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Conserved domains on  [gi|16130419|ref|NP_416989|]
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beta-barrel assembly-enhancing protease [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M48C_bepA_like cd07333
Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase ...
 48-262 4.94e-61

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: 197.33  E-value: 4.94e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  48 QEMQMGDYYVRQLRGSAPLINDPLLTQYINSLGMRLVSHANSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYSDNE 127
Cdd:cd07333   1 QEVELGKQFAQQIRQQLPLVEDPEVNEYVNRIGQRLAAVSPRPPFPYRFFVVNDDSINAFATPGGYIYVNTGLILAADNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 128 SQLASVMAHEISHVTQRHLARAMEDqqrsapltwvgalgsillamaspqagmaaltgtlagtrqgmiSFTQQNEQEADRI 207
Cdd:cd07333  81 AELAGVLAHEIGHVVARHIAKQIEK------------------------------------------SYSREDEREADQL 118

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130419 208 GIQVLQRSGFDPQAMPTFLEKLLDQARYS-SRPPEILLTHPLPESRLADARNRANQ 262
Cdd:cd07333 119 GLQYLTKAGYDPRGMVSFFKKLRRKEWFGgSSIPTYLSTHPAPAERIAYLEELIAS 174
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 307-440 1.13e-13

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: 67.91  E-value: 1.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 307 QQRAAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLR-TNPVLQLNLANA 385
Cdd:COG4783   2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDpDEPEARLNLGLA 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16130419 386 YLQGGQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQELAARAEGYALA 440
Cdd:COG4783  82 LLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
 
Name Accession Description Interval E-value
M48C_bepA_like cd07333
Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase ...
 48-262 4.94e-61

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: 197.33  E-value: 4.94e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  48 QEMQMGDYYVRQLRGSAPLINDPLLTQYINSLGMRLVSHANSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYSDNE 127
Cdd:cd07333   1 QEVELGKQFAQQIRQQLPLVEDPEVNEYVNRIGQRLAAVSPRPPFPYRFFVVNDDSINAFATPGGYIYVNTGLILAADNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 128 SQLASVMAHEISHVTQRHLARAMEDqqrsapltwvgalgsillamaspqagmaaltgtlagtrqgmiSFTQQNEQEADRI 207
Cdd:cd07333  81 AELAGVLAHEIGHVVARHIAKQIEK------------------------------------------SYSREDEREADQL 118

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130419 208 GIQVLQRSGFDPQAMPTFLEKLLDQARYS-SRPPEILLTHPLPESRLADARNRANQ 262
Cdd:cd07333 119 GLQYLTKAGYDPRGMVSFFKKLRRKEWFGgSSIPTYLSTHPAPAERIAYLEELIAS 174
COG4784 COG4784
Putative Zn-dependent protease [General function prediction only];
1-262 6.11e-42

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


Pssm-ID: 443814 [Multi-domain]  Cd Length: 488  Bit Score: 155.82  E-value: 6.11e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419   1 MFRQLKKNLVATLIAAMTIGQVAPAfadsadTLPDMGTSAGSTLSIGQEMQMGDYYVRQLRGS-APLINDPLLTQYINSL 79
Cdd:COG4784   1 MRRRRRRALRLLLALALALLLAGCA------TNPVTGKRDLVLMSEEQEIAIGAEEHPRILAQyGGAYDDPKLQAYVARV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  80 GMRLVSHANSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMEDQQRSApl 159
Cdd:COG4784  75 GQRLAAASHRPDLPYTFTVLDSPVVNAFALPGGYVYVTRGLLALANDEAELAAVLGHEIGHVTARHAVQRQSRATAAQ-- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 160 twvGALGSILLAM-ASPQAGMAAltgtLAGTRQGMISFTQQNEQEADRIGIQVLQRSGFDPQAMPTFLEKLLDQARYSSR 238
Cdd:COG4784 153 ---IGLGRVLSPVlGSAQAGQLA----GAGAQLLLASFSRDQELEADRLGVRYLARAGYDPYAMARFLGSLKRQSAFRAR 225

                       250       260       270
                ....*....|....*....|....*....|...
gi 16130419 239 P---------PEILLTHPLPESRLADARNRANQ 262
Cdd:COG4784 226 LagregrrsyPDFLSTHPDTPDRVQRAVAAARQ 258
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 70-260 5.10e-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: 110.60  E-value: 5.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419    70 PLLTQYINSLGMRLVSHANSVKTPFHFFLIN-NDEINAFAFF---GGNVVLHSALFRYSDNESQLASVMAHEISHVTQRH 145
Cdd:pfam01435   1 PLRNAELQRVVERLAAAAGLPLPPWYVVVIKsSPVPNAFAYGllpGGRVVVTTGLLDLLETEDELAAVLGHEIGHIKARH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419   146 LARAMEDQQRSAPLTWVGALGSILLAM---ASPQAGMAALTGTLAGTRQGMI-SFTQQNEQEADRIGIQVLQRSGFDPQA 221
Cdd:pfam01435  81 SVESLSIMGGLSLAQLFLALLLLGAAAsgfANFGIIFLLLIGPLAALLTLLLlPYSRAQEYEADRLGAELMARAGYDPRA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 16130419   222 MPTFLEK--LLDQARYSSRPPEILLTHPLPESRLADARNRA 260
Cdd:pfam01435 161 LIKLWGEidNNGRASDGALYPELLSTHPSLVERIAALRERA 201
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 307-440 1.13e-13

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: 67.91  E-value: 1.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 307 QQRAAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLR-TNPVLQLNLANA 385
Cdd:COG4783   2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDpDEPEARLNLGLA 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16130419 386 YLQGGQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQELAARAEGYALA 440
Cdd:COG4783  82 LLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
TPR_19 pfam14559
Tetratricopeptide repeat;
356-418 7.76e-07

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 46.42  E-value: 7.76e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130419   356 QNKANEAINRLKNARDL-RTNPVLQLNLANAYLQGGQPQEAANILNRYTFNNKDDSNGWDLLAQ 418
Cdd:pfam14559   1 EGDYAEALELLEQALAEdPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAK 64
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 299-434 2.21e-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: 47.00  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419   299 EWAKGNVRqqraAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLRTNPVL 378
Cdd:TIGR02917 663 ELKPDNTE----AQIGLAQLLLAAKRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSSQN 738

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130419   379 QLNLANAYLQGGQPQEAANILNRYTFNNKDDSNGwdLLAQAEAALNNRDQELAARA 434
Cdd:TIGR02917 739 AIKLHRALLASGNTAEAVKTLEAWLKTHPNDAVL--RTALAELYLAQKDYDKAIKH 792
PRK03001 PRK03001
zinc metalloprotease HtpX;
97-247 2.60e-03

zinc metalloprotease HtpX;


Pssm-ID: 179524 [Multi-domain]  Cd Length: 283  Bit Score: 39.62  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419   97 FLINNDEINAFAFfGGN-----VVLHSALFRYSdNESQLASVMAHEISHVTQRHL-----------ARAM---------- 150
Cdd:PRK03001  88 YLINEDQPNAFAT-GRNpehaaVAATTGILRVL-SEREIRGVMAHELAHVKHRDIlistisatmagAISAlanfamffgg 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  151 --EDQQRSAPLTwvgalgSILLAMASPQAgmaaltgtlAGTRQGMISFTQqnEQEADRIGIQVlqrSGfDPQAMPTFLEK 228
Cdd:PRK03001 166 rdENGRPVNPIA------GIAVAILAPLA---------ASLIQMAISRAR--EFEADRGGARI---SG-DPQALASALDK 224

                        170
                 ....*....|....*....
gi 16130419  229 LLDQARysSRPPEILLTHP 247
Cdd:PRK03001 225 IHRYAS--GIPFQAAEAHP 241
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
 307-434 6.21e-03

tetratricopeptide repeat protein; Provisional


Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 39.02  E-value: 6.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  307 QQRAAQYG--RALQAMEANKYDEARKTLQPLLAAEPGNA-WYLDLAtDIDLGQNKANEAINRLKNArdLRTNP-----VL 378
Cdd:PRK11788 176 RVEIAHFYceLAQQALARGDLDAARALLKKALAADPQCVrASILLG-DLALAQGDYAAAIEALERV--EEQDPeylseVL 252

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130419  379 QLnLANAYLQGGQPQEAANILNRYTfnnkDDSNGWDLLAQAEAALNNRDQELAARA 434
Cdd:PRK11788 253 PK-LMECYQALGDEAEGLEFLRRAL----EEYPGADLLLALAQLLEEQEGPEAAQA 303
 
Name Accession Description Interval E-value
M48C_bepA_like cd07333
Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase ...
 48-262 4.94e-61

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: 197.33  E-value: 4.94e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  48 QEMQMGDYYVRQLRGSAPLINDPLLTQYINSLGMRLVSHANSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYSDNE 127
Cdd:cd07333   1 QEVELGKQFAQQIRQQLPLVEDPEVNEYVNRIGQRLAAVSPRPPFPYRFFVVNDDSINAFATPGGYIYVNTGLILAADNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 128 SQLASVMAHEISHVTQRHLARAMEDqqrsapltwvgalgsillamaspqagmaaltgtlagtrqgmiSFTQQNEQEADRI 207
Cdd:cd07333  81 AELAGVLAHEIGHVVARHIAKQIEK------------------------------------------SYSREDEREADQL 118

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130419 208 GIQVLQRSGFDPQAMPTFLEKLLDQARYS-SRPPEILLTHPLPESRLADARNRANQ 262
Cdd:cd07333 119 GLQYLTKAGYDPRGMVSFFKKLRRKEWFGgSSIPTYLSTHPAPAERIAYLEELIAS 174
M48C_Oma1-like cd07324
Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 ...
 75-258 6.13e-51

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: 169.67  E-value: 6.13e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  75 YINSLGMRLVSHANSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMEdqq 154
Cdd:cd07324   1 YLNRLGDRLAAASGRPDLPYRFFVVDDPSINAFALPGGYIFVTTGLLLLLESEDELAAVLAHEIGHVTLRHIARQLE--- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 155 rsapltwvgalgsillamaspqagmaaltgtlagtrqgmiSFTQQNEQEADRIGIQVLQRSGFDPQAMPTFLEKLLDQAR 234
Cdd:cd07324  78 ----------------------------------------RYSRDQEREADRLGLQLLARAGYDPRGMARFFERLARQEG 117

                       170       180
                ....*....|....*....|....*
gi 16130419 235 YS-SRPPEILLTHPLPESRLADARN 258
Cdd:cd07324 118 LSgSRLPEFLSTHPLTAERIAALRA 142
COG4784 COG4784
Putative Zn-dependent protease [General function prediction only];
1-262 6.11e-42

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


Pssm-ID: 443814 [Multi-domain]  Cd Length: 488  Bit Score: 155.82  E-value: 6.11e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419   1 MFRQLKKNLVATLIAAMTIGQVAPAfadsadTLPDMGTSAGSTLSIGQEMQMGDYYVRQLRGS-APLINDPLLTQYINSL 79
Cdd:COG4784   1 MRRRRRRALRLLLALALALLLAGCA------TNPVTGKRDLVLMSEEQEIAIGAEEHPRILAQyGGAYDDPKLQAYVARV 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  80 GMRLVSHANSVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMEDQQRSApl 159
Cdd:COG4784  75 GQRLAAASHRPDLPYTFTVLDSPVVNAFALPGGYVYVTRGLLALANDEAELAAVLGHEIGHVTARHAVQRQSRATAAQ-- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 160 twvGALGSILLAM-ASPQAGMAAltgtLAGTRQGMISFTQQNEQEADRIGIQVLQRSGFDPQAMPTFLEKLLDQARYSSR 238
Cdd:COG4784 153 ---IGLGRVLSPVlGSAQAGQLA----GAGAQLLLASFSRDQELEADRLGVRYLARAGYDPYAMARFLGSLKRQSAFRAR 225

                       250       260       270
                ....*....|....*....|....*....|...
gi 16130419 239 P---------PEILLTHPLPESRLADARNRANQ 262
Cdd:COG4784 226 LagregrrsyPDFLSTHPDTPDRVQRAVAAARQ 258
M48C_Oma1_like cd07331
Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 76-263 2.77e-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: 132.70  E-value: 2.77e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  76 INSLGMRLVSHAN-----SVKTPFHFFLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLAram 150
Cdd:cd07331   1 VRRVAARLIAAAGddppqSAGWDWEVHVIDSPEVNAFVLPGGKIFVFTGLLPVAKNDDELAAVLGHEIAHALARHSA--- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 151 edqQRSAPLTWVGALGSILLAMA-SPQAGMAALTGTLAGTRQGMISFTQQNEQEADRIGIQVLQRSGFDPQAMPTFLEKl 229
Cdd:cd07331  78 ---ERMSQQKLLQLLLLLLLAALgASLAGLALGLLGLGAQLGLLLPYSRKQELEADRIGLQLMAKAGYDPRAAVTFWEK- 153

                       170       180       190
                ....*....|....*....|....*....|....
gi 16130419 230 LDQARYSSRPPEILLTHPLPESRLADARNRANQM 263
Cdd:cd07331 154 MAAAEGGGKPPEFLSTHPSSETRIEALEELLPEA 187
M48C_Oma1_like cd07332
Peptidase M48C Ste24p, integral membrane endopeptidase; This subfamily contains peptidase M48C ...
 49-258 5.38e-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: 121.91  E-value: 5.38e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  49 EMQMGDYYVRQLRGSAPLINDPLLT--QYINSLGMRLVShANSVKTPFHFFLIN-NDEINAFAFFGGNVVLHSALFRYSD 125
Cdd:cd07332  21 EEKLGEQTLELLDETLLEPSELPAErqAALQQLFARLLA-ALPLPYPYRLHFRDsGIGANAFALPGGTIVVTDGLVELAE 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 126 NESQLASVMAHEISHVTQRHLARAMedqQRSApltwvgALGSILLAMASPQAGMAALTGTLAGTRQGMiSFTQQNEQEAD 205
Cdd:cd07332 100 SPEELAAVLAHEIGHVEHRHSLRQL---IRSS------GLSLLVSLLTGDVSGLSDLLAGLPALLLSL-SYSRDFEREAD 169

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 16130419 206 RIGIQVLQRSGFDPQAMPTFLEKLLDQARYSSRPPEILLTHPLPESRLADARN 258
Cdd:cd07332 170 AFALELLKAAGISPEGLADFFERLEEEHGDGGSLPEWLSTHPDTEERIEAIRE 222
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 70-260 5.10e-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: 110.60  E-value: 5.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419    70 PLLTQYINSLGMRLVSHANSVKTPFHFFLIN-NDEINAFAFF---GGNVVLHSALFRYSDNESQLASVMAHEISHVTQRH 145
Cdd:pfam01435   1 PLRNAELQRVVERLAAAAGLPLPPWYVVVIKsSPVPNAFAYGllpGGRVVVTTGLLDLLETEDELAAVLGHEIGHIKARH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419   146 LARAMEDQQRSAPLTWVGALGSILLAM---ASPQAGMAALTGTLAGTRQGMI-SFTQQNEQEADRIGIQVLQRSGFDPQA 221
Cdd:pfam01435  81 SVESLSIMGGLSLAQLFLALLLLGAAAsgfANFGIIFLLLIGPLAALLTLLLlPYSRAQEYEADRLGAELMARAGYDPRA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 16130419   222 MPTFLEK--LLDQARYSSRPPEILLTHPLPESRLADARNRA 260
Cdd:pfam01435 161 LIKLWGEidNNGRASDGALYPELLSTHPSLVERIAALRERA 201
M48C_loiP_like cd07334
Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase ...
 43-259 5.04e-20

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: 88.41  E-value: 5.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  43 TLSIGQEMQMGDYYVRQLRGSAPL--INDPLlTQYINslgmRLVS-HANSVKTPFHFFLINNDEINAFAFFGGNVVLHSA 119
Cdd:cd07334  10 TLSDEEVKALAAQSAAQMDAKNPVapANSPY-AKRLA----RLTKgLKSYDGLPLNFKVYLTPDVNAFAMADGSVRVYSG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 120 LF-RYSDNEsqLASVMAHEISHVTQRHLARAMEDQ-QRSAPLTWVGALGSILLAMASPQAGmaALTGTLAGTRqgmisFT 197
Cdd:cd07334  85 LMdMMTDDE--LLGVIGHEIGHVKLGHSKKAMKTAyLTSAARKAAASASGTVGALSDSQLG--ALAEKLINAQ-----FS 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130419 198 QQNEQEADRIGIQVLQRSGFDPQAMPTFLEKLldQARYSSRPPEILLTHPLPESRLADARNR 259
Cdd:cd07334 156 QKQESEADDYGYKFLKKNGYNPQAAVSALEKL--AALSGGGKSSLFSSHPDPAKRAERIRAR 215
M48C_Oma1_like cd07342
M48C peptidase, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 96-254 1.17e-16

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: 77.30  E-value: 1.17e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  96 FFLINNDEINAFAFfGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMedqqrsapltWVGALGSILLAMAsp 175
Cdd:cd07342  23 VELGNSDGVNAYAD-GRRVQITSGMMDFAQDDDELALVVAHELAHNILGHRDRLR----------ANGVAGGLLDGFG-- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 176 qAGMAaltgtlagtrqgmisFTQQNEQEADRIGIQVLQRSGFDPQAMPTFLEKLLdqarySSRPPEILL--THPLPESRL 253
Cdd:cd07342  90 -GNAA---------------YSREFEIEADYLGLYLMARAGYDIDGAADFWRRLG-----ASHPVGIGRaaTHPSTAERF 148


                .
gi 16130419 254 A 254
Cdd:cd07342 149 A 149
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 307-440 1.13e-13

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: 67.91  E-value: 1.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 307 QQRAAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLR-TNPVLQLNLANA 385
Cdd:COG4783   2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDpDEPEARLNLGLA 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16130419 386 YLQGGQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQELAARAEGYALA 440
Cdd:COG4783  82 LLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 97-265 4.02e-11

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


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 62.59  E-value: 4.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  97 FLINNDEINAFAF-FGGN---VVLHSALFRYSDnESQLASVMAHEISHVTQRH---LARAMedqqrsAPLTWVGALGSIL 169
Cdd:COG0501  23 YVMDSPAPNAFATgRGPNnarIVVTDGLLELLD-RDELEAVLAHELGHIKNGDillMTLAS------GLLGLIGFLARLL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 170 LAMASPQAGMAALTGTLAGTRQGMIS------FTQQNEQEADRIGIQVLQrsgfDPQAMPTFLEKLldqARYSSRPPE-- 241
Cdd:COG0501  96 PLAFGRDRDAGLLLGLLLGILAPFLAtliqlaLSRKREYEADRAAAELTG----DPDALASALRKL---AGGNLSIPLrr 168

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 16130419 242 ------------------ILLTHPLPESRLADARNRANQMRP 265
Cdd:COG0501 169 afpaqahafiinplklssLFSTHPPLEERIARLRELAAEGEY 210
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
311-480 5.90e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 53.86  E-value: 5.90e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 311 AQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLR-TNPVLQLNLANAYLQG 389
Cdd:COG0457  44 ALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDpDDAEALYNLGLALLEL 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 390 GQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQELAARAEGYALAGRLDQAISLLSSASSQVKLGSLQQARYDA 469
Cdd:COG0457 124 GRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLAL 203

                       170
                ....*....|.
gi 16130419 470 RIDQLRQLQER 480
Cdd:COG0457 204 EQALRKKLAIL 214
M48B_HtpX_like cd07337
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 72-240 8.28e-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: 320696 [Multi-domain]  Cd Length: 203  Bit Score: 52.70  E-value: 8.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  72 LTQYINSLGMRLVSHANSVKtpfhFFLINNDEINAFAfFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHlarame 151
Cdd:cd07337  41 INPELEDKARRLGPDPEKVK----LFISDDEYPNAFA-LGRNTICVTKGLLDLLDYEELKGILAHELGHLSHKD------ 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 152 dqqrsaplTWVGALGSILLAMaspqAGMAALTGTLAGTRQGMIS---FTQQNEQEADR----IG-----IQVLQRSGFDP 219
Cdd:cd07337 110 --------TDYLLLIFVLLLL----AAIWTKLGTLLIFVWIRLLvmfSSRKAEYRADAfavkIGygeglRSALDQLREYE 177

                       170       180
                ....*....|....*....|.
gi 16130419 220 QAMPTFLEKLldqarYSSRPP 240
Cdd:cd07337 178 DAPKGFLAAL-----YSTHPP 193
M48_Ste24p_like cd07325
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 96-254 2.41e-07

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: 51.07  E-value: 2.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  96 FFLINNDEINAFAF-FGGN--VVLHSALFRYSDnESQLASVMAHEISHVTQRH-LARAMedqqrSAPLTWVGALGSILLA 171
Cdd:cd07325  34 LYVYQSPVLNAFALgFEGRpfIVLNSGLVELLD-DDELRFVIGHELGHIKSGHvLYRTL-----LLLLLLLGELIGILLL 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 172 MASPQAGMAALtgtlagTRQGMISftqqneqeADRIG----------IQVLQR--SGFDPQAMPTFLEKLLDQARYSSRP 239
Cdd:cd07325 108 SSALPLALLAW------SRAAEYS--------ADRAGllvcqdpeaaIRALMKlaGGSKLLKDVNNIEYFLEEEAQADAL 173

                       170       180
                ....*....|....*....|..
gi 16130419 240 P-------EILLTHPLPESRLA 254
Cdd:cd07325 174 DgffkwlsELLSTHPFLVKRAA 195
TPR_19 pfam14559
Tetratricopeptide repeat;
356-418 7.76e-07

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 46.42  E-value: 7.76e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130419   356 QNKANEAINRLKNARDL-RTNPVLQLNLANAYLQGGQPQEAANILNRYTFNNKDDSNGWDLLAQ 418
Cdd:pfam14559   1 EGDYAEALELLEQALAEdPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAK 64
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 311-428 8.04e-07

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: 50.50  E-value: 8.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 311 AQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDL-RTNPVLQLNLANAYLQG 389
Cdd:COG2956 112 ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLdPDCARALLLLAELYLEQ 191

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 16130419 390 GQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQ 428
Cdd:COG2956 192 GDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEE 230
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 294-440 1.99e-06

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 50.38  E-value: 1.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 294 SDLLDEWAKGNVRQQRAAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLR 373
Cdd:COG3914  63 AAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALN 142

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130419 374 -TNPVLQLNLANAYLQGGQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQELAARAEGYALA 440
Cdd:COG3914 143 pDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELD 210
M48B_HtpX_like cd07338
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 84-254 3.54e-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: 320697 [Multi-domain]  Cd Length: 216  Bit Score: 47.96  E-value: 3.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  84 VSHANSVKTPfHFFLINNDEINAFAF----FGGNVVLHSALFRYSdNESQLASVMAHEISHVtqRHlaRAMedqqrsAPL 159
Cdd:cd07338  42 VARRAGIKPP-KVGIAEDPIPNAFAYgsplTGARVAVTRGLLDIL-NRDELEAVIGHELGHI--KH--RDV------AIM 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 160 TWVGALGSIL--LAMASPQAGMAALTGTLAGTR--------------QGMI-SFTQQNEQEADRIGIQVLQrsgfDPQAM 222
Cdd:cd07338 110 TAIGLIPSIIyyIGRSLLFSGGSSGGRNGGGALlavgiaafavyflfQLLVlGFSRLREYYADAHSAKVTG----NGRAL 185

                       170       180       190
                ....*....|....*....|....*....|..
gi 16130419 223 PTFLEKLldqARYSSRppEILLTHPLPESRLA 254
Cdd:cd07338 186 QSALAKI---AYGYLA--EIFSTHPLPAKRIQ 212
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 311-402 9.32e-06

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: 47.42  E-value: 9.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 311 AQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLRTNPVLQLNLANAYLQGG 390
Cdd:COG2956 180 ALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKE 259

                        90
                ....*....|..
gi 16130419 391 QPQEAANILNRY 402
Cdd:COG2956 260 GLEAALALLERQ 271
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 320-432 1.46e-05

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: 46.65  E-value: 1.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 320 MEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLR-TNPVLQLNLANAYLQGGQPQEAANI 398
Cdd:COG2956  53 RRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDpDDAEALRLLAEIYEQEGDWEKAIEV 132

                        90       100       110
                ....*....|....*....|....*....|....
gi 16130419 399 LNRYTFNNKDDSNGWDLLAQAEAALNNRDQELAA 432
Cdd:COG2956 133 LERLLKLGPENAHAYCELAELYLEQGDYDEAIEA 166
Peptidase_M48_M56 cd05843
Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral ...
 93-147 1.68e-05

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: 43.59  E-value: 1.68e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16130419  93 PFHFFLINNDEINAFAFFGGN--VVLHSALFRySDNESQLASVMAHEISHVTQRHLA 147
Cdd:cd05843  17 LDKVVVVPGSVPNAFFTGGANkrVVLTTALLE-LLSEEELAAVIAHELGHFKAHEYQ 72
M56_like cd07329
Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains ...
 97-253 2.09e-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: 45.13  E-value: 2.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  97 FLINNDEINAFA---FFGGNVVLHSALFRySDNESQLASVMAHEISHVTQRH----------------LARAMEDQQRSA 157
Cdd:cd07329  15 YVVDSDVPNAFAvgrSRGPTVVVTTGLLD-LLDDDELEAVLAHELAHLKRRDvlvlllfdpllllvvgLLLFLSLFIFEL 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 158 PLTWVGALGSILLAMASPQAGMAALTGTLAGTRqgmisftqqNEQEADRIGiqvlqrsgfDPQAMPTFLEKLLDQARY-- 235
Cdd:cd07329  94 LGFFFQPLLFLAFFALLRLAELLADALAVARTS---------AARRARLTG---------LPAALASALEKIEDASDRal 155

                       170       180
                ....*....|....*....|....*...
gi 16130419 236 ----------SSRPPEILLTHPLPESRL 253
Cdd:cd07329 156 eaglvlpalaADASSLEKTDHPPLEERV 183
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 310-409 2.21e-05

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: 44.41  E-value: 2.21e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 310 AAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLR-TNPVLQLNLANAYLQ 388
Cdd:COG4783  39 EAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDpEHPEAYLRLARAYRA 118

                        90       100
                ....*....|....*....|.
gi 16130419 389 GGQPQEAANILNRYTFNNKDD 409
Cdd:COG4783 119 LGRPDEAIAALEKALELDPDD 139
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 299-434 2.21e-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: 47.00  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419   299 EWAKGNVRqqraAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLRTNPVL 378
Cdd:TIGR02917 663 ELKPDNTE----AQIGLAQLLLAAKRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSSQN 738

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130419   379 QLNLANAYLQGGQPQEAANILNRYTFNNKDDSNGwdLLAQAEAALNNRDQELAARA 434
Cdd:TIGR02917 739 AIKLHRALLASGNTAEAVKTLEAWLKTHPNDAVL--RTALAELYLAQKDYDKAIKH 792
YfgM COG2976
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal ...
 300-432 2.84e-05

Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal transduction mechanisms];


Pssm-ID: 442215 [Multi-domain]  Cd Length: 207  Bit Score: 45.23  E-value: 2.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 300 WAKGNVRQQRAAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAwYLDLAT----DIDLGQNKANEAINRLKNARDLRTN 375
Cdd:COG2976  44 SYQESQAEEASALYEQLLEALAAGDAAAAAAAAEKLIDDYGGTA-YAALAAlllaKAAVDAGDLDKAAAQLQWVLDNAKD 122

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130419 376 PVLQ----LNLANAYLQGGQPQEAANILnrytfnNKDDSNGW-----DLLAQAEAALNNRDQELAA 432
Cdd:COG2976 123 PALKalarLRLARVLLAQKKYDEALATL------DAVKPEAFaalyaELRGDILLAQGDKAEARAA 182
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
311-481 4.47e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.00  E-value: 4.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 311 AQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLR-TNPVLQLNLANAYLQG 389
Cdd:COG0457  10 AYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDpDDAEALNNLGLALQAL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 390 GQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQelAARAEGYALAGRLDQAISLLSSASSQVKLGSLQQARYDA 469
Cdd:COG0457  90 GRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDE--AIEAYERALELDPDDADALYNLGIALEKLGRYEEALELL 167

                       170
                ....*....|..
gi 16130419 470 RIDQLRQLQERF 481
Cdd:COG0457 168 EKLEAAALAALL 179
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 276-441 5.28e-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: 45.84  E-value: 5.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419   276 LAKARTLGMYNSGRNQLTSDL--LDEWAKGNVRQQRAAQY-GRALQAmeANKYDEARKTLQPLLAAEPGNAWYLDLATDI 352
Cdd:TIGR02917 567 IEPALALAQYYLGKGQLKKALaiLNEAADAAPDSPEAWLMlGRAQLA--AGDLNKAVSSFKKLLALQPDSALALLLLADA 644

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419   353 DLGQNKANEAINRLKNARDLRT-NPVLQLNLANAYLQGGQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQELA 431
Cdd:TIGR02917 645 YAVMKNYAKAITSLKRALELKPdNTEAQIGLAQLLLAAKRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQ 724

                         170
                  ....*....|
gi 16130419   432 ARAEGYALAG 441
Cdd:TIGR02917 725 AYRKALKRAP 734
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
310-477 7.04e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 44.23  E-value: 7.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 310 AAQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLR-TNPVLQLNLANAYLQ 388
Cdd:COG0457  77 EALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDpDDADALYNLGIALEK 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 389 GGQPQEAANILNRYTFNNKDDSNGWDLLAQAEAALNNRDQELAARAEGYALAGRLDQAISLLSSASSQVKLGSLQQARYD 468
Cdd:COG0457 157 LGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLA 236


                ....*....
gi 16130419 469 ARIDQLRQL 477
Cdd:COG0457 237 ALALYQYRA 245
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 311-422 2.67e-04

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: 40.76  E-value: 2.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 311 AQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLR-TNPVLQLNLANAYLQG 389
Cdd:COG4235  19 GWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDpDNPEALYLLGLAAFQQ 98

                        90       100       110
                ....*....|....*....|....*....|...
gi 16130419 390 GQPQEAANILNRYTFNNKDDSNGWDLLAQAEAA 422
Cdd:COG4235  99 GDYAEAIAAWQKLLALLPADAPARLLEASIAEA 131
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 305-433 3.45e-04

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: 43.15  E-value: 3.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419   305 VRQQRAAQYGRALQAMEANKYDEARKTLQPLLAAEPG--NAWYLDLATDIDLGQ-NKANEAINR-LKNARDlrtNPVLQL 380
Cdd:TIGR02917 257 APNSPLAHYLKALVDFQKKNYEDARETLQDALKSAPEylPALLLAGASEYQLGNlEQAYQYLNQiLKYAPN---SHQARR 333

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 16130419   381 NLANAYLQGGQPQEAANILNRYTFNNKDDSNGWDLLaqAEAALNNRDQELAAR 433
Cdd:TIGR02917 334 LLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLL--GEAYLALGDFEKAAE 384
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 327-428 3.67e-04

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: 40.37  E-value: 3.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 327 EARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLR-TNPVLQLNLANAYLQGGQPQEAANILNRYTFN 405
Cdd:COG4235   1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDpDNADALLDLAEALLAAGDTEEAEELLERALAL 80

                        90       100
                ....*....|....*....|...
gi 16130419 406 NKDDSNGWDLLAQAEAALNNRDQ 428
Cdd:COG4235  81 DPDNPEALYLLGLAAFQQGDYAE 103
MecR1 COG4219
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ...
 55-147 1.92e-03

Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms];


Pssm-ID: 443363 [Multi-domain]  Cd Length: 337  Bit Score: 40.42  E-value: 1.92e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  55 YYVRQLRGSAPLINDPLLTQYINSLGMRLVSHAN-------SVKTPFhfflinndeinAFAFFGGNVVLHSALFRYSDNE 127
Cdd:COG4219  17 LRLRRLLRRARPVTDEELLELLERLARRLGIRRPvrllesdRITSPF-----------SFGLLRPVILLPAGLEELSEEE 85

                        90       100
                ....*....|....*....|
gi 16130419 128 sqLASVMAHEISHVTQRHLA 147
Cdd:COG4219  86 --LEAILAHELAHIRRRDLL 103
PRK03001 PRK03001
zinc metalloprotease HtpX;
97-247 2.60e-03

zinc metalloprotease HtpX;


Pssm-ID: 179524 [Multi-domain]  Cd Length: 283  Bit Score: 39.62  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419   97 FLINNDEINAFAFfGGN-----VVLHSALFRYSdNESQLASVMAHEISHVTQRHL-----------ARAM---------- 150
Cdd:PRK03001  88 YLINEDQPNAFAT-GRNpehaaVAATTGILRVL-SEREIRGVMAHELAHVKHRDIlistisatmagAISAlanfamffgg 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  151 --EDQQRSAPLTwvgalgSILLAMASPQAgmaaltgtlAGTRQGMISFTQqnEQEADRIGIQVlqrSGfDPQAMPTFLEK 228
Cdd:PRK03001 166 rdENGRPVNPIA------GIAVAILAPLA---------ASLIQMAISRAR--EFEADRGGARI---SG-DPQALASALDK 224

                        170
                 ....*....|....*....
gi 16130419  229 LLDQARysSRPPEILLTHP 247
Cdd:PRK03001 225 IHRYAS--GIPFQAAEAHP 241
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
319-402 3.67e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 36.69  E-value: 3.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 319 AMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLRTNPVLQLNLANAYLQGGQPQEAANI 398
Cdd:COG3063   2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALEKALKLDPNNAEALLNLAELLLELGDYDEALAY 81


                ....
gi 16130419 399 LNRY 402
Cdd:COG3063  82 LERA 85
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 311-396 3.86e-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: 40.07  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419   311 AQYGRALQAMEANKYDEARKTLQPLLAAEPGNAWYLDLATDIDLGQNKANEAINRLKNARDLR-TNPVLQLNLANAYLQG 389
Cdd:TIGR02917 161 AKLGLAQLALAENRFDEARALIDEVLTADPGNVDALLLKGDLLLSLGNIELALAAYRKAIALRpNNIAVLLALATILIEA 240


                  ....*..
gi 16130419   390 GQPQEAA 396
Cdd:TIGR02917 241 GEFEEAE 247
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
345-442 5.75e-03

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


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 38.32  E-value: 5.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419 345 YLDLAtDIDLGQNKANEAINRLKNA--RDLRTNPVLQLNLANAYLQGGQPQEAANILNRYTFNNKD--DSNGWDLLAQAE 420
Cdd:COG4700  92 RVRLA-DALLELGRYDEAIELYEEAltGIFADDPHILLGLAQALFELGRYAEALETLEKLIAKNPDfkSSDAHLLYARAL 170

                        90       100
                ....*....|....*....|..
gi 16130419 421 AALNNRDqelAARAEGYALAGR 442
Cdd:COG4700 171 EALGDLE---AAEAELEALARR 189
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
 307-434 6.21e-03

tetratricopeptide repeat protein; Provisional


Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 39.02  E-value: 6.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130419  307 QQRAAQYG--RALQAMEANKYDEARKTLQPLLAAEPGNA-WYLDLAtDIDLGQNKANEAINRLKNArdLRTNP-----VL 378
Cdd:PRK11788 176 RVEIAHFYceLAQQALARGDLDAARALLKKALAADPQCVrASILLG-DLALAQGDYAAAIEALERV--EEQDPeylseVL 252

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130419  379 QLnLANAYLQGGQPQEAANILNRYTfnnkDDSNGWDLLAQAEAALNNRDQELAARA 434
Cdd:PRK11788 253 PK-LMECYQALGDEAEGLEFLRRAL----EEYPGADLLLALAQLLEEQEGPEAAQA 303
 
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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