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Conserved domains on  [gi|504513165|ref|WP_014700267|]
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lipopolysaccharide assembly protein LapB [Pectobacterium parmentieri]

Protein Classification

lipopolysaccharide assembly protein LapB( domain architecture ID 11485508)

lipopolysaccharide assembly protein LapB is a tetratricopeptide repeat (TPR) protein that modulates cellular lipopolysaccharide (LPS) levels by regulating LpxC, which is involved in lipid A biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
 10-389 0e+00

tetratricopeptide repeat protein; Provisional


:

Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 622.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  10 PVAAAYGWYMGRRGAQQDKEQESNRLSREYVTGVNFLLSNQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAI 89
Cdd:PRK11788  10 PVAAAYGWYMGRRSARQDQQKESNRLSRDYFKGLNFLLNEQPDKAIDLFIEMLKVDPETVELHLALGNLFRRRGEVDRAI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  90 RIHQALTESASLTFEQRLLAVQQLGRDYMVAGLYDRAEEIFNQLVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVK 169
Cdd:PRK11788  90 RIHQNLLSRPDLTREQRLLALQELGQDYLKAGLLDRAEELFLQLVDEGDFAEGALQQLLEIYQQEKDWQKAIDVAERLEK 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 170 MGKDQLRVDIAHFYCELALLAMGSDDLDKALTLLKKGATADKQCARASIMMGRIYMAQQDHSRAVEALRQVLDQDKELVS 249
Cdd:PRK11788 170 LGGDSLRVEIAHFYCELAQQALARGDLDAARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEALERVEEQDPEYLS 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 250 ETLPMLQECYQHLDKLLDWANFLKRCVEENTGATAELMLADILEKEEGAEVAQAYINRQLQRHPTMRVFHRLMDFHLHEA 329
Cdd:PRK11788 250 EVLPKLMECYQALGDEAEGLEFLRRALEEYPGADLLLALAQLLEEQEGPEAAQALLREQLRRHPSLRGFHRLLDYHLAEA 329

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 330 EDGRTKENLQGLRDMVGEQIRTKPRYNCRKCGFTSQSLYWQCPSCRTWASVKPIRGLDGQ 389
Cdd:PRK11788 330 EEGRAKESLLLLRDLVGEQLKRKPRYRCRNCGFTARTLYWHCPSCKAWETIKPIRGLDGE 389
 
Name Accession Description Interval E-value
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
 10-389 0e+00

tetratricopeptide repeat protein; Provisional


Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 622.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  10 PVAAAYGWYMGRRGAQQDKEQESNRLSREYVTGVNFLLSNQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAI 89
Cdd:PRK11788  10 PVAAAYGWYMGRRSARQDQQKESNRLSRDYFKGLNFLLNEQPDKAIDLFIEMLKVDPETVELHLALGNLFRRRGEVDRAI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  90 RIHQALTESASLTFEQRLLAVQQLGRDYMVAGLYDRAEEIFNQLVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVK 169
Cdd:PRK11788  90 RIHQNLLSRPDLTREQRLLALQELGQDYLKAGLLDRAEELFLQLVDEGDFAEGALQQLLEIYQQEKDWQKAIDVAERLEK 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 170 MGKDQLRVDIAHFYCELALLAMGSDDLDKALTLLKKGATADKQCARASIMMGRIYMAQQDHSRAVEALRQVLDQDKELVS 249
Cdd:PRK11788 170 LGGDSLRVEIAHFYCELAQQALARGDLDAARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEALERVEEQDPEYLS 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 250 ETLPMLQECYQHLDKLLDWANFLKRCVEENTGATAELMLADILEKEEGAEVAQAYINRQLQRHPTMRVFHRLMDFHLHEA 329
Cdd:PRK11788 250 EVLPKLMECYQALGDEAEGLEFLRRALEEYPGADLLLALAQLLEEQEGPEAAQALLREQLRRHPSLRGFHRLLDYHLAEA 329

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 330 EDGRTKENLQGLRDMVGEQIRTKPRYNCRKCGFTSQSLYWQCPSCRTWASVKPIRGLDGQ 389
Cdd:PRK11788 330 EEGRAKESLLLLRDLVGEQLKRKPRYRCRNCGFTARTLYWHCPSCKAWETIKPIRGLDGE 389
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 10-312 6.61e-84

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: 256.96  E-value: 6.61e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  10 PVAAAYGWYMgrrgaqqdkeqesnrlsreyvTGVNFLLSNQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAI 89
Cdd:COG2956    4 PVAAALGWYF---------------------KGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAI 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  90 RIHQALTESAsltfEQRLLAVQQLGRDYMVAGLYDRAEEIFNQLVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVK 169
Cdd:COG2956   63 RIHQKLLERD----PDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLK 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 170 MGKDQlrvdiAHFYCELALLAMGSDDLDKALTLLKKGATADKQCARASIMMGRIYMAQQDHSRAVEALRQVLDQDKELVS 249
Cdd:COG2956  139 LGPEN-----AHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLP 213

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513165 250 eTLPMLQECYQHLDKLLDWANFLKRCVEENTGATAELMLADILEKEEGAEVAQAYINRQLQRH 312
Cdd:COG2956  214 -ALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEGLEAALALLERQLRRH 275
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 42-344 4.50e-11

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: 64.72  E-value: 4.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165   42 GVNFLLSNQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAIRIHQALTES----ASLtfeQRLLAVQQLGRdy 117
Cdd:TIGR02917 404 GISKLSQGDPSEAIADLETAAQLDPELGRADLLLILSYLRSGQFDKALAAAKKLEKKqpdnASL---HNLLGAIYLGK-- 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  118 mvaGLYDRAEEIFNQ-LVDEEDFrRSALQQLLQIHQATSDWQTAIDVAEKLVKMGKDQLRVDIAhfyceLALLAMGSDDL 196
Cdd:TIGR02917 479 ---GDLAKAREAFEKaLSIEPDF-FPAAANLARIDIQEGNPDDAIQRFEKVLTIDPKNLRAILA-----LAGLYLRTGNE 549

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  197 DKALTLLKKGATADKQCARASIMMGRIYMAQQDHSRAVEALRQVLDQDKELVsETLPMLQECYQHLDKLLDWANFLKRCV 276
Cdd:TIGR02917 550 EEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKKALAILNEAADAAPDSP-EAWLMLGRAQLAAGDLNKAVSSFKKLL 628

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513165  277 EEN-TGATAELMLADILEKEEGAEVAQAYINRQLQRHPTMRVFHRLMdfHLHEAEDGRTKENLQGLRDM 344
Cdd:TIGR02917 629 ALQpDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNTEAQIGL--AQLLLAAKRTESAKKIAKSL 695
Rubredoxin_2 pfam18073
Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found ...
 355-382 2.20e-10

Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found in Interest in lipopolysaccharide (LPS) assembly protein B (LapB). Rubredoxin proteins form small non-heme iron binding sites that use four cysteine residues to coordinate a single metal ion in a tetrahedral environment. Rubredoxins are most commonly found in bacterial systems, but have also been found in eukaryotes. The key features of these rubredoxin-like domains are the extended loops or 'knuckles' and the tetracysteine mode of iron binding. Structural analysis of LapB from Escherichia coli show that the rubredoxin metal binding domain is intimately bound to the TPR motifs and that this association to the TPR motifs is essential to LPS regulation and growth in vivo. Other family members include RadA proteins which play a role in DNA damage repair. In E. coli, a protein known as RadA (or Sms) participates in the recombinational repair of radiation-damaged DNA in a process that uses an undamaged DNA strand in one DNA duplex to fill a DNA strand gap in a homologous sister DNA duplex. RadA carries a zinc finger at the N-terminal domain.


Pssm-ID: 436248 [Multi-domain]  Cd Length: 28  Bit Score: 55.24  E-value: 2.20e-10
                          10        20
                  ....*....|....*....|....*...
gi 504513165  355 YNCRKCGFTSQSLYWQCPSCRTWASVKP 382
Cdd:pfam18073   1 YRCSQCGFESPQWFGRCPSCGSWGTLVE 28
 
Name Accession Description Interval E-value
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
 10-389 0e+00

tetratricopeptide repeat protein; Provisional


Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 622.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  10 PVAAAYGWYMGRRGAQQDKEQESNRLSREYVTGVNFLLSNQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAI 89
Cdd:PRK11788  10 PVAAAYGWYMGRRSARQDQQKESNRLSRDYFKGLNFLLNEQPDKAIDLFIEMLKVDPETVELHLALGNLFRRRGEVDRAI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  90 RIHQALTESASLTFEQRLLAVQQLGRDYMVAGLYDRAEEIFNQLVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVK 169
Cdd:PRK11788  90 RIHQNLLSRPDLTREQRLLALQELGQDYLKAGLLDRAEELFLQLVDEGDFAEGALQQLLEIYQQEKDWQKAIDVAERLEK 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 170 MGKDQLRVDIAHFYCELALLAMGSDDLDKALTLLKKGATADKQCARASIMMGRIYMAQQDHSRAVEALRQVLDQDKELVS 249
Cdd:PRK11788 170 LGGDSLRVEIAHFYCELAQQALARGDLDAARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEALERVEEQDPEYLS 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 250 ETLPMLQECYQHLDKLLDWANFLKRCVEENTGATAELMLADILEKEEGAEVAQAYINRQLQRHPTMRVFHRLMDFHLHEA 329
Cdd:PRK11788 250 EVLPKLMECYQALGDEAEGLEFLRRALEEYPGADLLLALAQLLEEQEGPEAAQALLREQLRRHPSLRGFHRLLDYHLAEA 329

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 330 EDGRTKENLQGLRDMVGEQIRTKPRYNCRKCGFTSQSLYWQCPSCRTWASVKPIRGLDGQ 389
Cdd:PRK11788 330 EEGRAKESLLLLRDLVGEQLKRKPRYRCRNCGFTARTLYWHCPSCKAWETIKPIRGLDGE 389
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 10-312 6.61e-84

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: 256.96  E-value: 6.61e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  10 PVAAAYGWYMgrrgaqqdkeqesnrlsreyvTGVNFLLSNQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAI 89
Cdd:COG2956    4 PVAAALGWYF---------------------KGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAI 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  90 RIHQALTESAsltfEQRLLAVQQLGRDYMVAGLYDRAEEIFNQLVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVK 169
Cdd:COG2956   63 RIHQKLLERD----PDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLK 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 170 MGKDQlrvdiAHFYCELALLAMGSDDLDKALTLLKKGATADKQCARASIMMGRIYMAQQDHSRAVEALRQVLDQDKELVS 249
Cdd:COG2956  139 LGPEN-----AHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLP 213

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513165 250 eTLPMLQECYQHLDKLLDWANFLKRCVEENTGATAELMLADILEKEEGAEVAQAYINRQLQRH 312
Cdd:COG2956  214 -ALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEGLEAALALLERQLRRH 275
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 104-246 6.02e-12

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: 62.90  E-value: 6.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 104 EQRLLAVQQLGRDYMVAGLYDRAEEIFNQLVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVKMGKDQLRVdiahfY 183
Cdd:COG4783    1 AACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEA-----R 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504513165 184 CELALLAMGSDDLDKALTLLKKGATADKQCARASIMMGRIYMAQQDHSRAVEALRQVLDQDKE 246
Cdd:COG4783   76 LNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPD 138
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 42-344 4.50e-11

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: 64.72  E-value: 4.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165   42 GVNFLLSNQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAIRIHQALTES----ASLtfeQRLLAVQQLGRdy 117
Cdd:TIGR02917 404 GISKLSQGDPSEAIADLETAAQLDPELGRADLLLILSYLRSGQFDKALAAAKKLEKKqpdnASL---HNLLGAIYLGK-- 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  118 mvaGLYDRAEEIFNQ-LVDEEDFrRSALQQLLQIHQATSDWQTAIDVAEKLVKMGKDQLRVDIAhfyceLALLAMGSDDL 196
Cdd:TIGR02917 479 ---GDLAKAREAFEKaLSIEPDF-FPAAANLARIDIQEGNPDDAIQRFEKVLTIDPKNLRAILA-----LAGLYLRTGNE 549

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  197 DKALTLLKKGATADKQCARASIMMGRIYMAQQDHSRAVEALRQVLDQDKELVsETLPMLQECYQHLDKLLDWANFLKRCV 276
Cdd:TIGR02917 550 EEAVAWLEKAAELNPQEIEPALALAQYYLGKGQLKKALAILNEAADAAPDSP-EAWLMLGRAQLAAGDLNKAVSSFKKLL 628

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504513165  277 EEN-TGATAELMLADILEKEEGAEVAQAYINRQLQRHPTMRVFHRLMdfHLHEAEDGRTKENLQGLRDM 344
Cdd:TIGR02917 629 ALQpDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNTEAQIGL--AQLLLAAKRTESAKKIAKSL 695
Rubredoxin_2 pfam18073
Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found ...
 355-382 2.20e-10

Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found in Interest in lipopolysaccharide (LPS) assembly protein B (LapB). Rubredoxin proteins form small non-heme iron binding sites that use four cysteine residues to coordinate a single metal ion in a tetrahedral environment. Rubredoxins are most commonly found in bacterial systems, but have also been found in eukaryotes. The key features of these rubredoxin-like domains are the extended loops or 'knuckles' and the tetracysteine mode of iron binding. Structural analysis of LapB from Escherichia coli show that the rubredoxin metal binding domain is intimately bound to the TPR motifs and that this association to the TPR motifs is essential to LPS regulation and growth in vivo. Other family members include RadA proteins which play a role in DNA damage repair. In E. coli, a protein known as RadA (or Sms) participates in the recombinational repair of radiation-damaged DNA in a process that uses an undamaged DNA strand in one DNA duplex to fill a DNA strand gap in a homologous sister DNA duplex. RadA carries a zinc finger at the N-terminal domain.


Pssm-ID: 436248 [Multi-domain]  Cd Length: 28  Bit Score: 55.24  E-value: 2.20e-10
                          10        20
                  ....*....|....*....|....*...
gi 504513165  355 YNCRKCGFTSQSLYWQCPSCRTWASVKP 382
Cdd:pfam18073   1 YRCSQCGFESPQWFGRCPSCGSWGTLVE 28
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
62-247 2.60e-09

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 57.32  E-value: 2.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  62 LKDDSNTFEAHLTLGNLFRSRGEVDRAIRIHQALTESASLTFEqrllAVQQLGRDYMVAGLYDRAEEIFNQLVDEEDFRR 141
Cdd:COG0457    1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAE----ALYNLGLAYLRLGRYEEALADYEQALELDPDDA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 142 SALQQLLQIHQATSDWQTAIDVAEKLVkmgkdQLRVDIAHFYCELALLAMGSDDLDKALTLLKKGATADKQCARASIMMG 221
Cdd:COG0457   77 EALNNLGLALQALGRYEEALEDYDKAL-----ELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLG 151

                        170       180
                 ....*....|....*....|....*.
gi 504513165 222 RIYMAQQDHSRAVEALRQVLDQDKEL 247
Cdd:COG0457  152 IALEKLGRYEEALELLEKLEAAALAA 177
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 49-314 1.20e-08

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: 57.02  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165   49 NQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAIRIHQALTESASltfeQRLLAVQQLGRDYMVAGLYDRAEE 128
Cdd:TIGR02917 309 GNLEQAYQYLNQILKYAPNSHQARRLLASIQLRLGRVDEAIATLSPALGLDP----DDPAALSLLGEAYLALGDFEKAAE 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  129 IFNQLVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVKMGKDQLRVDIAhfyceLALLAMGSDDLDKALTLLKKGAT 208
Cdd:TIGR02917 385 YLAKATELDPENAAARTQLGISKLSQGDPSEAIADLETAAQLDPELGRADLL-----LILSYLRSGQFDKALAAAKKLEK 459

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  209 adKQCARASI--MMGRIYMAQQDHSRAVEALRQVLDqdkelvsetlpmlqecyqhldklLDWANFlkrcveentgaTAEL 286
Cdd:TIGR02917 460 --KQPDNASLhnLLGAIYLGKGDLAKAREAFEKALS-----------------------IEPDFF-----------PAAA 503

                         250       260
                  ....*....|....*....|....*...
gi 504513165  287 MLADILEKEEGAEVAQAYINRQLQRHPT 314
Cdd:TIGR02917 504 NLARIDIQEGNPDDAIQRFEKVLTIDPK 531
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 32-170 2.16e-08

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 52.50  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  32 SNRLSREYVTGVNFLLSNQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAIR-IHQALTESAsltfeQRLLAV 110
Cdd:COG4783    1 AACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVlLHEALELDP-----DEPEAR 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 111 QQLGRDYMVAGLYDRAEEIFNQLVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVKM 170
Cdd:COG4783   76 LNLGLALLKAGDYDEALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALEL 135
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 142-279 4.42e-08

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 51.73  E-value: 4.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 142 SALQQLLQIHQATSDWQTAIDVAEKLVKMGKDQlrvdiAHFYCELALLAMGSDDLDKALTLLKKGATADKQCARASIMMG 221
Cdd:COG4783    5 EALYALAQALLLAGDYDEAEALLEKALELDPDN-----PEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLG 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504513165 222 RIYMAQQDHSRAVEALRQVLDQDKELVsETLPMLQECYQHLDKLLDWANFLKRCVEEN 279
Cdd:COG4783   80 LALLKAGDYDEALALLEKALKLDPEHP-EAYLRLARAYRALGRPDEAIAALEKALELD 136
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 42-243 2.97e-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: 52.39  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165   42 GVNFLLSNQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAIR-IHQALTESASLTFEQRLLAvqqlgRDYMVA 120
Cdd:TIGR02917 608 GRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITsLKRALELKPDNTEAQIGLA-----QLLLAA 682

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  121 GLYDRAEEIFNQLvdEEDFRRSALQQLL--QIHQATSDWQTAIDVAEKLVKM-GKDQLRVDIAHfycelALLAMG--SDD 195
Cdd:TIGR02917 683 KRTESAKKIAKSL--QKQHPKAALGFELegDLYLRQKDYPAAIQAYRKALKRaPSSQNAIKLHR-----ALLASGntAEA 755

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 504513165  196 LDKALTLLKKGATAdkqcARASIMMGRIYMAQQDHSRAVEALRQVLDQ 243
Cdd:TIGR02917 756 VKTLEAWLKTHPND----AVLRTALAELYLAQKDYDKAIKHYQTVVKK 799
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 42-197 5.33e-07

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 51.53  E-value: 5.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  42 GVNFLLSNQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAIRIHQALTESAsltfEQRLLAVQQLGRDYMVAG 121
Cdd:COG3914  119 GNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELD----PDNAEALNNLGNALQDLG 194

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504513165 122 LYDRAEEIFNQLV--DEEDFRrsALQQLLQIHQATSDWQTAIDVAEKLVKMGKDQlrVDIAHFYcelaLLAMGSDDLD 197
Cdd:COG3914  195 RLEEAIAAYRRALelDPDNAD--AHSNLLFALRQACDWEVYDRFEELLAALARGP--SELSPFA----LLYLPDDDPA 264
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 12-214 5.52e-07

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 51.53  E-value: 5.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  12 AAAYGWYMGRRGAQQDKEQESNRLSREYVTGVNFLLSNQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAIRI 91
Cdd:COG3914   55 AAAALLALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAA 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  92 -HQALTESASLtfeqrLLAVQQLGRDYMVAGLYDRAEEIFNQLVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVKM 170
Cdd:COG3914  135 lRRALALNPDF-----AEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALEL 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 504513165 171 GKDQLrvDIAHFYCELALLAMGSDDLDKALTLLKKGATADKQCA 214
Cdd:COG3914  210 DPDNA--DAHSNLLFALRQACDWEVYDRFEELLAALARGPSELS 251
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 185-313 6.49e-07

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: 6.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 185 ELALLAMGSDDLDKALTLLKKGATADKQCARASIMMGRIYMAQQDHSRAVEALRQVLDQDKELvSETLPMLQECYQHLDK 264
Cdd:COG4783    9 ALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDE-PEARLNLGLALLKAGD 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 504513165 265 LLDWANFLKRCVEENTG-ATAELMLADILEKEEGAEVAQAYINRQLQRHP 313
Cdd:COG4783   88 YDEALALLEKALKLDPEhPEAYLRLARAYRALGRPDEAIAALEKALELDP 137
HemYx COG3071
Uncharacterized protein HemY, contains HemY_N domain and TPR repeats (unrelated to ...
 52-248 2.14e-06

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: 49.14  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  52 DKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAIR-IHQALTESASLTFEQRLLAVQQLGRDymvaGLYDRAEEIF 130
Cdd:COG3071   33 ARAEKLLSKAAEHSEAPLLAYLLAARAAQALGDYERRDEyLAQALELAPEAELAVLLTRAELLLDQ----GQAEQALATL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 131 NQLVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVK---MGKDQLRVDIAHFYCElaLLAMGSDDLDKALTLLKKGA 207
Cdd:COG3071  109 EALRAGAPRHPQVLRLLLQAYRQLGDWEELLELLPALRKhkaLSAEEAQALERRAYLG--LLRQAARDAEALKALWKALP 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 504513165 208 TADKQCARASIMMGRIYMAQQDHSRAVEALRQVLDQ--DKELV 248
Cdd:COG3071  187 RAERRDPELAAAYARALIALGDHDEAERLLREALKRqwDPRLV 229
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 143-246 3.26e-06

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 46.15  E-value: 3.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 143 ALQQLLQIHQATSDWQTAIDVAEKLVkmgkdQLRVDIAHFYCELALLAMGSDDLDKALTLLKKGATADKQCARASIMMGR 222
Cdd:COG4235   19 GWLLLGRAYLRLGRYDEALAAYEKAL-----RLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGL 93

                         90       100
                 ....*....|....*....|....
gi 504513165 223 IYMAQQDHSRAVEALRQVLDQDKE 246
Cdd:COG4235   94 AAFQQGDYAEAIAAWQKLLALLPA 117
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 90-245 3.44e-06

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: 46.49  E-value: 3.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  90 RIHQALTESASLTFEQRLLAVQQLGRDYMVAGLYDRAEEIFNQLVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVK 169
Cdd:COG5010    3 ALEGFDRLPLYLLLLTKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQ 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504513165 170 MGKDQlrvdiAHFYCELALLAMGSDDLDKALTLLKKGATADKQCARASIMMGRIYMAQQDHSRAVEALRQVLDQDK 245
Cdd:COG5010   83 LDPNN-----PELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
49-212 1.02e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 46.54  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  49 NQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAIRIHQALTESASltfeQRLLAVQQLGRDYMVAGLYDRAEE 128
Cdd:COG0457   22 GRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDP----DDAEALNNLGLALQALGRYEEALE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 129 IFNQLVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVkmgkdQLRVDIAHFYCELALLAMGSDDLDKALTLLKKGAT 208
Cdd:COG0457   98 DYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERAL-----ELDPDDADALYNLGIALEKLGRYEEALELLEKLEA 172


                 ....
gi 504513165 209 ADKQ 212
Cdd:COG0457  173 AALA 176
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
174-313 7.62e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 43.84  E-value: 7.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 174 QLRVDIAHFYCELALLAMGSDDLDKALTLLKKGATADKQCARASIMMGRIYMAQQDHSRAVEALRQVLDQDKELVsETLP 253
Cdd:COG0457    2 ELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDA-EALN 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504513165 254 MLQECYQHLDKLLDWANFLKRCVEENTG-ATAELMLADILEKEEGAEVAQAYINRQLQRHP 313
Cdd:COG0457   81 NLGLALQALGRYEEALEDYDKALELDPDdAEALYNLGLALLELGRYDEAIEAYERALELDP 141
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 115-205 1.44e-04

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: 40.75  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 115 RDYMVAGLYDRAEEIFNQLVD---EEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVKMGKDQLRVDIAHFYceLALLAM 191
Cdd:COG1729    1 KALLKAGDYDEAIAAFKAFLKrypNSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDALLK--LGLSYL 78

                         90
                 ....*....|....
gi 504513165 192 GSDDLDKALTLLKK 205
Cdd:COG1729   79 ELGDYDKARATLEE 92
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 156-243 1.57e-04

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: 40.75  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 156 DWQTAIDVAEKLVKMGKDQLRVDIAHFYceLALLAMGSDDLDKALTLLKKGATA---DKQCARASIMMGRIYMAQQDHSR 232
Cdd:COG1729    8 DYDEAIAAFKAFLKRYPNSPLAPDALYW--LGEAYYALGDYDEAAEAFEKLLKRypdSPKAPDALLKLGLSYLELGDYDK 85

                         90
                 ....*....|.
gi 504513165 233 AVEALRQVLDQ 243
Cdd:COG1729   86 ARATLEELIKK 96
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 75-244 1.84e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 43.44  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  75 LGNLFRSRGEVDRAIRIHQALTESASLTFEQRLLA--VQQLGRDYMVAGLYDRAEEIFNQLVDEEDFRRSALQQLLQIHQ 152
Cdd:COG3914   44 ALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAalLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLL 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 153 ATSDWQTAIDVAEKLVkmgkdQLRVDIAHFYCELALLAMGSDDLDKALTLLKKG-------ATADKQCARASIMMGRiym 225
Cdd:COG3914  124 ALGRLEEALAALRRAL-----ALNPDFAEAYLNLGEALRRLGRLEEAIAALRRAleldpdnAEALNNLGNALQDLGR--- 195

                        170
                 ....*....|....*....
gi 504513165 226 aqqdHSRAVEALRQVLDQD 244
Cdd:COG3914  196 ----LEEAIAAYRRALELD 210
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
52-242 1.89e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 42.69  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  52 DKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAIRIHQALTESASltfeQRLLAVQQLGRDYMVAGLYDRAEEIFN 131
Cdd:COG0457   59 EEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDP----DDAEALYNLGLALLELGRYDEAIEAYE 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 132 QLVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVKMGKDQLRVDIAHFYCELALLAMGSDDLDKALTLLKKGATADK 211
Cdd:COG0457  135 RALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAIL 214

                        170       180       190
                 ....*....|....*....|....*....|.
gi 504513165 212 QCARASIMMGRIYMAQQDHSRAVEALRQVLD 242
Cdd:COG0457  215 TLAALAELLLLALALLLALRLAALALYQYRA 245
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
45-135 1.95e-04

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 40.15  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  45 FLLSNQQDKAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAIRIHQALTESAsltfeQRLLAVQQLGRDYMVAGLYD 124
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALEKALKLDP-----NNAEALLNLAELLLELGDYD 76

                         90
                 ....*....|.
gi 504513165 125 RAEEIFNQLVD 135
Cdd:COG3063   77 EALAYLERALE 87
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
150-247 8.79e-04

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 38.23  E-value: 8.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165 150 IHQATSDWQTAIDVAEKLVKmgkdqLRVDIAHFYCELALLAMGSDDLDKALTLlKKGATADKQCARASIMMGRIYMAQQD 229
Cdd:COG3063    1 LYLKLGDLEEAEEYYEKALE-----LDPDNADALNNLGLLLLEQGRYDEAIAL-EKALKLDPNNAEALLNLAELLLELGD 74

                         90
                 ....*....|....*...
gi 504513165 230 HSRAVEALRQVLDQDKEL 247
Cdd:COG3063   75 YDEALAYLERALELDPSA 92
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 53-170 3.25e-03

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: 37.29  E-value: 3.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  53 KAVELFLDMLKDDSNTFEAHLTLGNLFRSRGEVDRAIrihQALTESASLTfEQRLLAVQQLGRDYMVAGLYDRAEEIFNQ 132
Cdd:COG4235    1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEAL---AAYEKALRLD-PDNADALLDLAEALLAAGDTEEAEELLER 76

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 504513165 133 LVDEEDFRRSALQQLLQIHQATSDWQTAIDVAEKLVKM 170
Cdd:COG4235   77 ALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLAL 114
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 43-136 4.43e-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: 36.51  E-value: 4.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504513165  43 VNFLLSNQQDKAVELFLDMLK---DDSNTFEAHLTLGNLFRSRGEVDRAIRIHQALTESASlTFEQRLLAVQQLGRDYMV 119
Cdd:COG1729    1 KALLKAGDYDEAIAAFKAFLKrypNSPLAPDALYWLGEAYYALGDYDEAAEAFEKLLKRYP-DSPKAPDALLKLGLSYLE 79

                         90
                 ....*....|....*..
gi 504513165 120 AGLYDRAEEIFNQLVDE 136
Cdd:COG1729   80 LGDYDKARATLEELIKK 96
TPR_19 pfam14559
Tetratricopeptide repeat;
195-246 5.99e-03

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 34.87  E-value: 5.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 504513165  195 DLDKALTLLKKGATADKQCARASIMMGRIYMAQQDHSRAVEALRQVLDQDKE 246
Cdd:pfam14559   3 DYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPD 54
 
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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