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Conserved domains on  [gi|2730679916|ref|WP_344800383|]
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M48 family metalloprotease [Litoribacillus peritrichatus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_M48_M56 super family cl28898
Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral ...
 43-252 1.15e-50

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.


The actual alignment was detected with superfamily member cd07333:

Pssm-ID: 333718 [Multi-domain]  Cd Length: 174  Bit Score: 169.98  E-value: 1.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  43 QEYQLGRGWLRALRSQTPILEDPLLNDYLEFTIYRLAENSQLTDRRIETIIVDNKSLNAFAVPGGVIGVNTGLFLYSQSE 122
Cdd:cd07333     1 QEVELGKQFAQQIRQQLPLVEDPEVNEYVNRIGQRLAAVSPRPPFPYRFFVVNDDSINAFATPGGYIYVNTGLILAADNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 123 GEFSSVLSHELAHISQRHFARRVQDaqkrqpltlagllatvllavttggtaaiaagstayaanaqaslAFSRDMEQEADR 202
Cdd:cd07333    81 AELAGVLAHEIGHVVARHIAKQIEK-------------------------------------------SYSREDEREADQ 117

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2730679916 203 IGMETLYNSGYNPNEMTDMFRNMNDAKRYFGTNPPEYLLTHPLTESRVSD 252
Cdd:cd07333   118 LGLQYLTKAGYDPRGMVSFFKKLRRKEWFGGSSIPTYLSTHPAPAERIAY 167
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 294-437 2.25e-12

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 67.45  E-value: 2.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 294 YESAVQESKGTSKhtAQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPE 373
Cdd:COG2956    99 LEKLLELDPDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPD 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2730679916 374 NYVITMYLANTLGKNGKARESAFLLQDMSFKRPDDAHVWNRLAEAQRinnnQIGYYKAAAEYYQ 437
Cdd:COG2956   177 CARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYE----KLGDPEEALELLR 236
 
Name Accession Description Interval E-value
M48C_bepA_like cd07333
Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase ...
 43-252 1.15e-50

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: 169.98  E-value: 1.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  43 QEYQLGRGWLRALRSQTPILEDPLLNDYLEFTIYRLAENSQLTDRRIETIIVDNKSLNAFAVPGGVIGVNTGLFLYSQSE 122
Cdd:cd07333     1 QEVELGKQFAQQIRQQLPLVEDPEVNEYVNRIGQRLAAVSPRPPFPYRFFVVNDDSINAFATPGGYIYVNTGLILAADNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 123 GEFSSVLSHELAHISQRHFARRVQDaqkrqpltlagllatvllavttggtaaiaagstayaanaqaslAFSRDMEQEADR 202
Cdd:cd07333    81 AELAGVLAHEIGHVVARHIAKQIEK-------------------------------------------SYSREDEREADQ 117

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2730679916 203 IGMETLYNSGYNPNEMTDMFRNMNDAKRYFGTNPPEYLLTHPLTESRVSD 252
Cdd:cd07333   118 LGLQYLTKAGYDPRGMVSFFKKLRRKEWFGGSSIPTYLSTHPAPAERIAY 167
COG4784 COG4784
Putative Zn-dependent protease [General function prediction only];
24-274 6.26e-40

Putative Zn-dependent protease [General function prediction only];


Pssm-ID: 443814 [Multi-domain]  Cd Length: 488  Bit Score: 150.04  E-value: 6.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  24 AAAQLPTLGDSTSGFISLDQEYQLGRgwlRA----LRSQTPILEDPLLNDYLEFTIYRLAENSQLTDRRIETIIVDNKSL 99
Cdd:COG4784    23 GCATNPVTGKRDLVLMSEEQEIAIGA---EEhpriLAQYGGAYDDPKLQAYVARVGQRLAAASHRPDLPYTFTVLDSPVV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 100 NAFAVPGGVIGVNTGLFLYSQSEGEFSSVLSHELAHISQRHFARRvqdaQKRQplTLAGLLATVLLAVTTGGTAAIAAGS 179
Cdd:COG4784   100 NAFALPGGYVYVTRGLLALANDEAELAAVLGHEIGHVTARHAVQR----QSRA--TAAQIGLGRVLSPVLGSAQAGQLAG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 180 TAyaanAQASLA-FSRDMEQEADRIGMETLYNSGYNPNEMTDMFRNMND----AKRYFGTNP----PEYLLTHPLTESRV 250
Cdd:COG4784   174 AG----AQLLLAsFSRDQELEADRLGVRYLARAGYDPYAMARFLGSLKRqsafRARLAGREGrrsyPDFLSTHPDTPDRV 249

                         250       260
                  ....*....|....*....|....
gi 2730679916 251 SDSANRASQYPAVKNGRTNFEYQL 274
Cdd:COG4784   250 QRAVAAARQLGAPGQGERDRDAYL 273
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 65-251 5.66e-28

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: 110.21  E-value: 5.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  65 PLLNDYLEFTIYRLAENSQLTDRRIE-TIIVDNKSLNAFAV---PGGVIGVNTGLFLYSQSEGEFSSVLSHELAHISQRH 140
Cdd:pfam01435   1 PLRNAELQRVVERLAAAAGLPLPPWYvVVIKSSPVPNAFAYgllPGGRVVVTTGLLDLLETEDELAAVLGHEIGHIKARH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 141 FARRVQDAQKRQPLTLAGLLAtVLLAVTTGGTAA--IAAGSTAYAANA--QASLAFSRDMEQEADRIGMETLYNSGYNPN 216
Cdd:pfam01435  81 SVESLSIMGGLSLAQLFLALL-LLGAAASGFANFgiIFLLLIGPLAALltLLLLPYSRAQEYEADRLGAELMARAGYDPR 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2730679916 217 EMTDMFRNM-NDAKRYFGTNPPEYLLTHPLTESRVS 251
Cdd:pfam01435 160 ALIKLWGEIdNNGRASDGALYPELLSTHPSLVERIA 195
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 294-437 2.25e-12

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 67.45  E-value: 2.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 294 YESAVQESKGTSKhtAQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPE 373
Cdd:COG2956    99 LEKLLELDPDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPD 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2730679916 374 NYVITMYLANTLGKNGKARESAFLLQDMSFKRPDDAHVWNRLAEAQRinnnQIGYYKAAAEYYQ 437
Cdd:COG2956   177 CARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYE----KLGDPEEALELLR 236
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 309-455 7.37e-09

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 58.17  E-value: 7.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 309 AQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTlgkn 388
Cdd:TIGR02917 433 ADLLLILSYLRSGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDFFPAAANLARI---- 508

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2730679916 389 gkaresafllqDMSFKRPDDAHvwNRLAEAQRINNNQIGYYKAAAEYYQLNGDFTNSQRQLMRALKL 455
Cdd:TIGR02917 509 -----------DIQEGNPDDAI--QRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLEKAAEL 562
PRK01345 PRK01345
heat shock protein HtpX; Provisional
 75-206 1.01e-04

heat shock protein HtpX; Provisional


Pssm-ID: 234944 [Multi-domain]  Cd Length: 317  Bit Score: 44.24  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  75 IYRLAENSQLTDRRIetIIVDNKSLNAFAV---P-GGVIGVNTGLfLYSQSEGEFSSVLSHELAHIsqrhfarrvqdaQK 150
Cdd:PRK01345   73 VRDLARRAGLPMPKV--YIIDNPQPNAFATgrnPeNAAVAATTGL-LQRLSPEEVAGVMAHELAHV------------KN 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2730679916 151 RQPLTLAgLLATVLLAVT-------------------TGGTAAIAAGSTAYAANAQASLAFSRDMEQEADRIGME 206
Cdd:PRK01345  138 RDTLTMT-ITATLAGAISmlanfafffggnrennngpLGLVGTLAAMIVAPLAAMLVQMAISRTREYAADRRGAE 211
TPR_19 pfam14559
Tetratricopeptide repeat;
356-416 1.05e-04

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 40.26  E-value: 1.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2730679916 356 DLDEAESILKKMLKDNPENYVITMYLANTLGKNGKARESAFLLQDMSFKRPDDAHVWNRLA 416
Cdd:pfam14559   3 DYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLA 63
 
Name Accession Description Interval E-value
M48C_bepA_like cd07333
Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase ...
 43-252 1.15e-50

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: 169.98  E-value: 1.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  43 QEYQLGRGWLRALRSQTPILEDPLLNDYLEFTIYRLAENSQLTDRRIETIIVDNKSLNAFAVPGGVIGVNTGLFLYSQSE 122
Cdd:cd07333     1 QEVELGKQFAQQIRQQLPLVEDPEVNEYVNRIGQRLAAVSPRPPFPYRFFVVNDDSINAFATPGGYIYVNTGLILAADNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 123 GEFSSVLSHELAHISQRHFARRVQDaqkrqpltlagllatvllavttggtaaiaagstayaanaqaslAFSRDMEQEADR 202
Cdd:cd07333    81 AELAGVLAHEIGHVVARHIAKQIEK-------------------------------------------SYSREDEREADQ 117

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2730679916 203 IGMETLYNSGYNPNEMTDMFRNMNDAKRYFGTNPPEYLLTHPLTESRVSD 252
Cdd:cd07333   118 LGLQYLTKAGYDPRGMVSFFKKLRRKEWFGGSSIPTYLSTHPAPAERIAY 167
M48C_Oma1-like cd07324
Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 ...
 70-252 3.99e-48

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: 162.35  E-value: 3.99e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  70 YLEFTIYRLAENSQLTDRRIETIIVDNKSLNAFAVPGGVIGVNTGLFLYSQSEGEFSSVLSHELAHISQRHFARRVQdaq 149
Cdd:cd07324     1 YLNRLGDRLAAASGRPDLPYRFFVVDDPSINAFALPGGYIFVTTGLLLLLESEDELAAVLAHEIGHVTLRHIARQLE--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 150 krqpltlagllatvllavttggtaaiaagstayaanaqaslAFSRDMEQEADRIGMETLYNSGYNPNEMTDMFRNMNDAK 229
Cdd:cd07324    78 -----------------------------------------RYSRDQEREADRLGLQLLARAGYDPRGMARFFERLARQE 116

                         170       180
                  ....*....|....*....|...
gi 2730679916 230 RYFGTNPPEYLLTHPLTESRVSD 252
Cdd:cd07324   117 GLSGSRLPEFLSTHPLTAERIAA 139
COG4784 COG4784
Putative Zn-dependent protease [General function prediction only];
24-274 6.26e-40

Putative Zn-dependent protease [General function prediction only];


Pssm-ID: 443814 [Multi-domain]  Cd Length: 488  Bit Score: 150.04  E-value: 6.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  24 AAAQLPTLGDSTSGFISLDQEYQLGRgwlRA----LRSQTPILEDPLLNDYLEFTIYRLAENSQLTDRRIETIIVDNKSL 99
Cdd:COG4784    23 GCATNPVTGKRDLVLMSEEQEIAIGA---EEhpriLAQYGGAYDDPKLQAYVARVGQRLAAASHRPDLPYTFTVLDSPVV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 100 NAFAVPGGVIGVNTGLFLYSQSEGEFSSVLSHELAHISQRHFARRvqdaQKRQplTLAGLLATVLLAVTTGGTAAIAAGS 179
Cdd:COG4784   100 NAFALPGGYVYVTRGLLALANDEAELAAVLGHEIGHVTARHAVQR----QSRA--TAAQIGLGRVLSPVLGSAQAGQLAG 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 180 TAyaanAQASLA-FSRDMEQEADRIGMETLYNSGYNPNEMTDMFRNMND----AKRYFGTNP----PEYLLTHPLTESRV 250
Cdd:COG4784   174 AG----AQLLLAsFSRDQELEADRLGVRYLARAGYDPYAMARFLGSLKRqsafRARLAGREGrrsyPDFLSTHPDTPDRV 249

                         250       260
                  ....*....|....*....|....
gi 2730679916 251 SDSANRASQYPAVKNGRTNFEYQL 274
Cdd:COG4784   250 QRAVAAARQLGAPGQGERDRDAYL 273
M48C_Oma1_like cd07331
Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 77-252 1.69e-36

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: 133.09  E-value: 1.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  77 RLAENSQLTDRRIETI-----IVDNKSLNAFAVPGGVIGVNTGLFLYSQSEGEFSSVLSHELAHISQRHFARRVQDAQkr 151
Cdd:cd07331     7 RLIAAAGDDPPQSAGWdwevhVIDSPEVNAFVLPGGKIFVFTGLLPVAKNDDELAAVLGHEIAHALARHSAERMSQQK-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 152 qpltLAGLLATVLLAVTTGGTAAIAAGSTAYAANAQASLAFSRDMEQEADRIGMETLYNSGYNPNEMTDMFRNMNDAKRy 231
Cdd:cd07331    85 ----LLQLLLLLLLAALGASLAGLALGLLGLGAQLGLLLPYSRKQELEADRIGLQLMAKAGYDPRAAVTFWEKMAAAEG- 159

                         170       180
                  ....*....|....*....|.
gi 2730679916 232 fGTNPPEYLLTHPLTESRVSD 252
Cdd:cd07331   160 -GGKPPEFLSTHPSSETRIEA 179
M48C_Oma1_like cd07332
Peptidase M48C Ste24p, integral membrane endopeptidase; This subfamily contains peptidase M48C ...
 28-250 1.16e-32

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: 123.84  E-value: 1.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  28 LPTLGDSTSGFISLDQEYQLGRGWLRALRSQTPILEDPL------LNDYLEftiyRLAENSQLTDR-RIEtIIVDNKSLN 100
Cdd:cd07332     5 LPALAELAAPLLPPSVEEKLGEQTLELLDETLLEPSELPaerqaaLQQLFA----RLLAALPLPYPyRLH-FRDSGIGAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 101 AFAVPGGVIGVNTGLFLYSQSEGEFSSVLSHELAHISQRHFARRVqdaqkrqpltLAGLLATVLLAVTTGGTAAIAAGST 180
Cdd:cd07332    80 AFALPGGTIVVTDGLVELAESPEELAAVLAHEIGHVEHRHSLRQL----------IRSSGLSLLVSLLTGDVSGLSDLLA 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 181 AyAANAQASLAFSRDMEQEADRIGMETLYNSGYNPNEMTDMFRNMNDAKRYfGTNPPEYLLTHPLTESRV 250
Cdd:cd07332   150 G-LPALLLSLSYSRDFEREADAFALELLKAAGISPEGLADFFERLEEEHGD-GGSLPEWLSTHPDTEERI 217
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 65-251 5.66e-28

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: 110.21  E-value: 5.66e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  65 PLLNDYLEFTIYRLAENSQLTDRRIE-TIIVDNKSLNAFAV---PGGVIGVNTGLFLYSQSEGEFSSVLSHELAHISQRH 140
Cdd:pfam01435   1 PLRNAELQRVVERLAAAAGLPLPPWYvVVIKSSPVPNAFAYgllPGGRVVVTTGLLDLLETEDELAAVLGHEIGHIKARH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 141 FARRVQDAQKRQPLTLAGLLAtVLLAVTTGGTAA--IAAGSTAYAANA--QASLAFSRDMEQEADRIGMETLYNSGYNPN 216
Cdd:pfam01435  81 SVESLSIMGGLSLAQLFLALL-LLGAAASGFANFgiIFLLLIGPLAALltLLLLPYSRAQEYEADRLGAELMARAGYDPR 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2730679916 217 EMTDMFRNM-NDAKRYFGTNPPEYLLTHPLTESRVS 251
Cdd:pfam01435 160 ALIKLWGEIdNNGRASDGALYPELLSTHPSLVERIA 195
M48C_Oma1_like cd07342
M48C peptidase, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 93-250 2.18e-14

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: 70.75  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  93 IVDNKSLNAFAvPGGVIGVNTGLFLYSQSEGEFSSVLSHELAHISQRHFARrvqdaqKRQPLTLAGLLatvllavttGGT 172
Cdd:cd07342    25 LGNSDGVNAYA-DGRRVQITSGMMDFAQDDDELALVVAHELAHNILGHRDR------LRANGVAGGLL---------DGF 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2730679916 173 AAIAAgstayaanaqaslaFSRDMEQEADRIGMETLYNSGYNPNEMTDMFRNMndAKRYFGTNppEYLLTHPLTESRV 250
Cdd:cd07342    89 GGNAA--------------YSREFEIEADYLGLYLMARAGYDIDGAADFWRRL--GASHPVGI--GRAATHPSTAERF 148
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 294-437 2.25e-12

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 67.45  E-value: 2.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 294 YESAVQESKGTSKhtAQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPE 373
Cdd:COG2956    99 LEKLLELDPDDAE--ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPD 176

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2730679916 374 NYVITMYLANTLGKNGKARESAFLLQDMSFKRPDDAHVWNRLAEAQRinnnQIGYYKAAAEYYQ 437
Cdd:COG2956   177 CARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYE----KLGDPEEALELLR 236
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 309-437 2.65e-11

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 61.36  E-value: 2.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 309 AQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTLGKN 388
Cdd:COG4783     6 ALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKA 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2730679916 389 GKARESAFLLQDMSFKRPDDAHVWNRLAEAQRinnnQIGYYKAAAEYYQ 437
Cdd:COG4783    86 GDYDEALALLEKALKLDPEHPEAYLRLARAYR----ALGRPDEAIAALE 130
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 93-250 1.16e-10

Zn-dependent protease with chaperone function [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 61.05  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  93 IVDNKSLNAFAV----PGGVIGVNTGLF-LYSQSEGEFssVLSHELAHISQRHFARRvqdaqkrqplTLAGLLATVLLAV 167
Cdd:COG0501    24 VMDSPAPNAFATgrgpNNARIVVTDGLLeLLDRDELEA--VLAHELGHIKNGDILLM----------TLASGLLGLIGFL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 168 TT------------GGTAAIAAGSTAYAANAQASLAFSRDMEQEADRIGMETLYN-----------SGYnpNEMTDMFRN 224
Cdd:COG0501    92 ARllplafgrdrdaGLLLGLLLGILAPFLATLIQLALSRKREYEADRAAAELTGDpdalasalrklAGG--NLSIPLRRA 169

                         170       180
                  ....*....|....*....|....*....
gi 2730679916 225 MNDAKRYFGTNPPEY---LLTHPLTESRV 250
Cdd:COG0501   170 FPAQAHAFIINPLKLsslFSTHPPLEERI 198
M48B_HtpX_like cd07337
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 45-250 1.33e-10

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: 60.79  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  45 YQLGRGWLRALRSQTPILEDPLLNDYLEFTIYRLAENSQLTDRRIETIIVDNKSLNAFAVPGGVIGVNTGLfLYSQSEGE 124
Cdd:cd07337    15 ESILRALSGCRIRRGARKPTRRELEEINPELEDKARRLGPDPEKVKLFISDDEYPNAFALGRNTICVTKGL-LDLLDYEE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 125 FSSVLSHELAHISQRHfarrvqdaqkrqplTLAGLLATVLLAVTTGGTAAIAAGSTAYAANAQAslAFSRDMEQEADRIG 204
Cdd:cd07337    94 LKGILAHELGHLSHKD--------------TDYLLLIFVLLLLAAIWTKLGTLLIFVWIRLLVM--FSSRKAEYRADAFA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2730679916 205 metlYNSGYNPNEMT--DMFRNMNDAKRYFgtnppEYLL--THPLTESRV 250
Cdd:cd07337   158 ----VKIGYGEGLRSalDQLREYEDAPKGF-----LAALysTHPPTEKRI 198
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 294-437 2.20e-10

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 61.28  E-value: 2.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 294 YESAVQESKGTSKhtAQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPE 373
Cdd:COG2956    31 LEEALELDPETVE--AHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPD 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2730679916 374 NYVITMYLANTLGKNGKARESAFLLQDMSFKRPDDAHVWNRLAEAQRINNNqigyYKAAAEYYQ 437
Cdd:COG2956   109 DAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGD----YDEAIEALE 168
M48C_loiP_like cd07334
Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase ...
 100-250 3.48e-10

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: 59.91  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 100 NAFAVPGGVIGVNTGLF-LYSQSEGEFssVLSHELAHISQRHfarrVQDAQKRQPLTLAGLLAtvllAVTTGGTAAIAAG 178
Cdd:cd07334    70 NAFAMADGSVRVYSGLMdMMTDDELLG--VIGHEIGHVKLGH----SKKAMKTAYLTSAARKA----AASASGTVGALSD 139

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2730679916 179 ST----AYAA-NAQaslaFSRDMEQEADRIGMETLYNSGYNPNEMTDMFRNMndAKRYFGTNpPEYLLTHPLTESRV 250
Cdd:cd07334   140 SQlgalAEKLiNAQ----FSQKQESEADDYGYKFLKKNGYNPQAAVSALEKL--AALSGGGK-SSLFSSHPDPAKRA 209
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 306-437 5.27e-10

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 60.13  E-value: 5.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 306 KHTAQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTL 385
Cdd:COG2956    75 RAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELY 154

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2730679916 386 GKNGKARESAFLLQDMSFKRPDDAHVWNRLAEAQRINNNqigyYKAAAEYYQ 437
Cdd:COG2956   155 LEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGD----YEEAIAALE 202
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 310-456 2.42e-09

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 58.20  E-value: 2.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 310 QYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTLGKNG 389
Cdd:COG2956    11 WYFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 390 KARESAFLLQDMSFKRPDDAHVWNRLAE-----------------AQRINNNQIGYYKAAAEYYQLNGDFTNSQRQLMRA 452
Cdd:COG2956    91 LLDRAEELLEKLLELDPDDAEALRLLAEiyeqegdwekaievlerLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA 170


                  ....
gi 2730679916 453 LKLA 456
Cdd:COG2956   171 LKLD 174
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 309-455 7.37e-09

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 58.17  E-value: 7.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 309 AQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTlgkn 388
Cdd:TIGR02917 433 ADLLLILSYLRSGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDFFPAAANLARI---- 508

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2730679916 389 gkaresafllqDMSFKRPDDAHvwNRLAEAQRINNNQIGYYKAAAEYYQLNGDFTNSQRQLMRALKL 455
Cdd:TIGR02917 509 -----------DIQEGNPDDAI--QRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLEKAAEL 562
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 309-408 4.30e-08

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 52.12  E-value: 4.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 309 AQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTLGKN 388
Cdd:COG4783    40 AFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRAL 119

                          90       100
                  ....*....|....*....|
gi 2730679916 389 GKARESAFLLQDMSFKRPDD 408
Cdd:COG4783   120 GRPDEAIAALEKALELDPDD 139
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
309-437 2.91e-07

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 51.55  E-value: 2.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 309 AQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTLGKN 388
Cdd:COG0457    10 AYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQAL 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2730679916 389 GKARESAFLLQDMSFKRPDDAHVWNRLAEAQRinnnQIGYYKAAAEYYQ 437
Cdd:COG0457    90 GRYEEALEDYDKALELDPDDAEALYNLGLALL----ELGRYDEAIEAYE 134
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 293-436 1.79e-06

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 50.47  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 293 KYESAVQESKGTSKHTAQY--ALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKD 370
Cdd:TIGR02917 585 KALAILNEAADAAPDSPEAwlMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALEL 664

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2730679916 371 NPENYVITMYLANTLGKNGKARESAFLLQDMSFKRPDDAHVWNRLAEAQRINNNqigyYKAAAEYY 436
Cdd:TIGR02917 665 KPDNTEAQIGLAQLLLAAKRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKD----YPAAIQAY 726
M48_Ste24p_like cd07328
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 87-177 2.56e-06

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: 47.16  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  87 RRIETIIVDNkSLNAFAVPGGVIGVNTGLF------LYSQSEGEFSSVLSHELAHISQRH--FARRVqDAQKRQpltlag 158
Cdd:cd07328    42 PPPDEVVLTA-DVNASVTELGLLLGRRGLLtlglplLAALSPEELRAVLAHELGHFANGDtrLGAWI-LSRRAE------ 113

                          90
                  ....*....|....*....
gi 2730679916 159 LLATvLLAVTTGGTAAIAA 177
Cdd:cd07328   114 YEAD-RVAARVAGSAAAAS 131
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 260-437 4.81e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 49.22  E-value: 4.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 260 YPAVKNGRTNFEYQLMKRRVEVHTLKSADACTNKYESAVQESKGTSKHTAQYALAICYTEDKQFEKALATLKPLQELWPL 339
Cdd:COG3914    31 ELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPD 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 340 SITINVLEAEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTLGKNGKARESAFLLQDMSFKRPDDAHVWNRLAEAQ 419
Cdd:COG3914   111 NAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNAL 190

                         170
                  ....*....|....*...
gi 2730679916 420 RinnnQIGYYKAAAEYYQ 437
Cdd:COG3914   191 Q----DLGRLEEAIAAYR 204
M56_like cd07329
Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains ...
 77-176 7.51e-06

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: 46.68  E-value: 7.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  77 RLAENSQLTDRRIetIIVDNKSLNAFAV---PGGVIGVNTGLF--LysqSEGEFSSVLSHELAHIsqrhfARRvqDAQKR 151
Cdd:cd07329     2 RLARQADVPPPRV--YVVDSDVPNAFAVgrsRGPTVVVTTGLLdlL---DDDELEAVLAHELAHL-----KRR--DVLVL 69

                          90       100
                  ....*....|....*....|....*
gi 2730679916 152 QPLTLAGLLATVLLAVTTGGTAAIA 176
Cdd:cd07329    70 LLFDPLLLLVVGLLLFLSLFIFELL 94
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 309-418 9.10e-06

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 45.00  E-value: 9.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 309 AQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTLGKN 388
Cdd:COG4235    19 GWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQ 98

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2730679916 389 GKARESAFLLQDMSFKRPDDAH---VWNRLAEA 418
Cdd:COG4235    99 GDYAEAIAAWQKLLALLPADAParlLEASIAEA 131
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 285-457 4.45e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 46.23  E-value: 4.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 285 KSADACTNKYESAVQESKGTSKhtAQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESIL 364
Cdd:TIGR02917 513 GNPDDAIQRFEKVLTIDPKNLR--AILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKKALAIL 590

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 365 KKML---KDNPENYVI--TMYLANtlGKNGKARESaflLQDMSFKRPDDAHVWNRLAEAQRINNNqigyYKAAAEYYQ-- 437
Cdd:TIGR02917 591 NEAAdaaPDSPEAWLMlgRAQLAA--GDLNKAVSS---FKKLLALQPDSALALLLLADAYAVMKN----YAKAITSLKra 661

                         170       180
                  ....*....|....*....|..
gi 2730679916 438 --LNGDFTNSQRQLMRALKLAE 457
Cdd:TIGR02917 662 leLKPDNTEAQIGLAQLLLAAK 683
M48B_HtpX_like cd07338
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 93-250 9.03e-05

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: 43.72  E-value: 9.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  93 IVDNKSLNAFA----VPGGVIGVNTGLFLYSqSEGEFSSVLSHELAHISQRHFARrvqdaqkrqpLTLAGLLATVL--LA 166
Cdd:cd07338    55 IAEDPIPNAFAygspLTGARVAVTRGLLDIL-NRDELEAVIGHELGHIKHRDVAI----------MTAIGLIPSIIyyIG 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 167 VTT-----------GGTAAIAAGSTAYAAN--AQ-ASLAFSRDMEQEADRIGMETLynsgynPNEmtdmfRNMNDA--KR 230
Cdd:cd07338   124 RSLlfsggssggrnGGGALLAVGIAAFAVYflFQlLVLGFSRLREYYADAHSAKVT------GNG-----RALQSAlaKI 192

                         170       180
                  ....*....|....*....|
gi 2730679916 231 YFGTnPPEYLLTHPLTESRV 250
Cdd:cd07338   193 AYGY-LAEIFSTHPLPAKRI 211
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 236-416 9.09e-05

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 45.07  E-value: 9.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 236 PPEYLLTHPLTESRVSDSANRASQyPAVKNGRTNFEYQLMKRRVEVHTLKSADActNKYESAVQESKgtSKHTAQYAL-A 314
Cdd:TIGR02917 636 LALLLLADAYAVMKNYAKAITSLK-RALELKPDNTEAQIGLAQLLLAAKRTESA--KKIAKSLQKQH--PKAALGFELeG 710

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 315 ICYTEDKQFEKALATLKPLQELWPLSITInVLEAEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTLGKNGKARES 394
Cdd:TIGR02917 711 DLYLRQKDYPAAIQAYRKALKRAPSSQNA-IKLHRALLASGNTAEAVKTLEAWLKTHPNDAVLRTALAELYLAQKDYDKA 789

                         170       180
                  ....*....|....*....|..
gi 2730679916 395 AFLLQDMSFKRPDDAHVWNRLA 416
Cdd:TIGR02917 790 IKHYQTVVKKAPDNAVVLNNLA 811
PRK01345 PRK01345
heat shock protein HtpX; Provisional
 75-206 1.01e-04

heat shock protein HtpX; Provisional


Pssm-ID: 234944 [Multi-domain]  Cd Length: 317  Bit Score: 44.24  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  75 IYRLAENSQLTDRRIetIIVDNKSLNAFAV---P-GGVIGVNTGLfLYSQSEGEFSSVLSHELAHIsqrhfarrvqdaQK 150
Cdd:PRK01345   73 VRDLARRAGLPMPKV--YIIDNPQPNAFATgrnPeNAAVAATTGL-LQRLSPEEVAGVMAHELAHV------------KN 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2730679916 151 RQPLTLAgLLATVLLAVT-------------------TGGTAAIAAGSTAYAANAQASLAFSRDMEQEADRIGME 206
Cdd:PRK01345  138 RDTLTMT-ITATLAGAISmlanfafffggnrennngpLGLVGTLAAMIVAPLAAMLVQMAISRTREYAADRRGAE 211
TPR_19 pfam14559
Tetratricopeptide repeat;
356-416 1.05e-04

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 40.26  E-value: 1.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2730679916 356 DLDEAESILKKMLKDNPENYVITMYLANTLGKNGKARESAFLLQDMSFKRPDDAHVWNRLA 416
Cdd:pfam14559   3 DYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLA 63
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 308-399 1.17e-04

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 42.64  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 308 TAQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTLGK 387
Cdd:COG5010    55 AIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLS 134

                          90
                  ....*....|..
gi 2730679916 388 NGKARESAFLLQ 399
Cdd:COG5010   135 LGQDDEAKAALQ 146
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 348-456 1.77e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 41.72  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 348 AEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTLGKNGKARESAFLLQDMSFKRPDDAHVWNRLAEAqrinnnqig 427
Cdd:COG4783    11 AQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA--------- 81

                          90       100
                  ....*....|....*....|....*....
gi 2730679916 428 yykaaaeyYQLNGDFTNSQRQLMRALKLA 456
Cdd:COG4783    82 --------LLKAGDYDEALALLEKALKLD 102
M48B_HtpX_like cd07335
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This family contains ...
 35-136 6.46e-04

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: 41.41  E-value: 6.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  35 TSGFISLdqeyQLGRgWLrALRS-QTPILEDPLLND--YLEFTIYRLAENSQLtdRRIETIIVDNKSLNAFAV----PGG 107
Cdd:cd07335     3 GGSFISL----LLSK-WM-AKRAmGVKVIDNPSNEKerWLVETVAELARKAGI--KMPEVGIYPSPDVNAFATgpsrNNS 74

                          90       100
                  ....*....|....*....|....*....
gi 2730679916 108 VIGVNTGLfLYSQSEGEFSSVLSHELAHI 136
Cdd:cd07335    75 LVAVSTGL-LDNMSEDEVEAVLAHEISHI 102
M48B_HtpX_like cd07327
HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, ...
 77-250 7.10e-04

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: 40.70  E-value: 7.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  77 RLAENSQLTDRRIetIIVDNKSLNAFAVpGG-----VIGVNTGLfLYSQSEGEFSSVLSHELAHISQRhfarrvqDaqkr 151
Cdd:cd07327    32 RLARRAGLPKPRV--AIVDTPMPNAFAT-GRnpknaAVAVTTGL-LQLLNEDELEAVLAHELSHIKNR-------D---- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 152 qplTLAGLLAtvllavttggtaaiaagstayaanaqaslAFSRDMEQEADRIG--------------------METLYNS 211
Cdd:cd07327    97 ---VLVMTLA-----------------------------SLSRYREFAADRGSakltgdplalasalmkisgsMQRIPKR 144

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2730679916 212 GYNPNEMTDMFRNMNDAKRYFGtnppEYLLTHPLTESRV 250
Cdd:cd07327   145 DLRQVEASAFFIIPPLSGGSLA----ELFSTHPPTEKRI 179
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
294-414 8.65e-04

Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 41.02  E-value: 8.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 294 YESAVQESKGTSKHtAQYALAICYTEDKQFEKALATLKPLQELWPL--SITINVLEAEILSKKRDLDEAESILKKMLK-- 369
Cdd:COG4700   112 YEEALTGIFADDPH-ILLGLAQALFELGRYAEALETLEKLIAKNPDfkSSDAHLLYARALEALGDLEAAEAELEALARry 190

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2730679916 370 DNPENYVitmYLANTLGKNGKARESAFLLQDMSfkrpDDAHVWNR 414
Cdd:COG4700   191 SGPEARY---RYAKFLARQGRTAEAKELLEEIL----DEAKHMPK 228
M56_BlaR1_MecR1_like cd07326
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 101-181 1.17e-03

Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; 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 ?-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: 320685 [Multi-domain]  Cd Length: 165  Bit Score: 39.60  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 101 AFAVPG--GVIGVNTGLF--LysqSEGEFSSVLSHELAHISQRH------------------FARRVQD----------- 147
Cdd:cd07326    39 AFCLGGrrPRIVLSTGLLelL---SPEELRAVLAHERAHLRRRDplllllasalaralpflpLLRRLAAayrllrelaad 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2730679916 148 ---AQKRQPLTLAGLLATVLLA---VTTGGTAAIAAGSTA 181
Cdd:cd07326   116 daaARRVGPRALASALLKLARAgapAAPAGALAFAGAAVN 155
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
316-407 1.23e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 38.23  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 316 CYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESiLKKMLKDNPENYVITMYLANTLGKNGKARESA 395
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEAL 79

                          90
                  ....*....|..
gi 2730679916 396 FLLQDMSFKRPD 407
Cdd:COG3063    80 AYLERALELDPS 91
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 346-459 1.96e-03

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 40.10  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 346 LEAEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTLGKNGKARESAFLLQDMSFKRPDDAHVWNRLAEAqrinnnq 425
Cdd:COG2956    13 FKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQD------- 85

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2730679916 426 igyykaaaeyYQLNGDFTNSQRQLMRALKLAEFD 459
Cdd:COG2956    86 ----------YLKAGLLDRAEELLEKLLELDPDD 109
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
350-437 2.12e-03

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 37.46  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 350 ILSKKRDLDEAESILKKMLKDNPENYVITMYLANTLGKNGKARESAFLLQDMSFKrPDDAHVWNRLAEAQRinnnQIGYY 429
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALEKALKLD-PNNAEALLNLAELLL----ELGDY 75


                  ....*...
gi 2730679916 430 KAAAEYYQ 437
Cdd:COG3063    76 DEALAYLE 83
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 309-372 2.13e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 38.79  E-value: 2.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2730679916 309 AQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNP 372
Cdd:COG5010    90 LYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 319-454 2.23e-03

Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to protoporphyrinogen oxidase HemY) [Function unknown];


Pssm-ID: 442305 [Multi-domain]  Cd Length: 323  Bit Score: 39.89  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 319 EDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNpenyVITMYLANTLgkngKARESAFLL 398
Cdd:COG3071    97 DQGQAEQALATLEALRAGAPRHPQVLRLLLQAYRQLGDWEELLELLPALRKHK----ALSAEEAQAL----ERRAYLGLL 168

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2730679916 399 QDMSFKRPDDAHVWNRLAEAQRinnNQIGYYKAAAEYYQLNGDFTNSQRQLMRALK 454
Cdd:COG3071   169 RQAARDAEALKALWKALPRAER---RDPELAAAYARALIALGDHDEAERLLREALK 221
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 309-437 2.46e-03

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 38.79  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 309 AQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILKKMLKDNPENYVITMYLANTLGKN 388
Cdd:COG5010    22 TLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRS 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2730679916 389 GKARESAFLLQDMSFKRPDDAHVWNRLAEAQRinnnQIGYYKAAAEYYQ 437
Cdd:COG5010   102 GDKDEAKEYYEKALALSPDNPNAYSNLAALLL----SLGQDDEAKAALQ 146
PRK02391 PRK02391
heat shock protein HtpX; Provisional
 63-163 4.00e-03

heat shock protein HtpX; Provisional


Pssm-ID: 179418 [Multi-domain]  Cd Length: 296  Bit Score: 39.15  E-value: 4.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916  63 EDPLLNDylefTIYRLAENSQLTDRRIEtiIVDNKSLNAFAV---PG-GVIGVNTGLfLYSQSEGEFSSVLSHELAHISQ 138
Cdd:PRK02391   74 EYPELHA----MVERLCALADLPKPRVA--VADSDVPNAFATgrsPKnAVVCVTTGL-MRRLDPDELEAVLAHELSHVKN 146

                          90       100
                  ....*....|....*....|....*
gi 2730679916 139 RHFArrvqdaqkrqPLTLAGLLATV 163
Cdd:PRK02391  147 RDVA----------VMTIASFLSTI 161
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 291-456 8.90e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 38.91  E-value: 8.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 291 TNKYESAVQESKGTSKHT-----AQYALAICYTEDKQFEKALATLKPLQELWPLSITINVLEAEILSKKRDLDEAESILK 365
Cdd:TIGR02917 240 AGEFEEAEKHADALLKKApnsplAHYLKALVDFQKKNYEDARETLQDALKSAPEYLPALLLAGASEYQLGNLEQAYQYLN 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730679916 366 KMLKDNPENYVITMYLANTLGKNGKARESAFLLQDMSFKRPDDAHVWNRLAEAqrinnnqigyykaaaeyYQLNGDFTNS 445
Cdd:TIGR02917 320 QILKYAPNSHQARRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEA-----------------YLALGDFEKA 382

                         170
                  ....*....|.
gi 2730679916 446 QRQLMRALKLA 456
Cdd:TIGR02917 383 AEYLAKATELD 393
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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