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Conserved domains on  [gi|544825812|ref|WP_021241809|]
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MULTISPECIES: beta-barrel assembly-enhancing protease [Enterobacter]

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 11469162)

tetratricopeptide repeat (TPR) protein may adopt a right-handed helical structure with an amphipathic channel and may function as an interaction scaffold in the formation of multi-protein complexes

CATH:  1.25.40.10
Gene Ontology:  GO:0005515
PubMed:  10517866|30708253
SCOP:  3001345

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 2.31e-62

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: 200.80  E-value: 2.31e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  48 QEMQMGDYYVRQLRGSAPLINDPLLVQYINGLGMRLVAHADSVKTPFHFYLINNDEINAFAFFGGNVVLHSALFRYSDNE 127
Cdd:cd07333    1 QEVELGKQFAQQIRQQLPLVEDPEVNEYVNRIGQRLAAVSPRPPFPYRFFVVNDDSINAFATPGGYIYVNTGLILAADNE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 128 SQLASVMAHEISHVTQRHLARAMEDqkrnapltwvgalgsillamaspqagmaaltgtlagtrqgmiSFTQQNEQEADRI 207
Cdd:cd07333   81 AELAGVLAHEIGHVVARHIAKQIEK------------------------------------------SYSREDEREADQL 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544825812 208 GIQVLQRSGFDPQAMPSFLEKLLDQARYS-SRPPEILLTHPLPESRLSDARNRANQ 262
Cdd:cd07333  119 GLQYLTKAGYDPRGMVSFFKKLRRKEWFGgSSIPTYLSTHPAPAERIAYLEELIAS 174
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 307-439 3.37e-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: 66.75  E-value: 3.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 307 EKNAAQYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDVR-TNPVLQLNLANA 385
Cdd:COG4783    2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDpDEPEARLNLGLA 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 544825812 386 YLQGGQPGEAATILNRYTFNNKDDQNGWDLLAQAEAQLGNRDQELAARAEGFAL 439
Cdd:COG4783   82 LLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALEL 135
 
Name Accession Description Interval E-value
M48C_bepA_like cd07333
Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase ...
 48-262 2.31e-62

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: 200.80  E-value: 2.31e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  48 QEMQMGDYYVRQLRGSAPLINDPLLVQYINGLGMRLVAHADSVKTPFHFYLINNDEINAFAFFGGNVVLHSALFRYSDNE 127
Cdd:cd07333    1 QEVELGKQFAQQIRQQLPLVEDPEVNEYVNRIGQRLAAVSPRPPFPYRFFVVNDDSINAFATPGGYIYVNTGLILAADNE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 128 SQLASVMAHEISHVTQRHLARAMEDqkrnapltwvgalgsillamaspqagmaaltgtlagtrqgmiSFTQQNEQEADRI 207
Cdd:cd07333   81 AELAGVLAHEIGHVVARHIAKQIEK------------------------------------------SYSREDEREADQL 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544825812 208 GIQVLQRSGFDPQAMPSFLEKLLDQARYS-SRPPEILLTHPLPESRLSDARNRANQ 262
Cdd:cd07333  119 GLQYLTKAGYDPRGMVSFFKKLRRKEWFGgSSIPTYLSTHPAPAERIAYLEELIAS 174
COG4784 COG4784
Putative Zn-dependent protease [General function prediction only];
1-262 9.85e-44

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


Pssm-ID: 443814 [Multi-domain]  Cd Length: 488  Bit Score: 160.83  E-value: 9.85e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812   1 MFRQLRKTLVATLIAAVTVgqVLPAFAdssdTLPDMGTTAGSTLSIGQEMQMGDYYVRQLRGS-APLINDPLLVQYINGL 79
Cdd:COG4784    1 MRRRRRRALRLLLALALAL--LLAGCA----TNPVTGKRDLVLMSEEQEIAIGAEEHPRILAQyGGAYDDPKLQAYVARV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  80 GMRLVAHADSVKTPFHFYLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMEDQKRNApl 159
Cdd:COG4784   75 GQRLAAASHRPDLPYTFTVLDSPVVNAFALPGGYVYVTRGLLALANDEAELAAVLGHEIGHVTARHAVQRQSRATAAQ-- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 160 twvGALGSILLAM-ASPQAGMAAltgtLAGTRQGMISFTQQNEQEADRIGIQVLQRSGFDPQAMPSFLEKLLDQARYSSR 238
Cdd:COG4784  153 ---IGLGRVLSPVlGSAQAGQLA----GAGAQLLLASFSRDQELEADRLGVRYLARAGYDPYAMARFLGSLKRQSAFRAR 225

                        250       260       270
                 ....*....|....*....|....*....|...
gi 544825812 239 P---------PEILLTHPLPESRLSDARNRANQ 262
Cdd:COG4784  226 LagregrrsyPDFLSTHPDTPDRVQRAVAAARQ 258
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 70-260 1.11e-26

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: 106.75  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812   70 PLLVQYINGLGMRLVAHADSVKTPFHFYLIN-NDEINAFAFF---GGNVVLHSALFRYSDNESQLASVMAHEISHVTQRH 145
Cdd:pfam01435   1 PLRNAELQRVVERLAAAAGLPLPPWYVVVIKsSPVPNAFAYGllpGGRVVVTTGLLDLLETEDELAAVLGHEIGHIKARH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  146 LARAMEDQKRNAPLTWVGALGSILLAM---ASPQAGMAALTGTLAGTRQGMI-SFTQQNEQEADRIGIQVLQRSGFDPQA 221
Cdd:pfam01435  81 SVESLSIMGGLSLAQLFLALLLLGAAAsgfANFGIIFLLLIGPLAALLTLLLlPYSRAQEYEADRLGAELMARAGYDPRA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 544825812  222 MPSFLEK--LLDQARYSSRPPEILLTHPLPESRLSDARNRA 260
Cdd:pfam01435 161 LIKLWGEidNNGRASDGALYPELLSTHPSLVERIAALRERA 201
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 307-439 3.37e-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: 66.75  E-value: 3.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 307 EKNAAQYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDVR-TNPVLQLNLANA 385
Cdd:COG4783    2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDpDEPEARLNLGLA 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 544825812 386 YLQGGQPGEAATILNRYTFNNKDDQNGWDLLAQAEAQLGNRDQELAARAEGFAL 439
Cdd:COG4783   82 LLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALEL 135
TPR_19 pfam14559
Tetratricopeptide repeat;
356-418 4.11e-06

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 44.11  E-value: 4.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544825812  356 QKKPADAINRLKGA-KDVRTNPVLQLNLANAYLQGGQPGEAATILNRYTFNNKDDQNGWDLLAQ 418
Cdd:pfam14559   1 EGDYAEALELLEQAlAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAK 64
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
 297-434 1.26e-05

tetratricopeptide repeat protein; Provisional


Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 47.50  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 297 LDALAKGNVReKNAAQYG--QALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDvrT 374
Cdd:PRK11788 167 LEKLGGDSLR-VEIAHFYceLAQQALARGDLDAARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEALERVEE--Q 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825812 375 NP-----VLQLnLANAYLQGGQPGEAATILNRYTfnnkDDQNGWDL---LAQAEAQLGNRDqelAARA 434
Cdd:PRK11788 244 DPeylseVLPK-LMECYQALGDEAEGLEFLRRAL----EEYPGADLllaLAQLLEEQEGPE---AAQA 303
PRK01345 PRK01345
heat shock protein HtpX; Provisional
 97-234 4.43e-05

heat shock protein HtpX; Provisional


Pssm-ID: 234944 [Multi-domain]  Cd Length: 317  Bit Score: 45.39  E-value: 4.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  97 YLINNDEINAFAFfGGN-----VVLHSALFRYSDNEsQLASVMAHEISHVTQRH---------LARAM------------ 150
Cdd:PRK01345  88 YIIDNPQPNAFAT-GRNpenaaVAATTGLLQRLSPE-EVAGVMAHELAHVKNRDtltmtitatLAGAIsmlanfafffgg 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 151 EDQKRNAPLtwvGALGSILLAMASPQAGMAAltgtlagtrQGMISFTQqnEQEADRIGIQVLQrsgfDPQAMPSFLEKLL 230
Cdd:PRK01345 166 NRENNNGPL---GLVGTLAAMIVAPLAAMLV---------QMAISRTR--EYAADRRGAEICG----NPLWLASALGKIE 227


                 ....
gi 544825812 231 DQAR 234
Cdd:PRK01345 228 RGAH 231
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 310-432 5.86e-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: 5.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  310 AAQYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRL-KGAKDVRTNPVLQLNLANAYLQ 388
Cdd:TIGR02917 500 PAAANLARIDIQEGNPDDAIQRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLeKAAELNPQEIEPALALAQYYLG 579

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 544825812  389 GGQPGEAATILNRYTFNNKDDQNGWDLLAQAEAQLGNRDQELAA 432
Cdd:TIGR02917 580 KGQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSS 623
 
Name Accession Description Interval E-value
M48C_bepA_like cd07333
Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase ...
 48-262 2.31e-62

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: 200.80  E-value: 2.31e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  48 QEMQMGDYYVRQLRGSAPLINDPLLVQYINGLGMRLVAHADSVKTPFHFYLINNDEINAFAFFGGNVVLHSALFRYSDNE 127
Cdd:cd07333    1 QEVELGKQFAQQIRQQLPLVEDPEVNEYVNRIGQRLAAVSPRPPFPYRFFVVNDDSINAFATPGGYIYVNTGLILAADNE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 128 SQLASVMAHEISHVTQRHLARAMEDqkrnapltwvgalgsillamaspqagmaaltgtlagtrqgmiSFTQQNEQEADRI 207
Cdd:cd07333   81 AELAGVLAHEIGHVVARHIAKQIEK------------------------------------------SYSREDEREADQL 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 544825812 208 GIQVLQRSGFDPQAMPSFLEKLLDQARYS-SRPPEILLTHPLPESRLSDARNRANQ 262
Cdd:cd07333  119 GLQYLTKAGYDPRGMVSFFKKLRRKEWFGgSSIPTYLSTHPAPAERIAYLEELIAS 174
M48C_Oma1-like cd07324
Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 ...
 75-258 3.41e-52

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: 173.13  E-value: 3.41e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  75 YINGLGMRLVAHADSVKTPFHFYLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMEdqk 154
Cdd:cd07324    1 YLNRLGDRLAAASGRPDLPYRFFVVDDPSINAFALPGGYIFVTTGLLLLLESEDELAAVLAHEIGHVTLRHIARQLE--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 155 rnapltwvgalgsillamaspqagmaaltgtlagtrqgmiSFTQQNEQEADRIGIQVLQRSGFDPQAMPSFLEKLLDQAR 234
Cdd:cd07324   78 ----------------------------------------RYSRDQEREADRLGLQLLARAGYDPRGMARFFERLARQEG 117

                        170       180
                 ....*....|....*....|....*
gi 544825812 235 YS-SRPPEILLTHPLPESRLSDARN 258
Cdd:cd07324  118 LSgSRLPEFLSTHPLTAERIAALRA 142
COG4784 COG4784
Putative Zn-dependent protease [General function prediction only];
1-262 9.85e-44

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


Pssm-ID: 443814 [Multi-domain]  Cd Length: 488  Bit Score: 160.83  E-value: 9.85e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812   1 MFRQLRKTLVATLIAAVTVgqVLPAFAdssdTLPDMGTTAGSTLSIGQEMQMGDYYVRQLRGS-APLINDPLLVQYINGL 79
Cdd:COG4784    1 MRRRRRRALRLLLALALAL--LLAGCA----TNPVTGKRDLVLMSEEQEIAIGAEEHPRILAQyGGAYDDPKLQAYVARV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  80 GMRLVAHADSVKTPFHFYLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMEDQKRNApl 159
Cdd:COG4784   75 GQRLAAASHRPDLPYTFTVLDSPVVNAFALPGGYVYVTRGLLALANDEAELAAVLGHEIGHVTARHAVQRQSRATAAQ-- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 160 twvGALGSILLAM-ASPQAGMAAltgtLAGTRQGMISFTQQNEQEADRIGIQVLQRSGFDPQAMPSFLEKLLDQARYSSR 238
Cdd:COG4784  153 ---IGLGRVLSPVlGSAQAGQLA----GAGAQLLLASFSRDQELEADRLGVRYLARAGYDPYAMARFLGSLKRQSAFRAR 225

                        250       260       270
                 ....*....|....*....|....*....|...
gi 544825812 239 P---------PEILLTHPLPESRLSDARNRANQ 262
Cdd:COG4784  226 LagregrrsyPDFLSTHPDTPDRVQRAVAAARQ 258
M48C_Oma1_like cd07331
Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 76-263 1.35e-35

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: 130.77  E-value: 1.35e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  76 INGLGMRLVAHAD-----SVKTPFHFYLINNDEINAFAFFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAM 150
Cdd:cd07331    1 VRRVAARLIAAAGddppqSAGWDWEVHVIDSPEVNAFVLPGGKIFVFTGLLPVAKNDDELAAVLGHEIAHALARHSAERM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 151 EDQKrnapltWVGALGSILLAMA-SPQAGMAALTGTLAGTRQGMISFTQQNEQEADRIGIQVLQRSGFDPQAMPSFLEKl 229
Cdd:cd07331   81 SQQK------LLQLLLLLLLAALgASLAGLALGLLGLGAQLGLLLPYSRKQELEADRIGLQLMAKAGYDPRAAVTFWEK- 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 544825812 230 LDQARYSSRPPEILLTHPLPESRLSDARNRANQM 263
Cdd:cd07331  154 MAAAEGGGKPPEFLSTHPSSETRIEALEELLPEA 187
M48C_Oma1_like cd07332
Peptidase M48C Ste24p, integral membrane endopeptidase; This subfamily contains peptidase M48C ...
 49-258 1.57e-31

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: 120.76  E-value: 1.57e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  49 EMQMGDYYVRQLRGSAPLINDPLL--VQYINGLGMRLVAHADSvKTPFHFYLIN-NDEINAFAFFGGNVVLHSALFRYSD 125
Cdd:cd07332   21 EEKLGEQTLELLDETLLEPSELPAerQAALQQLFARLLAALPL-PYPYRLHFRDsGIGANAFALPGGTIVVTDGLVELAE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 126 NESQLASVMAHEISHVTQRHLARAMedqKRNApltwvgALGSILLAMASPQAGMAALTGTLAGTRQGMiSFTQQNEQEAD 205
Cdd:cd07332  100 SPEELAAVLAHEIGHVEHRHSLRQL---IRSS------GLSLLVSLLTGDVSGLSDLLAGLPALLLSL-SYSRDFEREAD 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 544825812 206 RIGIQVLQRSGFDPQAMPSFLEKLLDQARYSSRPPEILLTHPLPESRLSDARN 258
Cdd:cd07332  170 AFALELLKAAGISPEGLADFFERLEEEHGDGGSLPEWLSTHPDTEERIEAIRE 222
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 70-260 1.11e-26

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: 106.75  E-value: 1.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812   70 PLLVQYINGLGMRLVAHADSVKTPFHFYLIN-NDEINAFAFF---GGNVVLHSALFRYSDNESQLASVMAHEISHVTQRH 145
Cdd:pfam01435   1 PLRNAELQRVVERLAAAAGLPLPPWYVVVIKsSPVPNAFAYGllpGGRVVVTTGLLDLLETEDELAAVLGHEIGHIKARH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  146 LARAMEDQKRNAPLTWVGALGSILLAM---ASPQAGMAALTGTLAGTRQGMI-SFTQQNEQEADRIGIQVLQRSGFDPQA 221
Cdd:pfam01435  81 SVESLSIMGGLSLAQLFLALLLLGAAAsgfANFGIIFLLLIGPLAALLTLLLlPYSRAQEYEADRLGAELMARAGYDPRA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 544825812  222 MPSFLEK--LLDQARYSSRPPEILLTHPLPESRLSDARNRA 260
Cdd:pfam01435 161 LIKLWGEidNNGRASDGALYPELLSTHPSLVERIAALRERA 201
M48C_loiP_like cd07334
Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase ...
 43-259 5.93e-19

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: 85.33  E-value: 5.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  43 TLSIGQEMQMGDYYVRQLRGSAPL--INDPL---LVQYINGLGmrlvaHADSVKTPFHFYLinNDEINAFAFFGGNVVLH 117
Cdd:cd07334   10 TLSDEEVKALAAQSAAQMDAKNPVapANSPYakrLARLTKGLK-----SYDGLPLNFKVYL--TPDVNAFAMADGSVRVY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 118 SALF-RYSDNEsqLASVMAHEISHVTQRHLARAMedqkRNAPLTwvgalgSILLAMASPQAG-MAALT----GTLAgtrQ 191
Cdd:cd07334   83 SGLMdMMTDDE--LLGVIGHEIGHVKLGHSKKAM----KTAYLT------SAARKAAASASGtVGALSdsqlGALA---E 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 192 GMIS--FTQQNEQEADRIGIQVLQRSGFDPQAMPSFLEKLldQARYSSRPPEILLTHPLPESRLSDARNR 259
Cdd:cd07334  148 KLINaqFSQKQESEADDYGYKFLKKNGYNPQAAVSALEKL--AALSGGGKSSLFSSHPDPAKRAERIRAR 215
M48C_Oma1_like cd07342
M48C peptidase, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 96-253 3.62e-17

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: 78.45  E-value: 3.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  96 FYLINNDEINAFAFfGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHLARAMedqkrnapltWVGALGSILLAMAsp 175
Cdd:cd07342   23 VELGNSDGVNAYAD-GRRVQITSGMMDFAQDDDELALVVAHELAHNILGHRDRLR----------ANGVAGGLLDGFG-- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 176 qAGMAaltgtlagtrqgmisFTQQNEQEADRIGIQVLQRSGFDPQAMPSFLEKLLdqarySSRPPEILL--THPLPESRL 253
Cdd:cd07342   90 -GNAA---------------YSREFEIEADYLGLYLMARAGYDIDGAADFWRRLG-----ASHPVGIGRaaTHPSTAERF 148
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 307-439 3.37e-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: 66.75  E-value: 3.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 307 EKNAAQYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDVR-TNPVLQLNLANA 385
Cdd:COG4783    2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDpDEPEARLNLGLA 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 544825812 386 YLQGGQPGEAATILNRYTFNNKDDQNGWDLLAQAEAQLGNRDQELAARAEGFAL 439
Cdd:COG4783   82 LLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALEL 135
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 82-265 4.96e-12

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


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 64.91  E-value: 4.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  82 RLVAHADsVKTPfHFYLINNDEINAFAF-FGGN---VVLHSALFRYSDnESQLASVMAHEISHVTQRH------------ 145
Cdd:COG0501   10 ELAARAG-IPMP-EVYVMDSPAPNAFATgRGPNnarIVVTDGLLELLD-RDELEAVLAHELGHIKNGDillmtlasgllg 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 146 -------LARAMEDQKRNAPLtwvgaLGSILLAMASPQAGMAAltgtlagtrQGMISftQQNEQEADRIGIQVLQrsgfD 218
Cdd:COG0501   87 ligflarLLPLAFGRDRDAGL-----LLGLLLGILAPFLATLI---------QLALS--RKREYEADRAAAELTG----D 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825812 219 PQAMPSFLEKLldqARYSSRPPE--------------------ILLTHPLPESRLSDARNRANQMRP 265
Cdd:COG0501  147 PDALASALRKL---AGGNLSIPLrrafpaqahafiinplklssLFSTHPPLEERIARLRELAAEGEY 210
M48B_HtpX_like cd07337
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 72-240 1.57e-07

Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not.


Pssm-ID: 320696 [Multi-domain]  Cd Length: 203  Bit Score: 51.93  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  72 LVQYINGLGMRLVAHADSVKtpfhFYLINNDEINAFAfFGGNVVLHSALFRYSDNESQLASVMAHEISHVTQRHlarame 151
Cdd:cd07337   41 INPELEDKARRLGPDPEKVK----LFISDDEYPNAFA-LGRNTICVTKGLLDLLDYEELKGILAHELGHLSHKD------ 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 152 dqkrnaplTWVGALGSILLAMaspqAGMAALTGTLAGTRQGMIS---FTQQNEQEADR----IG-----IQVLQRSGFDP 219
Cdd:cd07337  110 --------TDYLLLIFVLLLL----AAIWTKLGTLLIFVWIRLLvmfSSRKAEYRADAfavkIGygeglRSALDQLREYE 177

                        170       180
                 ....*....|....*....|.
gi 544825812 220 QAMPSFLEKLldqarYSSRPP 240
Cdd:cd07337  178 DAPKGFLAAL-----YSTHPP 193
M48_Ste24p_like cd07325
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 96-249 4.04e-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: 50.30  E-value: 4.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  96 FYLINNDEINAFAF-FGGN--VVLHSALFRYSDnESQLASVMAHEISHVTQRH-----LARAMEDQKRNAPLTWVG-ALG 166
Cdd:cd07325   34 LYVYQSPVLNAFALgFEGRpfIVLNSGLVELLD-DDELRFVIGHELGHIKSGHvlyrtLLLLLLLLGELIGILLLSsALP 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 167 SILLA---MA-------------SPQAGMAALTGtLAGtrqGMISFTQQNEQEAdrigiqvLQRSGFDPQAMPSFLEKLL 230
Cdd:cd07325  113 LALLAwsrAAeysadragllvcqDPEAAIRALMK-LAG---GSKLLKDVNNIEY-------FLEEEAQADALDGFFKWLS 181

                        170
                 ....*....|....*....
gi 544825812 231 dqaryssrppEILLTHPLP 249
Cdd:cd07325  182 ----------ELLSTHPFL 190
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 294-432 5.47e-07

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 52.30  E-value: 5.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 294 SDLLDALAKGNVREKNAAQYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDVR 373
Cdd:COG3914   63 AAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALN 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 374 -TNPVLQLNLANAYLQGGQPGEAATILNRYTFNNKDDQNGWDLLAQAEAQLGNRDQELAA 432
Cdd:COG3914  143 pDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAA 202
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 307-432 7.08e-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: 50.88  E-value: 7.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 307 EKNAAQYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRL-KGAKDVRTNPVLQLNLANA 385
Cdd:COG2956   74 DRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLeRLLKLGPENAHAYCELAEL 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 544825812 386 YLQGGQPGEAATILNRYTFNNKDDQNGWDLLAQAEAQLGNRDQELAA 432
Cdd:COG2956  154 YLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAA 200
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 311-431 7.96e-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: 7.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 311 AQYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGA--KDVRTNPVLqLNLANAYLQ 388
Cdd:COG2956  146 AYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERAleQDPDYLPAL-PRLAELYEK 224

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 544825812 389 GGQPGEAATILNRYtFNNKDDQNGWDLLAQAEAQLGNRDQELA 431
Cdd:COG2956  225 LGDPEEALELLRKA-LELDPSDDLLLALADLLERKEGLEAALA 266
M48B_HtpX_like cd07338
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 84-253 2.01e-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: 48.73  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  84 VAHADSVKTPfHFYLINNDEINAFAF----FGGNVVLHSALFRYSdNESQLASVMAHEISHVtqRHlaramedqKRNAPL 159
Cdd:cd07338   42 VARRAGIKPP-KVGIAEDPIPNAFAYgsplTGARVAVTRGLLDIL-NRDELEAVIGHELGHI--KH--------RDVAIM 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 160 TWVGALGSIL--LAMASPQAGMAALTGTLAGTR--------------QGMI-SFTQQNEQEADRIGIQVLQrsgfDPQAM 222
Cdd:cd07338  110 TAIGLIPSIIyyIGRSLLFSGGSSGGRNGGGALlavgiaafavyflfQLLVlGFSRLREYYADAHSAKVTG----NGRAL 185

                        170       180       190
                 ....*....|....*....|....*....|.
gi 544825812 223 PSFLEKLldqARYSSRppEILLTHPLPESRL 253
Cdd:cd07338  186 QSALAKI---AYGYLA--EIFSTHPLPAKRI 211
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
314-480 2.22e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.85  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 314 GQALQAMEasKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDVR-TNPVLQLNLANAYLQGGQP 392
Cdd:COG0457   49 GLAYLRLG--RYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDpDDAEALYNLGLALLELGRY 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 393 GEAATILNRYTFNNKDDQNGWDLLAQAEAQLGNRDQELAARAEGFALVGRLDQAISALSSASSQVKLGSLQQARYDARID 472
Cdd:COG0457  127 DEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQA 206


                 ....*...
gi 544825812 473 QLRGLQQR 480
Cdd:COG0457  207 LRKKLAIL 214
TPR_19 pfam14559
Tetratricopeptide repeat;
356-418 4.11e-06

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 44.11  E-value: 4.11e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544825812  356 QKKPADAINRLKGA-KDVRTNPVLQLNLANAYLQGGQPGEAATILNRYTFNNKDDQNGWDLLAQ 418
Cdd:pfam14559   1 EGDYAEALELLEQAlAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAK 64
Peptidase_M48_M56 cd05843
Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral ...
 87-147 4.16e-06

Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral membrane metallopeptidases; This family contains peptidase M48 (also known as Ste24 peptidase, Ste24p, Ste24 endopeptidase, a-factor converting enzyme, AFC1), M56 (also known as BlaR1 peptidase) as well as a novel family called minigluzincins. Peptidase M48 belongs to Ste24 endopeptidase family. Members of this family include Ste24 protease (peptidase M48A), protease htpX homolog (peptidase M48B), or CAAX prenyl protease 1, and mitochondrial metalloendopeptidase OMA1 (peptidase M48C). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. The Ste24p contains multiple membrane spans, a zinc metalloprotease motif (HEXXH), and a COOH-terminal ER retrieval signal (KKXX). Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Ste24p has limited homology to HtpX family of prokaryotic proteins; HtpX proteins, also part of the M48 peptidase family, are smaller and homology is restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins; HtpX then undergoes self-degradation and collaborates with FtsH to eliminate these misfolded proteins. Peptidase M56 includes zinc metalloprotease domain in MecR1 and BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain beta-lactam antibiotics in MRSA. Also included are a novel family of related proteins that consist of the soluble minimal scaffold similar to the catalytic domains of the integral-membrane metallopeptidase M48 and M56, thus called minigluzincins.


Pssm-ID: 320682 [Multi-domain]  Cd Length: 94  Bit Score: 45.13  E-value: 4.16e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544825812  87 ADSVKTPF--HFYLINNDEINAFAFFGGN--VVLHSALFRySDNESQLASVMAHEISHVTQRHLA 147
Cdd:cd05843    9 LLSAGAFPldKVVVVPGSVPNAFFTGGANkrVVLTTALLE-LLSEEELAAVIAHELGHFKAHEYQ 72
M56_like cd07329
Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains ...
 97-254 4.42e-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: 47.06  E-value: 4.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  97 YLINNDEINAFA---FFGGNVVLHSALFRySDNESQLASVMAHEISHVTQRH----------------LARAMEDQKRNA 157
Cdd:cd07329   15 YVVDSDVPNAFAvgrSRGPTVVVTTGLLD-LLDDDELEAVLAHELAHLKRRDvlvlllfdpllllvvgLLLFLSLFIFEL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 158 PLTWVGALGSILLAMASPQAGMAALTGTLAGTRqgmisftqqNEQEADRIGiqvlqrsgfDPQAMPSFLEKLLDQARY-- 235
Cdd:cd07329   94 LGFFFQPLLFLAFFALLRLAELLADALAVARTS---------AARRARLTG---------LPAALASALEKIEDASDRal 155

                        170       180
                 ....*....|....*....|....*....
gi 544825812 236 ----------SSRPPEILLTHPLPESRLS 254
Cdd:cd07329  156 eaglvlpalaADASSLEKTDHPPLEERVE 184
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
 297-434 1.26e-05

tetratricopeptide repeat protein; Provisional


Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 47.50  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 297 LDALAKGNVReKNAAQYG--QALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDvrT 374
Cdd:PRK11788 167 LEKLGGDSLR-VEIAHFYceLAQQALARGDLDAARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEALERVEE--Q 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825812 375 NP-----VLQLnLANAYLQGGQPGEAATILNRYTfnnkDDQNGWDL---LAQAEAQLGNRDqelAARA 434
Cdd:PRK11788 244 DPeylseVLPK-LMECYQALGDEAEGLEFLRRAL----EEYPGADLllaLAQLLEEQEGPE---AAQA 303
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 299-402 2.63e-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: 45.88  E-value: 2.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 299 ALAKGNVReknaAQYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDVRTNPVL 378
Cdd:COG2956  172 KLDPDCAR----ALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDL 247

                         90       100
                 ....*....|....*....|....
gi 544825812 379 QLNLANAYLQGGQPGEAATILNRY 402
Cdd:COG2956  248 LLALADLLERKEGLEAALALLERQ 271
PRK01345 PRK01345
heat shock protein HtpX; Provisional
 97-234 4.43e-05

heat shock protein HtpX; Provisional


Pssm-ID: 234944 [Multi-domain]  Cd Length: 317  Bit Score: 45.39  E-value: 4.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  97 YLINNDEINAFAFfGGN-----VVLHSALFRYSDNEsQLASVMAHEISHVTQRH---------LARAM------------ 150
Cdd:PRK01345  88 YIIDNPQPNAFAT-GRNpenaaVAATTGLLQRLSPE-EVAGVMAHELAHVKNRDtltmtitatLAGAIsmlanfafffgg 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 151 EDQKRNAPLtwvGALGSILLAMASPQAGMAAltgtlagtrQGMISFTQqnEQEADRIGIQVLQrsgfDPQAMPSFLEKLL 230
Cdd:PRK01345 166 NRENNNGPL---GLVGTLAAMIVAPLAAMLV---------QMAISRTR--EYAADRRGAEICG----NPLWLASALGKIE 227


                 ....
gi 544825812 231 DQAR 234
Cdd:PRK01345 228 RGAH 231
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 310-409 5.83e-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: 42.87  E-value: 5.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 310 AAQYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDVR-TNPVLQLNLANAYLQ 388
Cdd:COG4783   39 EAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDpEHPEAYLRLARAYRA 118

                         90       100
                 ....*....|....*....|.
gi 544825812 389 GGQPGEAATILNRYTFNNKDD 409
Cdd:COG4783  119 LGRPDEAIAALEKALELDPDD 139
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 327-428 5.85e-05

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: 42.69  E-value: 5.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 327 EARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRL-KGAKDVRTNPVLQLNLANAYLQGGQPGEAATILNRYTFN 405
Cdd:COG4235    1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYeKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL 80

                         90       100
                 ....*....|....*....|...
gi 544825812 406 NKDDQNGWDLLAQAEAQLGNRDQ 428
Cdd:COG4235   81 DPDNPEALYLLGLAAFQQGDYAE 103
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 310-432 5.86e-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: 5.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  310 AAQYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRL-KGAKDVRTNPVLQLNLANAYLQ 388
Cdd:TIGR02917 500 PAAANLARIDIQEGNPDDAIQRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLeKAAELNPQEIEPALALAQYYLG 579

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 544825812  389 GGQPGEAATILNRYTFNNKDDQNGWDLLAQAEAQLGNRDQELAA 432
Cdd:TIGR02917 580 KGQLKKALAILNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSS 623
PRK03001 PRK03001
zinc metalloprotease HtpX;
97-247 8.02e-05

zinc metalloprotease HtpX;


Pssm-ID: 179524 [Multi-domain]  Cd Length: 283  Bit Score: 44.24  E-value: 8.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  97 YLINNDEINAFAFfGGN-----VVLHSALFRYSdNESQLASVMAHEISHVTQRHL-----------ARAM---------- 150
Cdd:PRK03001  88 YLINEDQPNAFAT-GRNpehaaVAATTGILRVL-SEREIRGVMAHELAHVKHRDIlistisatmagAISAlanfamffgg 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 151 --EDQKRNAPLTwvgalgSILLAMASPQAgmaaltgtlAGTRQGMISFTQqnEQEADRIGIQVlqrSGfDPQAMPSFLEK 228
Cdd:PRK03001 166 rdENGRPVNPIA------GIAVAILAPLA---------ASLIQMAISRAR--EFEADRGGARI---SG-DPQALASALDK 224

                        170
                 ....*....|....*....
gi 544825812 229 LLDQARysSRPPEILLTHP 247
Cdd:PRK03001 225 IHRYAS--GIPFQAAEAHP 241
MecR1 COG4219
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ...
 55-147 9.43e-05

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


Pssm-ID: 443363 [Multi-domain]  Cd Length: 337  Bit Score: 44.66  E-value: 9.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  55 YYVRQLRGSAPLINDPLLVQYINGLGMRL-------VAHADSVKTPFhfylinndeinAFAFFGGNVVLHSALFRYSDNE 127
Cdd:COG4219   17 LRLRRLLRRARPVTDEELLELLERLARRLgirrpvrLLESDRITSPF-----------SFGLLRPVILLPAGLEELSEEE 85

                         90       100
                 ....*....|....*....|
gi 544825812 128 sqLASVMAHEISHVTQRHLA 147
Cdd:COG4219   86 --LEAILAHELAHIRRRDLL 103
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
319-402 1.96e-04

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 40.54  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 319 AMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDVRTNPVLQLNLANAYLQGGQPGEAATI 398
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALEKALKLDPNNAEALLNLAELLLELGDYDEALAY 81


                 ....
gi 544825812 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 ...
 311-434 4.02e-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: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  311 AQYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDVRTNPVLQLNLANAYLQGG 390
Cdd:TIGR02917 671 AQIGLAQLLLAAKRTESAKKIAKSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSSQNAIKLHRALLASG 750

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 544825812  391 QPGEAATILNRYTFNNKDDQNGwdLLAQAEAQLGNRDQELAARA 434
Cdd:TIGR02917 751 NTAEAVKTLEAWLKTHPNDAVL--RTALAELYLAQKDYDKAIKH 792
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 312-428 8.67e-04

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: 41.25  E-value: 8.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 312 QYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDV-RTNPVLQLNLANAYLQGG 390
Cdd:COG2956   11 WYFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERdPDRAEALLELAQDYLKAG 90

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 544825812 391 QPGEAATILNRYTFNNKDDQNGWDLLAQAEAQLGNRDQ 428
Cdd:COG2956   91 LLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEK 128
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
311-432 1.45e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 40.38  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 311 AQYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDVR-TNPVLQLNLANAYLQG 389
Cdd:COG0457   10 AYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDpDDAEALNNLGLALQAL 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 544825812 390 GQPGEAATILNRYTFNNKDDQNGWDLLAQAEAQLGNRDQELAA 432
Cdd:COG0457   90 GRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEA 132
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
314-475 3.62e-03

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 39.22  E-value: 3.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 314 GQALQAMEasKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDVR-TNPVLQLNLANAYLQGGQP 392
Cdd:COG0457   83 GLALQALG--RYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDpDDADALYNLGIALEKLGRY 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 393 GEAATILNRYTFNNKDDQNGWDLLAQAEAQLGNRDQELAARAEGFALVGRLDQAISALSSASSQVKLGSLQQARYDARID 472
Cdd:COG0457  161 EEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALAL 240


                 ...
gi 544825812 473 QLR 475
Cdd:COG0457  241 YQY 243
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 306-440 6.58e-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: 38.74  E-value: 6.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 306 REKNAAQYGQALQAMEASKYDEARKALQPLLAADPNN---PWYLDLSTDidlgqkKPADAINRLKGA-KDVRTNPVLQLN 381
Cdd:COG3071  190 RRDPELAAAYARALIALGDHDEAERLLREALKRQWDPrlvRLYGRLQGG------DPAKQLKRAEKWlKKHPNDPDLLLA 263

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 544825812 382 LANAYLQGGQPGEAATILNRyTFNNKDDQNGWDLLAQAEAQLGNRDQELAARAEGFALV 440
Cdd:COG3071  264 LGRLCLRNQLWGKAREYLEA-ALALRPSAEAYAELARLLEQLGDPEEAAEHYRKALALA 321
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 295-401 7.37e-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: 37.25  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 295 DLLDALAKGNVREKNAAQYGQALQAMEASKYDEARKALQPLLAADPNNPWYLDLSTDIDLGQKKPADAINRLKGAKDVR- 373
Cdd:COG5010   40 DELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSp 119

                         90       100
                 ....*....|....*....|....*...
gi 544825812 374 TNPVLQLNLANAYLQGGQPGEAATILNR 401
Cdd:COG5010  120 DNPNAYSNLAALLLSLGQDDEAKAALQR 147
TPR_15 pfam13429
Tetratricopeptide repeat;
294-433 8.46e-03

Tetratricopeptide repeat;


Pssm-ID: 433199 [Multi-domain]  Cd Length: 279  Bit Score: 38.11  E-value: 8.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  294 SDLLDALAKGNVREKNAAQYGQALQAM-----EASKYDEARKALQPLLAADPNNP-------WYLdlstdIDLGQ-KKPA 360
Cdd:pfam13429 125 YDRLARLLASLEELPAAEQSPAFWLARaeyyrQTGEPDAALRDYRRALALAPASTelraallWFL-----IDLGRrAELR 199

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825812  361 DAINRLKGAKDvrTNPVLQLNLANAYLQGGQPGEAATILNRYTFNNKDDQnGWdLLAQAEAQLGNRDQELAAR 433
Cdd:pfam13429 200 PALAAWRARAE--TDADLWGPLAAAYLRLGRPRKALPYLRKQAASNRNDP-LW-LLAYADALEQAGRADAAWR 268
M48B_HtpX_like cd07336
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 97-240 9.78e-03

Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not.


Pssm-ID: 320695 [Multi-domain]  Cd Length: 266  Bit Score: 37.86  E-value: 9.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812  97 YLINNDEINAFAFfGGN-----VVLHSALFRYSDNEsQLASVMAHEISHVTQR----------------HLAR-AM---- 150
Cdd:cd07336   76 YIIPSPQPNAFAT-GRNpehaaVAVTTGILRLLDKD-ELEGVLAHELAHIKNRdilistiaatiagaisMLANmAQwgai 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825812 151 --EDQKRNAPLTWVGALGSILLAmasPqagMAALTGTLAgtrqgmISftQQNEQEADRIGIQVlqrSGfDPQAMPSFLEK 228
Cdd:cd07336  154 fgGRGGRDRGGNPIGALLLAILA---P---IAATLIQLA------IS--RSREYLADETGARI---SG-NPLALASALEK 215

                        170
                 ....*....|..
gi 544825812 229 LldqARYSSRPP 240
Cdd:cd07336  216 L---ERGAQRHP 224
 
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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