||
Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer. Pssm-ID: 320690 [Multi-domain] Cd Length: 187 Bit Score: 92.25 E-value: 5.22e-23
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| COG4784 | COG4784 | Putative Zn-dependent protease [General function prediction only]; |
7-244 | 7.66e-19 | |||||
Putative Zn-dependent protease [General function prediction only]; Pssm-ID: 443814 [Multi-domain] Cd Length: 488 Bit Score: 84.94 E-value: 7.66e-19
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| HtpX | COG0501 | Zn-dependent protease with chaperone function [Posttranslational modification, protein ... |
97-254 | 1.15e-16 | |||||
Zn-dependent protease with chaperone function [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440267 [Multi-domain] Cd Length: 210 Bit Score: 76.08 E-value: 1.15e-16
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| M48_Ste24p_like | cd07325 | M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ... |
75-248 | 3.24e-12 | |||||
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 family Ste24p-like proteins that are as yet uncharacterized, but probably function as intracellular, membrane-associated zinc metalloproteases; they all contain the HEXXH Zn-binding motif, which is critical for Ste24p activity. They likely remove the C-terminal three residues of farnesylated proteins proteolytically and are possibly associated with the endoplasmic reticulum and golgi. Some members also contain ankyrin domains which occur in very diverse families of proteins and mediate protein-protein interactions. Pssm-ID: 320684 [Multi-domain] Cd Length: 199 Bit Score: 63.40 E-value: 3.24e-12
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| M48B_HtpX_like | cd07337 | Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ... |
76-247 | 2.07e-11 | |||||
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not. Pssm-ID: 320696 [Multi-domain] Cd Length: 203 Bit Score: 61.56 E-value: 2.07e-11
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| M48C_Oma1_like | cd07342 | M48C peptidase, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ... |
87-243 | 9.70e-11 | |||||
M48C peptidase, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer. Pssm-ID: 320701 [Multi-domain] Cd Length: 158 Bit Score: 58.42 E-value: 9.70e-11
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| M48_Ste24p_like | cd07328 | M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ... |
77-247 | 3.62e-10 | |||||
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains peptidase M48-like proteins that are as yet uncharacterized, but probably function as intracellular, membrane-associated zinc metalloproteases; they all contain the HEXXH Zn-binding motif, which is critical for Ste24p activity. They likely remove the C-terminal three residues of farnesylated proteins proteolytically and are possibly associated with the endoplasmic reticulum and golgi. Pssm-ID: 320687 [Multi-domain] Cd Length: 160 Bit Score: 57.18 E-value: 3.62e-10
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| M48B_HtpX_like | cd07335 | Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This family contains ... |
97-247 | 8.14e-10 | |||||
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, also known as HtpX, which consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX, an integral membrane (IM) metallopeptidase, is widespread in bacteria and archaea, and plays a central role in protein quality control by preventing the accumulation of misfolded proteins in the membrane. Its expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and eliminating them by collaborating with FtsH, a membrane-bound and ATP-dependent protease. HtpX contains the zinc binding motif (HEXXH), has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not. Mutation studies of HtpX-like M48 metalloprotease from Leptospira interrogans (LA4131) has been shown to result in altered expression of a subset of metal toxicity and stress response genes. Pssm-ID: 320694 [Multi-domain] Cd Length: 240 Bit Score: 57.21 E-value: 8.14e-10
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| M48B_HtpX_like | cd07327 | HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, ... |
96-254 | 7.89e-09 | |||||
HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, also known as HtpX, which consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX, an integral membrane (IM) metallopeptidase, is widespread in bacteria and archaea, and plays a central role in protein quality control by preventing the accumulation of misfolded proteins in the membrane. Its expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and eliminating them by collaborating with FtsH, a membrane-bound and ATP-dependent protease. HtpX contains the zinc binding motif (HEXXH), has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not. Mutation studies of HtpX-like M48 metalloprotease from Leptospira interrogans (LA4131) has been shown to result in altered expression of a subset of metal toxicity and stress response genes. Pssm-ID: 320686 [Multi-domain] Cd Length: 183 Bit Score: 53.80 E-value: 7.89e-09
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| M48B_HtpX_like | cd07338 | Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ... |
113-244 | 3.13e-08 | |||||
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not. Pssm-ID: 320697 [Multi-domain] Cd Length: 216 Bit Score: 52.58 E-value: 3.13e-08
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| PRK05457 | PRK05457 | protease HtpX; |
97-242 | 4.25e-08 | |||||
protease HtpX; Pssm-ID: 235478 [Multi-domain] Cd Length: 284 Bit Score: 52.87 E-value: 4.25e-08
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| PRK03001 | PRK03001 | zinc metalloprotease HtpX; |
96-242 | 1.25e-07 | |||||
zinc metalloprotease HtpX; Pssm-ID: 179524 [Multi-domain] Cd Length: 283 Bit Score: 51.56 E-value: 1.25e-07
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| PRK04897 | PRK04897 | heat shock protein HtpX; Provisional |
96-247 | 1.32e-07 | |||||
heat shock protein HtpX; Provisional Pssm-ID: 235318 [Multi-domain] Cd Length: 298 Bit Score: 51.49 E-value: 1.32e-07
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| M48A_Ste24p-like | cd07345 | Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase ... |
119-251 | 1.37e-07 | |||||
Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase family M48 subfamily A-like CaaX prenyl protease 1, most of which are uncharacterized. Some of these contain tetratricopeptide (TPR) repeats at the C-terminus. Proteins in this family contain the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. They are thought to be possibly associated with the endoplasmic reticulum (ER), regardless of whether their genes possess the conventional signal motif (KKXX) in the C-terminal. These proteins putatively remove the C-terminal three residues of farnesylated proteins proteolytically. Pssm-ID: 320704 [Multi-domain] Cd Length: 346 Bit Score: 51.51 E-value: 1.37e-07
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| M48B_HtpX_like | cd07336 | Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ... |
96-247 | 1.53e-07 | |||||
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not. Pssm-ID: 320695 [Multi-domain] Cd Length: 266 Bit Score: 50.95 E-value: 1.53e-07
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| PRK03072 | PRK03072 | heat shock protein HtpX; Provisional |
100-242 | 8.97e-07 | |||||
heat shock protein HtpX; Provisional Pssm-ID: 235102 [Multi-domain] Cd Length: 288 Bit Score: 48.89 E-value: 8.97e-07
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| M48A_Zmpste24p_like | cd07343 | Peptidase M48 subfamily A, a type 1 CaaX endopeptidase; This family contains peptidase family ... |
119-247 | 1.35e-06 | |||||
Peptidase M48 subfamily A, a type 1 CaaX endopeptidase; This family contains peptidase family M48 subfamily A which includes a number of well-characterized genes such as those found in humans (ZMPSTE24, also known as farnesylated protein-converting enzyme 1 or FACE-1 or Hs Ste24), Taenia solium metacestode (TsSte24p), Arabidopsis (AtSte24) and yeast (Ste24p). Ste24p contains the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. It is thought to be intimately associated with the endoplasmic reticulum (ER), regardless of whether its genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. Ste24p is involved in the post-translational processing of prelamin A to mature lamin A, a major component of the nuclear envelope. ZmpSte24 deficiency causes an accumulation of prelamin A leading to lipodystrophy and other disease phenotypes, while mutations in this gene or in that encoding its substrate, prelamin A, result in a series of human inherited diseases known as laminopathies, the most severe of which are Hutchinson Gilford progeria syndrome (HGPS) and restrictive dermopathy (RD) which arise due to unsuccessful maturation of prelamin A. Two forms of mandibuloacral dysplasia, a condition that causes a variety of abnormalities involving bone development, skin pigmentation, and fat distribution, are caused by mutations in two different genes; mutations in the LMNA gene, which normally provides instructions for making lamin A and lamin C, cause mandibuloacral dysplasia with A-type lipodystrophy (MAD-A), and mutations in the ZMPSTE24 gene cause mandibuloacral dysplasia with B-type lipodystrophy (MAD-B). Within cells, these genes are involved in maintaining the structure of the nucleus and may play a role in many cellular processes. Certain HIV protease inhibitors have been shown to inhibit the enzymatic activity of ZMPSTE24, but not enzymes involved in prelamin A processing. Pssm-ID: 320702 [Multi-domain] Cd Length: 405 Bit Score: 48.63 E-value: 1.35e-06
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| M48B_Htpx_like | cd07340 | Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ... |
96-139 | 3.19e-06 | |||||
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not. Pssm-ID: 320699 [Multi-domain] Cd Length: 246 Bit Score: 47.11 E-value: 3.19e-06
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| Peptidase_M48_M56 | cd05843 | Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral ... |
83-163 | 3.65e-06 | |||||
Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral membrane metallopeptidases; This family contains peptidase M48 (also known as Ste24 peptidase, Ste24p, Ste24 endopeptidase, a-factor converting enzyme, AFC1), M56 (also known as BlaR1 peptidase) as well as a novel family called minigluzincins. Peptidase M48 belongs to Ste24 endopeptidase family. Members of this family include Ste24 protease (peptidase M48A), protease htpX homolog (peptidase M48B), or CAAX prenyl protease 1, and mitochondrial metalloendopeptidase OMA1 (peptidase M48C). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. The Ste24p contains multiple membrane spans, a zinc metalloprotease motif (HEXXH), and a COOH-terminal ER retrieval signal (KKXX). Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Ste24p has limited homology to HtpX family of prokaryotic proteins; HtpX proteins, also part of the M48 peptidase family, are smaller and homology is restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins; HtpX then undergoes self-degradation and collaborates with FtsH to eliminate these misfolded proteins. Peptidase M56 includes zinc metalloprotease domain in MecR1 and BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain beta-lactam antibiotics in MRSA. Also included are a novel family of related proteins that consist of the soluble minimal scaffold similar to the catalytic domains of the integral-membrane metallopeptidase M48 and M56, thus called minigluzincins. Pssm-ID: 320682 [Multi-domain] Cd Length: 94 Bit Score: 44.36 E-value: 3.65e-06
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| PRK02391 | PRK02391 | heat shock protein HtpX; Provisional |
99-140 | 1.03e-05 | |||||
heat shock protein HtpX; Provisional Pssm-ID: 179418 [Multi-domain] Cd Length: 296 Bit Score: 45.69 E-value: 1.03e-05
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| M56_like | cd07329 | Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains ... |
100-248 | 1.32e-05 | |||||
Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains peptidase M56, which includes zinc metalloprotease domain in MecR1 as well as BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain beta-lactam antibiotics in MRSA. Both, MecR1 and BlaR1, are transmembrane proteins that consist of four transmembrane helices, a cytoplasmic zinc protease domain, and the soluble C-terminal extracellular sensor domain, and are highly similar in sequence and function. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. All members contain the zinc metalloprotease motif (HEXXH). Homologs of this peptidase domain are also found in a number of other bacterial genome sequences, most of which are as yet uncharacterized. Pssm-ID: 320688 [Multi-domain] Cd Length: 188 Bit Score: 44.75 E-value: 1.32e-05
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| PRK03982 | PRK03982 | heat shock protein HtpX; Provisional |
96-139 | 3.73e-05 | |||||
heat shock protein HtpX; Provisional Pssm-ID: 235186 [Multi-domain] Cd Length: 288 Bit Score: 43.84 E-value: 3.73e-05
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| PRK01265 | PRK01265 | heat shock protein HtpX; Provisional |
83-148 | 3.24e-04 | |||||
heat shock protein HtpX; Provisional Pssm-ID: 234931 [Multi-domain] Cd Length: 324 Bit Score: 41.27 E-value: 3.24e-04
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| PRK02870 | PRK02870 | heat shock protein HtpX; Provisional |
98-139 | 3.17e-03 | |||||
heat shock protein HtpX; Provisional Pssm-ID: 235081 [Multi-domain] Cd Length: 336 Bit Score: 38.16 E-value: 3.17e-03
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