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Conserved domains on  [gi|20141001|sp|Q8ZCC3|]
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RecName: Full=Beta-barrel assembly-enhancing protease; Flags: Precursor

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 ...
 46-260 4.02e-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: 197.71  E-value: 4.02e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  46 QEMAMGDFYVRQMRASAPLIYDPLLTQYINTLGNRLVANANSVRTPFHFYLVNNDQINAFAFFGGNVVLHSALFRYTDNE 125
Cdd:cd07333   1 QEVELGKQFAQQIRQQLPLVEDPEVNEYVNRIGQRLAAVSPRPPFPYRFFVVNDDSINAFATPGGYIYVNTGLILAADNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 126 SELASVLAHEISHVTQRHLARAMEEqqrlapltwvgvlgsilltmaspqagmaglsgtlagaqqgiiSFTQGNEQEADRI 205
Cdd:cd07333  81 AELAGVLAHEIGHVVARHIAKQIEK------------------------------------------SYSREDEREADQL 118

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20141001 206 GIQVLQRSGFDPQAMPNFLQKLADQSRYVSK-PPEMLLTHPLPDSRLSDARNRANQ 260
Cdd:cd07333 119 GLQYLTKAGYDPRGMVSFFKKLRRKEWFGGSsIPTYLSTHPAPAERIAYLEELIAS 174
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 305-439 4.85e-17

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: 77.54  E-value: 4.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 305 EQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANA 384
Cdd:COG4783   2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20141001 385 YVQGRQPAAAIKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALS 439
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 ...
 46-260 4.02e-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: 197.71  E-value: 4.02e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  46 QEMAMGDFYVRQMRASAPLIYDPLLTQYINTLGNRLVANANSVRTPFHFYLVNNDQINAFAFFGGNVVLHSALFRYTDNE 125
Cdd:cd07333   1 QEVELGKQFAQQIRQQLPLVEDPEVNEYVNRIGQRLAAVSPRPPFPYRFFVVNDDSINAFATPGGYIYVNTGLILAADNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 126 SELASVLAHEISHVTQRHLARAMEEqqrlapltwvgvlgsilltmaspqagmaglsgtlagaqqgiiSFTQGNEQEADRI 205
Cdd:cd07333  81 AELAGVLAHEIGHVVARHIAKQIEK------------------------------------------SYSREDEREADQL 118

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20141001 206 GIQVLQRSGFDPQAMPNFLQKLADQSRYVSK-PPEMLLTHPLPDSRLSDARNRANQ 260
Cdd:cd07333 119 GLQYLTKAGYDPRGMVSFFKKLRRKEWFGGSsIPTYLSTHPAPAERIAYLEELIAS 174
COG4784 COG4784
Putative Zn-dependent protease [General function prediction only];
23-260 9.75e-46

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


Pssm-ID: 443814 [Multi-domain]  Cd Length: 488  Bit Score: 166.22  E-value: 9.75e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  23 GLLPAQDLLPDIGTSAGATLSIDQEMAMGDFYVRQMRASAPLIY-DPLLTQYINTLGNRLVANANSVRTPFHFYLVNNDQ 101
Cdd:COG4784  19 LLLAGCATNPVTGKRDLVLMSEEQEIAIGAEEHPRILAQYGGAYdDPKLQAYVARVGQRLAAASHRPDLPYTFTVLDSPV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 102 INAFAFFGGNVVLHSALFRYTDNESELASVLAHEISHVTQRHlARAMEEQQRLAPLTWVGVLGSILltmASPQAGMAGls 181
Cdd:COG4784  99 VNAFALPGGYVYVTRGLLALANDEAELAAVLGHEIGHVTARH-AVQRQSRATAAQIGLGRVLSPVL---GSAQAGQLA-- 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 182 gtLAGAQQGIISFTQGNEQEADRIGIQVLQRSGFDPQAMPNFLQKLADQSRYVSKP---------PEMLLTHPLPDSRLS 252
Cdd:COG4784 173 --GAGAQLLLASFSRDQELEADRLGVRYLARAGYDPYAMARFLGSLKRQSAFRARLagregrrsyPDFLSTHPDTPDRVQ 250


                ....*...
gi 20141001 253 DARNRANQ 260
Cdd:COG4784 251 RAVAAARQ 258
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 68-258 2.32e-30

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: 116.76  E-value: 2.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001    68 PLLTQYINTLGNRLVANANSVRTPFHFYLVN-NDQINAFAFF---GGNVVLHSALFRYTDNESELASVLAHEISHVTQRH 143
Cdd:pfam01435   1 PLRNAELQRVVERLAAAAGLPLPPWYVVVIKsSPVPNAFAYGllpGGRVVVTTGLLDLLETEDELAAVLGHEIGHIKARH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001   144 LARAMEEQQRLA-PLTWVGVLGSILLTMASPQAG---MAGLSGTLAGAQQGIISFTQGNEQEADRIGIQVLQRSGFDPQA 219
Cdd:pfam01435  81 SVESLSIMGGLSlAQLFLALLLLGAAASGFANFGiifLLLIGPLAALLTLLLLPYSRAQEYEADRLGAELMARAGYDPRA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 20141001   220 MPNFLQKLADQSRYVS--KPPEMLLTHPLPDSRLSDARNRA 258
Cdd:pfam01435 161 LIKLWGEIDNNGRASDgaLYPELLSTHPSLVERIAALRERA 201
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 305-439 4.85e-17

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: 77.54  E-value: 4.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 305 EQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANA 384
Cdd:COG4783   2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20141001 385 YVQGRQPAAAIKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALS 439
Cdd:COG4783  82 LLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 318-464 1.13e-07

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: 54.32  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001   318 YQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANAYVQGRQPAAAIKL 397
Cdd:TIGR02917 510 IQEGNPDDAIQRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKKALAI 589

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20141001   398 LHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALSGKLTQAIGLLSDASARVK-----LGSLEQA 464
Cdd:TIGR02917 590 LNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKnyakaITSLKRA 661
TPR_19 pfam14559
Tetratricopeptide repeat;
354-417 7.92e-06

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 43.34  E-value: 7.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20141001   354 QNKSAAAIARLQNAMVKQNDEPVLQLNLANAYVQGRQPAAAIKLLHRYTFAYPNDPNGWDLLAQ 417
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAK 64
PRK03001 PRK03001
zinc metalloprotease HtpX;
95-245 6.86e-05

zinc metalloprotease HtpX;


Pssm-ID: 179524 [Multi-domain]  Cd Length: 283  Bit Score: 44.63  E-value: 6.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001   95 YLVNNDQINAFAFfGGN-----VVLHSALFRYTdNESELASVLAHEISHVTQRHL-----------ARAM---------- 148
Cdd:PRK03001  88 YLINEDQPNAFAT-GRNpehaaVAATTGILRVL-SEREIRGVMAHELAHVKHRDIlistisatmagAISAlanfamffgg 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  149 --EEQQRLAPLtwVGVLGSILLTMASPQAGMAglsgtlagaqqgiISFTQgnEQEADRIGIQVlqrSGfDPQAMPNFLQK 226
Cdd:PRK03001 166 rdENGRPVNPI--AGIAVAILAPLAASLIQMA-------------ISRAR--EFEADRGGARI---SG-DPQALASALDK 224

                        170
                 ....*....|....*....
gi 20141001  227 LADQSRyvSKPPEMLLTHP 245
Cdd:PRK03001 225 IHRYAS--GIPFQAAEAHP 241
PRK11447 PRK11447
cellulose synthase subunit BcsC; Provisional
 323-452 9.05e-03

cellulose synthase subunit BcsC; Provisional


Pssm-ID: 183140 [Multi-domain]  Cd Length: 1157  Bit Score: 38.91  E-value: 9.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001   323 YDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANAYVQGRQPAAAIKLLHRyt 402
Cdd:PRK11447  619 YAAARAAYQRVLTREPGNADARLGLIEVDIAQGDLAAARAQLAKLPATANDSLNTQRRVALAWAALGDTAAAQRTFNR-- 696

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 20141001   403 faypndpngwdLLAQATATQGLRDQEL----AARAEslALSGKLTQAIGLLSDA 452
Cdd:PRK11447  697 -----------LIPQAKSQPPSMESALvlrdAARFE--AQTGQPQQALETYKDA 737
 
Name Accession Description Interval E-value
M48C_bepA_like cd07333
Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase ...
 46-260 4.02e-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: 197.71  E-value: 4.02e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  46 QEMAMGDFYVRQMRASAPLIYDPLLTQYINTLGNRLVANANSVRTPFHFYLVNNDQINAFAFFGGNVVLHSALFRYTDNE 125
Cdd:cd07333   1 QEVELGKQFAQQIRQQLPLVEDPEVNEYVNRIGQRLAAVSPRPPFPYRFFVVNDDSINAFATPGGYIYVNTGLILAADNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 126 SELASVLAHEISHVTQRHLARAMEEqqrlapltwvgvlgsilltmaspqagmaglsgtlagaqqgiiSFTQGNEQEADRI 205
Cdd:cd07333  81 AELAGVLAHEIGHVVARHIAKQIEK------------------------------------------SYSREDEREADQL 118

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 20141001 206 GIQVLQRSGFDPQAMPNFLQKLADQSRYVSK-PPEMLLTHPLPDSRLSDARNRANQ 260
Cdd:cd07333 119 GLQYLTKAGYDPRGMVSFFKKLRRKEWFGGSsIPTYLSTHPAPAERIAYLEELIAS 174
M48C_Oma1-like cd07324
Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 ...
 73-256 1.12e-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: 171.59  E-value: 1.12e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  73 YINTLGNRLVANANSVRTPFHFYLVNNDQINAFAFFGGNVVLHSALFRYTDNESELASVLAHEISHVTQRHLARAMEEqq 152
Cdd:cd07324   1 YLNRLGDRLAAASGRPDLPYRFFVVDDPSINAFALPGGYIFVTTGLLLLLESEDELAAVLAHEIGHVTLRHIARQLER-- 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 153 rlapltwvgvlgsilltmaspqagmaglsgtlagaqqgiisFTQGNEQEADRIGIQVLQRSGFDPQAMPNFLQKLADQSR 232
Cdd:cd07324  79 -----------------------------------------YSRDQEREADRLGLQLLARAGYDPRGMARFFERLARQEG 117

                       170       180
                ....*....|....*....|....*
gi 20141001 233 -YVSKPPEMLLTHPLPDSRLSDARN 256
Cdd:cd07324 118 lSGSRLPEFLSTHPLTAERIAALRA 142
COG4784 COG4784
Putative Zn-dependent protease [General function prediction only];
23-260 9.75e-46

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


Pssm-ID: 443814 [Multi-domain]  Cd Length: 488  Bit Score: 166.22  E-value: 9.75e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  23 GLLPAQDLLPDIGTSAGATLSIDQEMAMGDFYVRQMRASAPLIY-DPLLTQYINTLGNRLVANANSVRTPFHFYLVNNDQ 101
Cdd:COG4784  19 LLLAGCATNPVTGKRDLVLMSEEQEIAIGAEEHPRILAQYGGAYdDPKLQAYVARVGQRLAAASHRPDLPYTFTVLDSPV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 102 INAFAFFGGNVVLHSALFRYTDNESELASVLAHEISHVTQRHlARAMEEQQRLAPLTWVGVLGSILltmASPQAGMAGls 181
Cdd:COG4784  99 VNAFALPGGYVYVTRGLLALANDEAELAAVLGHEIGHVTARH-AVQRQSRATAAQIGLGRVLSPVL---GSAQAGQLA-- 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 182 gtLAGAQQGIISFTQGNEQEADRIGIQVLQRSGFDPQAMPNFLQKLADQSRYVSKP---------PEMLLTHPLPDSRLS 252
Cdd:COG4784 173 --GAGAQLLLASFSRDQELEADRLGVRYLARAGYDPYAMARFLGSLKRQSAFRARLagregrrsyPDFLSTHPDTPDRVQ 250


                ....*...
gi 20141001 253 DARNRANQ 260
Cdd:COG4784 251 RAVAAARQ 258
M48C_Oma1_like cd07331
Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 74-261 9.78e-38

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: 136.55  E-value: 9.78e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  74 INTLGNRLVANAN-----SVRTPFHFYLVNNDQINAFAFFGGNVVLHSALFRYTDNESELASVLAHEISHVTQRHLAram 148
Cdd:cd07331   1 VRRVAARLIAAAGddppqSAGWDWEVHVIDSPEVNAFVLPGGKIFVFTGLLPVAKNDDELAAVLGHEIAHALARHSA--- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 149 eEQQRLAPLTWVGVLGSILLTMASPQAGMAGLSGtlAGAQQGIIS-FTQGNEQEADRIGIQVLQRSGFDPQAMPNFLQKL 227
Cdd:cd07331  78 -ERMSQQKLLQLLLLLLLAALGASLAGLALGLLG--LGAQLGLLLpYSRKQELEADRIGLQLMAKAGYDPRAAVTFWEKM 154

                       170       180       190
                ....*....|....*....|....*....|....
gi 20141001 228 ADQSRyVSKPPEMLLTHPLPDSRLSDARNRANQM 261
Cdd:cd07331 155 AAAEG-GGKPPEFLSTHPSSETRIEALEELLPEA 187
M48C_Oma1_like cd07332
Peptidase M48C Ste24p, integral membrane endopeptidase; This subfamily contains peptidase M48C ...
 42-256 5.00e-34

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: 127.69  E-value: 5.00e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  42 LSIDQEMAMGDFYVRQMRASAPLIYDPLLT--QYINTLGNRLVAnANSVRTPFHFYLVN-NDQINAFAFFGGNVVLHSAL 118
Cdd:cd07332  16 LPPSVEEKLGEQTLELLDETLLEPSELPAErqAALQQLFARLLA-ALPLPYPYRLHFRDsGIGANAFALPGGTIVVTDGL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 119 FRYTDNESELASVLAHEISHVTQRHLARAMeeQQRLApltwVGVLGSILLTMASPQAGM-AGLSGTLAGAqqgiiSFTQG 197
Cdd:cd07332  95 VELAESPEELAAVLAHEIGHVEHRHSLRQL--IRSSG----LSLLVSLLTGDVSGLSDLlAGLPALLLSL-----SYSRD 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 20141001 198 NEQEADRIGIQVLQRSGFDPQAMPNFLQKLADQSRYVSKPPEMLLTHPLPDSRLSDARN 256
Cdd:cd07332 164 FEREADAFALELLKAAGISPEGLADFFERLEEEHGDGGSLPEWLSTHPDTEERIEAIRE 222
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 68-258 2.32e-30

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: 116.76  E-value: 2.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001    68 PLLTQYINTLGNRLVANANSVRTPFHFYLVN-NDQINAFAFF---GGNVVLHSALFRYTDNESELASVLAHEISHVTQRH 143
Cdd:pfam01435   1 PLRNAELQRVVERLAAAAGLPLPPWYVVVIKsSPVPNAFAYGllpGGRVVVTTGLLDLLETEDELAAVLGHEIGHIKARH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001   144 LARAMEEQQRLA-PLTWVGVLGSILLTMASPQAG---MAGLSGTLAGAQQGIISFTQGNEQEADRIGIQVLQRSGFDPQA 219
Cdd:pfam01435  81 SVESLSIMGGLSlAQLFLALLLLGAAASGFANFGiifLLLIGPLAALLTLLLLPYSRAQEYEADRLGAELMARAGYDPRA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 20141001   220 MPNFLQKLADQSRYVS--KPPEMLLTHPLPDSRLSDARNRA 258
Cdd:pfam01435 161 LIKLWGEIDNNGRASDgaLYPELLSTHPSLVERIAALRERA 201
M48C_loiP_like cd07334
Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase ...
 40-257 1.79e-21

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: 92.65  E-value: 1.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  40 ATLSIDQEMAMGDFYVRQMRASAPLIydPLLTQYINTLgNRLVAN-ANSVRTPFHF--YLVnnDQINAFAFFGGNVVLHS 116
Cdd:cd07334   9 ATLSDEEVKALAAQSAAQMDAKNPVA--PANSPYAKRL-ARLTKGlKSYDGLPLNFkvYLT--PDVNAFAMADGSVRVYS 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 117 ALF-RYTDNEseLASVLAHEISHVTQRHLARAMeeqqRLAPLTwvgvlgSILLTMASPQAGMAG---------LSGTLAG 186
Cdd:cd07334  84 GLMdMMTDDE--LLGVIGHEIGHVKLGHSKKAM----KTAYLT------SAARKAAASASGTVGalsdsqlgaLAEKLIN 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20141001 187 AQqgiisFTQGNEQEADRIGIQVLQRSGFDPQAMPNFLQKLADQSRyvSKPPEMLLTHPLPDSRLSDARNR 257
Cdd:cd07334 152 AQ-----FSQKQESEADDYGYKFLKKNGYNPQAAVSALEKLAALSG--GGKSSLFSSHPDPAKRAERIRAR 215
M48C_Oma1_like cd07342
M48C peptidase, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 94-245 1.26e-19

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: 85.77  E-value: 1.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  94 FYLVNNDQINAFAFfGGNVVLHSALFRYTDNESELASVLAHEISHVTQRHLARAMeeqqrlapltwvgvlgsilltmasp 173
Cdd:cd07342  23 VELGNSDGVNAYAD-GRRVQITSGMMDFAQDDDELALVVAHELAHNILGHRDRLR------------------------- 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20141001 174 qagMAGLSGTLAGAQQGIISFTQGNEQEADRIGIQVLQRSGFDPQAMPNFLQKLAdqsryVSKPPEMLL--THP 245
Cdd:cd07342  77 ---ANGVAGGLLDGFGGNAAYSREFEIEADYLGLYLMARAGYDIDGAADFWRRLG-----ASHPVGIGRaaTHP 142
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 305-439 4.85e-17

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: 77.54  E-value: 4.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 305 EQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANA 384
Cdd:COG4783   2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLA 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20141001 385 YVQGRQPAAAIKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALS 439
Cdd:COG4783  82 LLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 79-263 9.33e-12

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


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 64.14  E-value: 9.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  79 NRLVANANsVRTPfHFYLVNNDQINAFAF-FGGN---VVLHSALFRYTDnESELASVLAHEISHVTQRH---LARAMeeq 151
Cdd:COG0501   9 EELAARAG-IPMP-EVYVMDSPAPNAFATgRGPNnarIVVTDGLLELLD-RDELEAVLAHELGHIKNGDillMTLAS--- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 152 qrlAPLTWVGVLGSILLTMA--SPQAG------MAGLSGTLAGAQQGIISftQGNEQEADRIGIQVLQrsgfDPQAMPNF 223
Cdd:COG0501  83 ---GLLGLIGFLARLLPLAFgrDRDAGlllgllLGILAPFLATLIQLALS--RKREYEADRAAAELTG----DPDALASA 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20141001 224 LQKLADQSRYVSKPPE-----------------MLLTHPLPDSRLSDARNRANQMKP 263
Cdd:COG0501 154 LRKLAGGNLSIPLRRAfpaqahafiinplklssLFSTHPPLEERIARLRELAAEGEY 210
M48_Ste24p_like cd07325
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 94-247 1.49e-10

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: 60.70  E-value: 1.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  94 FYLVNNDQINAFAF-FGGN--VVLHSALFRYTDnESELASVLAHEISHVTQRH-LARAMeeqqrLAPLTWVGV-LGSILL 168
Cdd:cd07325  34 LYVYQSPVLNAFALgFEGRpfIVLNSGLVELLD-DDELRFVIGHELGHIKSGHvLYRTL-----LLLLLLLGElIGILLL 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 169 TMASPQAGM------------AGL--SGTLAGAQQGIISFTQGNEQEADRIGIQVLQRSGFDPQAMPNFLQKLAdqsryv 234
Cdd:cd07325 108 SSALPLALLawsraaeysadrAGLlvCQDPEAAIRALMKLAGGSKLLKDVNNIEYFLEEEAQADALDGFFKWLS------ 181

                       170
                ....*....|...
gi 20141001 235 skppEMLLTHPLP 247
Cdd:cd07325 182 ----ELLSTHPFL 190
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 304-475 1.22e-09

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 60.78  E-value: 1.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 304 REQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLAN 383
Cdd:COG3914  75 LLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGE 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 384 AYVQGRQPAAAIKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALSGKLTQAIGLLsdASARVKLGSLEQ 463
Cdd:COG3914 155 ALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNL--LFALRQACDWEV 232

                       170
                ....*....|...
gi 20141001 464 A-RYDARIDQLRR 475
Cdd:COG3914 233 YdRFEELLAALAR 245
M48B_HtpX_like cd07338
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 82-251 5.51e-08

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


Pssm-ID: 320697 [Multi-domain]  Cd Length: 216  Bit Score: 53.35  E-value: 5.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  82 VANANSVRTPfHFYLVNNDQINAFAF----FGGNVVLHSALFRYTdNESELASVLAHEISHVtqRHlaRAMeeqqrlAPL 157
Cdd:cd07338  42 VARRAGIKPP-KVGIAEDPIPNAFAYgsplTGARVAVTRGLLDIL-NRDELEAVIGHELGHI--KH--RDV------AIM 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 158 TWVGVLGSIL--LTMASPQAGMAGLSGTLAGA---------------QQGIISFTQGNEQEADRIGIQVLQrsgfDPQAM 220
Cdd:cd07338 110 TAIGLIPSIIyyIGRSLLFSGGSSGGRNGGGAllavgiaafavyflfQLLVLGFSRLREYYADAHSAKVTG----NGRAL 185

                       170       180       190
                ....*....|....*....|....*....|.
gi 20141001 221 PNFLQKLADQSRYvskppEMLLTHPLPDSRL 251
Cdd:cd07338 186 QSALAKIAYGYLA-----EIFSTHPLPAKRI 211
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 305-479 8.19e-08

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: 53.58  E-value: 8.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 305 EQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANA 384
Cdd:COG2956  74 DRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAEL 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 385 YVQGRQPAAAIKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALSGKLTQAIGLLSDAsarvklgSLEQA 464
Cdd:COG2956 154 YLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAEL-------YEKLG 226

                       170
                ....*....|....*
gi 20141001 465 RYDARIDQLRRLNER 479
Cdd:COG2956 227 DPEEALELLRKALEL 241
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 318-464 1.13e-07

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: 54.32  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001   318 YQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANAYVQGRQPAAAIKL 397
Cdd:TIGR02917 510 IQEGNPDDAIQRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKKALAI 589

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20141001   398 LHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALSGKLTQAIGLLSDASARVK-----LGSLEQA 464
Cdd:TIGR02917 590 LNEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKnyakaITSLKRA 661
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 293-475 1.20e-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: 53.19  E-value: 1.20e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 293 ELLDKLSKgTVREQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQN 372
Cdd:COG2956  97 ELLEKLLE-LDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDP 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 373 DEPVLQLNLANAYVQGRQPAAAIKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALSGKLTQAIGLlsdA 452
Cdd:COG2956 176 DCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLAL---A 252

                       170       180
                ....*....|....*....|...
gi 20141001 453 SARVKLGSLEQARYDARiDQLRR 475
Cdd:COG2956 253 DLLERKEGLEAALALLE-RQLRR 274
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 305-469 1.36e-07

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 54.23  E-value: 1.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 305 EQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANA 384
Cdd:COG3914  42 GLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNL 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 385 YVQGRQPAAAIKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALSGKLTQAIGLLsdASARVKLGSLEQA 464
Cdd:COG3914 122 LLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNL--GNALQDLGRLEEA 199


                ....*
gi 20141001 465 RYDAR 469
Cdd:COG3914 200 IAAYR 204
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 319-472 2.47e-07

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: 53.55  E-value: 2.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001   319 QAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANAYVQGRQPAAAIKLL 398
Cdd:TIGR02917 613 AAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNTEAQIGLAQLLLAAKRTESAKKIA 692

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20141001   399 HRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALSGKLTQAIGLlsdasARVKLGSLEQARYDARIDQ 472
Cdd:TIGR02917 693 KSLQKQHPKAALGFELEGDLYLRQKDYPAAIQAYRKALKRAPSSQNAIKL-----HRALLASGNTAEAVKTLEA 761
M56_like cd07329
Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains ...
 95-252 4.48e-07

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: 50.14  E-value: 4.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  95 YLVNNDQINAFA---FFGGNVVLHSALFRyTDNESELASVLAHEISHVTQRHLarameeqqrLAPLTWVGVLGSILLTMA 171
Cdd:cd07329  15 YVVDSDVPNAFAvgrSRGPTVVVTTGLLD-LLDDDELEAVLAHELAHLKRRDV---------LVLLLFDPLLLLVVGLLL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 172 SPQAGMAGLSGTLAG-----AQQGIISFTQ--GNEQEADRIGIQVLQRSGFDPQAMPNFLQKLADQSRYVSKP----PEM 240
Cdd:cd07329  85 FLSLFIFELLGFFFQpllflAFFALLRLAEllADALAVARTSAARRARLTGLPAALASALEKIEDASDRALEAglvlPAL 164

                       170       180
                ....*....|....*....|
gi 20141001 241 L--------LTHPLPDSRLS 252
Cdd:cd07329 165 AadasslekTDHPPLEERVE 184
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
309-484 5.97e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.78  E-value: 5.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 309 AKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANAYVQG 388
Cdd:COG0457  44 ALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLEL 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 389 RQPAAAIKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALSGKLTQAIGLLSDASARVKLGSLEQARYDA 468
Cdd:COG0457 124 GRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLAL 203

                       170
                ....*....|....*.
gi 20141001 469 RIDQLRRLNERFRKYQ 484
Cdd:COG0457 204 EQALRKKLAILTLAAL 219
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
305-486 7.51e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.39  E-value: 7.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 305 EQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANA 384
Cdd:COG0457   6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 385 YVQGRQPAAAIKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALSGKLTQAIGLLsdASARVKLGSLEQA 464
Cdd:COG0457  86 LQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL--GIALEKLGRYEEA 163

                       170       180
                ....*....|....*....|..
gi 20141001 465 RYDARIDQLRRLNERFRKYQKS 486
Cdd:COG0457 164 LELLEKLEAAALAALLAAALGE 185
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 305-408 1.02e-06

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: 48.26  E-value: 1.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 305 EQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANA 384
Cdd:COG4783  36 DNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARA 115

                        90       100
                ....*....|....*....|....
gi 20141001 385 YVQGRQPAAAIKLLHRYTFAYPND 408
Cdd:COG4783 116 YRALGRPDEAIAALEKALELDPDD 139
M48B_HtpX_like cd07337
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 70-171 1.24e-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: 320696 [Multi-domain]  Cd Length: 203  Bit Score: 49.23  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  70 LTQYINTLGNRLVANANSVRtpfhFYLVNNDQINAFAFfGGNVVLHSALFRYTDNESELASVLAHEISHVTQRHlarame 149
Cdd:cd07337  41 INPELEDKARRLGPDPEKVK----LFISDDEYPNAFAL-GRNTICVTKGLLDLLDYEELKGILAHELGHLSHKD------ 109

                        90       100
                ....*....|....*....|..
gi 20141001 150 eqqrlaplTWVGVLGSILLTMA 171
Cdd:cd07337 110 --------TDYLLLIFVLLLLA 123
Peptidase_M48_M56 cd05843
Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral ...
 91-145 1.50e-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: 46.29  E-value: 1.50e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 20141001  91 PFHFYLVNNDQINAFAFFGGN--VVLHSALFRyTDNESELASVLAHEISHVTQRHLA 145
Cdd:cd05843  17 LDKVVVVPGSVPNAFFTGGANkrVVLTTALLE-LLSEEELAAVIAHELGHFKAHEYQ 72
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 311-465 1.57e-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: 49.73  E-value: 1.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 311 YGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANAYVQGRQ 390
Cdd:COG2956  12 YFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGL 91

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20141001 391 PAAAIKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALSGKLTQAIGLLsdASARVKLGSLEQAR 465
Cdd:COG2956  92 LDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCEL--AELYLEQGDYDEAI 164
TPR_19 pfam14559
Tetratricopeptide repeat;
354-417 7.92e-06

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 43.34  E-value: 7.92e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20141001   354 QNKSAAAIARLQNAMVKQNDEPVLQLNLANAYVQGRQPAAAIKLLHRYTFAYPNDPNGWDLLAQ 417
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDPRYAALLAK 64
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 325-439 1.31e-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: 44.61  E-value: 1.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 325 EARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANAYVQGRQPAAAIKLLHRYTFA 404
Cdd:COG4235   1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 20141001 405 YPNDPNGWDLLAQATATQGLRDQELAARAESLALS 439
Cdd:COG4235  81 DPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALL 115
PRK03001 PRK03001
zinc metalloprotease HtpX;
95-245 6.86e-05

zinc metalloprotease HtpX;


Pssm-ID: 179524 [Multi-domain]  Cd Length: 283  Bit Score: 44.63  E-value: 6.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001   95 YLVNNDQINAFAFfGGN-----VVLHSALFRYTdNESELASVLAHEISHVTQRHL-----------ARAM---------- 148
Cdd:PRK03001  88 YLINEDQPNAFAT-GRNpehaaVAATTGILRVL-SEREIRGVMAHELAHVKHRDIlistisatmagAISAlanfamffgg 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  149 --EEQQRLAPLtwVGVLGSILLTMASPQAGMAglsgtlagaqqgiISFTQgnEQEADRIGIQVlqrSGfDPQAMPNFLQK 226
Cdd:PRK03001 166 rdENGRPVNPI--AGIAVAILAPLAASLIQMA-------------ISRAR--EFEADRGGARI---SG-DPQALASALDK 224

                        170
                 ....*....|....*....
gi 20141001  227 LADQSRyvSKPPEMLLTHP 245
Cdd:PRK03001 225 IHRYAS--GIPFQAAEAHP 241
MecR1 COG4219
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ...
 53-145 2.69e-04

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


Pssm-ID: 443363 [Multi-domain]  Cd Length: 337  Bit Score: 43.12  E-value: 2.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  53 FYVRQMRASAPLIYDPLLTQYINTLGNRLvananSVRTPFHFYLvnNDQINA---FAFFGGNVVLHSALFRYTDNEseLA 129
Cdd:COG4219  17 LRLRRLLRRARPVTDEELLELLERLARRL-----GIRRPVRLLE--SDRITSpfsFGLLRPVILLPAGLEELSEEE--LE 87

                        90
                ....*....|....*.
gi 20141001 130 SVLAHEISHVTQRHLA 145
Cdd:COG4219  88 AILAHELAHIRRRDLL 103
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
308-476 3.10e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 42.30  E-value: 3.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 308 AAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANAYVQ 387
Cdd:COG0457  77 EALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEK 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 388 GRQPAAAIKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALSGKLTQAIGLLSDASARVKLGSLEQARYD 467
Cdd:COG0457 157 LGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLA 236


                ....*....
gi 20141001 468 ARIDQLRRL 476
Cdd:COG0457 237 ALALYQYRA 245
YfgM COG2976
Putative negative regulator of RcsB-dependent stress response, UPF0070 family [Signal ...
 304-398 4.49e-04

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


Pssm-ID: 442215 [Multi-domain]  Cd Length: 207  Bit Score: 41.38  E-value: 4.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 304 REQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIW--FLDLMT-DIDLGQNKSAAAIARLQNAMVKQNDEPVLQ-- 378
Cdd:COG2976  50 AEEASALYEQLLEALAAGDAAAAAAAAEKLIDDYGGTAYaaLAALLLaKAAVDAGDLDKAAAQLQWVLDNAKDPALKAla 129

                        90       100
                ....*....|....*....|.
gi 20141001 379 -LNLANAYVQGRQPAAAIKLL 398
Cdd:COG2976 130 rLRLARVLLAQKKYDEALATL 150
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 305-417 5.97e-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: 39.99  E-value: 5.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 305 EQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANA 384
Cdd:COG4235  15 NDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLA 94

                        90       100       110
                ....*....|....*....|....*....|...
gi 20141001 385 YVQGRQPAAAIKLLHRYTFAYPNDPNGWDLLAQ 417
Cdd:COG4235  95 AFQQGDYAEAIAAWQKLLALLPADAPARLLEAS 127
M48B_HtpX_like cd07327
HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, ...
 95-142 1.18e-03

HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, also known as HtpX, which consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX, an integral membrane (IM) metallopeptidase, is widespread in bacteria and archaea, and plays a central role in protein quality control by preventing the accumulation of misfolded proteins in the membrane. Its expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and eliminating them by collaborating with FtsH, a membrane-bound and ATP-dependent protease. HtpX contains the zinc binding motif (HEXXH), has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not. Mutation studies of HtpX-like M48 metalloprotease from Leptospira interrogans (LA4131) has been shown to result in altered expression of a subset of metal toxicity and stress response genes.


Pssm-ID: 320686 [Multi-domain]  Cd Length: 183  Bit Score: 39.93  E-value: 1.18e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 20141001  95 YLVNNDQINAFAFfGGN-----VVLHSALFRyTDNESELASVLAHEISHVTQR 142
Cdd:cd07327  45 AIVDTPMPNAFAT-GRNpknaaVAVTTGLLQ-LLNEDELEAVLAHELSHIKNR 95
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 305-435 1.66e-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: 41.22  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001   305 EQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANA 384
Cdd:TIGR02917 293 EYLPALLLAGASEYQLGNLEQAYQYLNQILKYAPNSHQARRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEA 372

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 20141001   385 YVQGRQPAAAIKLLHRYTFAYPNDPN-----GWDLLAQATATQGLRDQELAARAES 435
Cdd:TIGR02917 373 YLALGDFEKAAEYLAKATELDPENAAartqlGISKLSQGDPSEAIADLETAAQLDP 428
M56_BlaR1_MecR1_like cd07326
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 104-143 1.68e-03

Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; This family contains peptidase M56, which includes zinc metalloprotease domain in MecR1 as well as BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain ?-lactam antibiotics in MRSA. Both, MecR1 and BlaR1, are transmembrane proteins that consist of four transmembrane helices, a cytoplasmic zinc protease domain, and the soluble C-terminal extracellular sensor domain, and are highly similar in sequence and function. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. All members contain the zinc metalloprotease motif (HEXXH). Homologs of this peptidase domain are also found in a number of other bacterial genome sequences, most of which are as yet uncharacterized.


Pssm-ID: 320685 [Multi-domain]  Cd Length: 165  Bit Score: 39.21  E-value: 1.68e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 20141001 104 AFAFFGGN--VVLHSALFRYTDnESELASVLAHEISHVTQRH 143
Cdd:cd07326  39 AFCLGGRRprIVLSTGLLELLS-PEELRAVLAHERAHLRRRD 79
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 308-473 1.89e-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: 40.84  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001   308 AAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAmVKQNDE--PVLQLNLANAY 385
Cdd:TIGR02917 228 AVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDFQKKNYEDARETLQDA-LKSAPEylPALLLAGASEY 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001   386 VQGRQPAAAiKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALSGKLTQAIGLLSdaSARVKLGSLEQA- 464
Cdd:TIGR02917 307 QLGNLEQAY-QYLNQILKYAPNSHQARRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLG--EAYLALGDFEKAa 383


                  ....*....
gi 20141001   465 RYDARIDQL 473
Cdd:TIGR02917 384 EYLAKATEL 392
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 315-409 3.02e-03

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 37.28  E-value: 3.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 315 VQLYQAKKYDEARNLLQPLLAQQPGNIWFLD---LMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQ---LNLANAYVQG 388
Cdd:COG1729   1 KALLKAGDYDEAIAAFKAFLKRYPNSPLAPDalyWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPdalLKLGLSYLEL 80

                        90       100
                ....*....|....*....|.
gi 20141001 389 RQPAAAIKLLHRYTFAYPNDP 409
Cdd:COG1729  81 GDYDKARATLEELIKKYPDSE 101
M48A_Ste24p-like cd07345
Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase ...
 119-144 3.32e-03

Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase family M48 subfamily A-like CaaX prenyl protease 1, most of which are uncharacterized. Some of these contain tetratricopeptide (TPR) repeats at the C-terminus. Proteins in this family contain the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. They are thought to be possibly associated with the endoplasmic reticulum (ER), regardless of whether their genes possess the conventional signal motif (KKXX) in the C-terminal. These proteins putatively remove the C-terminal three residues of farnesylated proteins proteolytically.


Pssm-ID: 320704 [Multi-domain]  Cd Length: 346  Bit Score: 39.57  E-value: 3.32e-03
                        10        20        30
                ....*....|....*....|....*....|....*
gi 20141001 119 FRY---TD------NESELASVLAHEISHVTQRHL 144
Cdd:cd07345 187 FRYiliTDalldslSPEELEAVLAHEIGHVKKRHL 221
M48B_HtpX_like cd07339
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 52-139 4.50e-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: 320698 [Multi-domain]  Cd Length: 229  Bit Score: 38.70  E-value: 4.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001  52 DFYVRQMRASaPLIYD--PLLTQYINTLGNRlvANANSVRTPfhfYLVNNDQINAFAFFGGN---VVLHSALFRyTDNES 126
Cdd:cd07339  11 RLILRLYGAR-PLSPGdaPELYRLLQELARR--AGLPRPPLL---YYVPSRVLNAFAVGSRKdaaIALTDGLLR-RLTLR 83

                        90
                ....*....|...
gi 20141001 127 ELASVLAHEISHV 139
Cdd:cd07339  84 ELAGVLAHEVSHI 96
M48B_HtpX_like cd07336
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 95-142 4.77e-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: 38.63  E-value: 4.77e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 20141001  95 YLVNNDQINAFAFfGGN-----VVLHSALFRYTDNEsELASVLAHEISHVTQR 142
Cdd:cd07336  76 YIIPSPQPNAFAT-GRNpehaaVAVTTGILRLLDKD-ELEGVLAHELAHIKNR 126
COG3864 COG3864
Predicted metal-dependent peptidase [General function prediction only];
92-154 6.73e-03

Predicted metal-dependent peptidase [General function prediction only];


Pssm-ID: 443073 [Multi-domain]  Cd Length: 384  Bit Score: 38.80  E-value: 6.73e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20141001  92 FHFYLVNNDQINAFAFFGGNVVLHSALFRYTDNESELASVLAHEISHVTQRHLARAMEEQQRL 154
Cdd:COG3864  30 LALRHVEDDAVPTAAVDGRWTLYYNPAFFARLSLEELAFVLAHEVLHLALRHLARRKGRDPLL 92
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
317-407 6.84e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 35.92  E-value: 6.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 317 LYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIArLQNAMVKQNDEPVLQLNLANAYVQGRQPAAAIK 396
Cdd:COG3063   2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALA 80

                        90
                ....*....|.
gi 20141001 397 LLHRYTFAYPN 407
Cdd:COG3063  81 YLERALELDPS 91
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 305-439 7.21e-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: 7.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 305 EQLAAKYGQAVQLYQAKKYDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANA 384
Cdd:COG5010  18 TKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALL 97

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20141001 385 YVQGRQPAAAIKLLHRYTFAYPNDPNGWDLLAQATATQGLRDQELAARAESLALS 439
Cdd:COG5010  98 YSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTS 152
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 255-406 7.49e-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: 7.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001 255 RNRANQMKPHPTASSQDYLFAKMRILGMYGADENSLTPELLDKLSKGTVREQLAAKYGQAVQLY-QAKKYDEARNLLQPL 333
Cdd:COG5010   1 ARALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYnKLGDFEESLALLEQA 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20141001 334 LAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANAYVQGRQPAAAIKLLHRYTFAYP 406
Cdd:COG5010  81 LQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
M48B_HtpX_like cd07335
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This family contains ...
 98-140 8.64e-03

Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, also known as HtpX, which consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX, an integral membrane (IM) metallopeptidase, is widespread in bacteria and archaea, and plays a central role in protein quality control by preventing the accumulation of misfolded proteins in the membrane. Its expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and eliminating them by collaborating with FtsH, a membrane-bound and ATP-dependent protease. HtpX contains the zinc binding motif (HEXXH), has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not. Mutation studies of HtpX-like M48 metalloprotease from Leptospira interrogans (LA4131) has been shown to result in altered expression of a subset of metal toxicity and stress response genes.


Pssm-ID: 320694 [Multi-domain]  Cd Length: 240  Bit Score: 37.95  E-value: 8.64e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 20141001  98 NNDQINAFAFfGGN-----VVLHSALFRyTDNESELASVLAHEISHVT 140
Cdd:cd07335  58 PSPDVNAFAT-GPSrnnslVAVSTGLLD-NMSEDEVEAVLAHEISHIA 103
PRK11447 PRK11447
cellulose synthase subunit BcsC; Provisional
 323-452 9.05e-03

cellulose synthase subunit BcsC; Provisional


Pssm-ID: 183140 [Multi-domain]  Cd Length: 1157  Bit Score: 38.91  E-value: 9.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20141001   323 YDEARNLLQPLLAQQPGNIWFLDLMTDIDLGQNKSAAAIARLQNAMVKQNDEPVLQLNLANAYVQGRQPAAAIKLLHRyt 402
Cdd:PRK11447  619 YAAARAAYQRVLTREPGNADARLGLIEVDIAQGDLAAARAQLAKLPATANDSLNTQRRVALAWAALGDTAAAQRTFNR-- 696

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 20141001   403 faypndpngwdLLAQATATQGLRDQEL----AARAEslALSGKLTQAIGLLSDA 452
Cdd:PRK11447  697 -----------LIPQAKSQPPSMESALvlrdAARFE--AQTGQPQQALETYKDA 737
 
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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