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Conserved domains on  [gi|738093748|ref|WP_036052399|]
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lipopolysaccharide assembly protein LapB [Burkholderia gladioli]

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
2-388 0e+00

tetratricopeptide repeat protein; Provisional


:

Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 548.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748   2 DLDFWWLLaIPVAFAFGWAASRYDLKK-LLSENANLPRSYFRGLNFLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLF 80
Cdd:PRK11788   1 MLELLFLL-LPVAAAYGWYMGRRSARQdQQKESNRLSRDYFKGLNFLLNEQPDKAIDLFIEMLKVDPETVELHLALGNLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  81 RRRGETDRAIRVHQNLLNRDDLPVNERDHALYELGQDFLKAGLLDRAEESFHRLAD-GDYALGAQRALLTIYGIEKDWNK 159
Cdd:PRK11788  80 RRRGEVDRAIRIHQNLLSRPDLTREQRLLALQELGQDYLKAGLLDRAEELFLQLVDeGDFAEGALQQLLEIYQQEKDWQK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 160 SIQTARKIETMSGSSLSTEIAQFHCELAGEALARKDGAAAAQQLREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRR 239
Cdd:PRK11788 160 AIDVAERLEKLGGDSLRVEIAHFYCELAQQALARGDLDAARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEALER 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 240 VEQQNAAYLPLVAEKLMKAYIARGQAAEGAELLTDYADRYPSNDLLDVAFQYVAELRGADAAHTLARTQMQKAPNLSGML 319
Cdd:PRK11788 240 VEEQDPEYLSEVLPKLMECYQALGDEAEGLEFLRRALEEYPGADLLLALAQLLEEQEGPEAAQALLREQLRRHPSLRGFH 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 320 HLLDAQIATADEPRRGE-LEMMRALVKQRTKNLPRYTCHDCGFRARLFYWQCPGCSGWETYAPRRVEAGV 388
Cdd:PRK11788 320 RLLDYHLAEAEEGRAKEsLLLLRDLVGEQLKRKPRYRCRNCGFTARTLYWHCPSCKAWETIKPIRGLDGE 389
 
Name Accession Description Interval E-value
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
2-388 0e+00

tetratricopeptide repeat protein; Provisional


Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 548.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748   2 DLDFWWLLaIPVAFAFGWAASRYDLKK-LLSENANLPRSYFRGLNFLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLF 80
Cdd:PRK11788   1 MLELLFLL-LPVAAAYGWYMGRRSARQdQQKESNRLSRDYFKGLNFLLNEQPDKAIDLFIEMLKVDPETVELHLALGNLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  81 RRRGETDRAIRVHQNLLNRDDLPVNERDHALYELGQDFLKAGLLDRAEESFHRLAD-GDYALGAQRALLTIYGIEKDWNK 159
Cdd:PRK11788  80 RRRGEVDRAIRIHQNLLSRPDLTREQRLLALQELGQDYLKAGLLDRAEELFLQLVDeGDFAEGALQQLLEIYQQEKDWQK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 160 SIQTARKIETMSGSSLSTEIAQFHCELAGEALARKDGAAAAQQLREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRR 239
Cdd:PRK11788 160 AIDVAERLEKLGGDSLRVEIAHFYCELAQQALARGDLDAARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEALER 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 240 VEQQNAAYLPLVAEKLMKAYIARGQAAEGAELLTDYADRYPSNDLLDVAFQYVAELRGADAAHTLARTQMQKAPNLSGML 319
Cdd:PRK11788 240 VEEQDPEYLSEVLPKLMECYQALGDEAEGLEFLRRALEEYPGADLLLALAQLLEEQEGPEAAQALLREQLRRHPSLRGFH 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 320 HLLDAQIATADEPRRGE-LEMMRALVKQRTKNLPRYTCHDCGFRARLFYWQCPGCSGWETYAPRRVEAGV 388
Cdd:PRK11788 320 RLLDYHLAEAEEGRAKEsLLLLRDLVGEQLKRKPRYRCRNCGFTARTLYWHCPSCKAWETIKPIRGLDGE 389
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
9-311 2.27e-73

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: 230.00  E-value: 2.27e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748   9 LAIPVAFAFGWaasrydlkkllsenanlprsYFRGLNFLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDR 88
Cdd:COG2956    1 LLLPVAAALGW--------------------YFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDR 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  89 AIRVHQNLLNRDDlpvnERDHALYELGQDFLKAGLLDRAEESFHRLADGD-YALGAQRALLTIYGIEKDWNKSIQTARKI 167
Cdd:COG2956   61 AIRIHQKLLERDP----DRAEALLELAQDYLKAGLLDRAEELLEKLLELDpDDAEALRLLAEIYEQEGDWEKAIEVLERL 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 168 ETMSGSSlsteiAQFHCELAGEALARKDGAAAAQQLREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQNAAY 247
Cdd:COG2956  137 LKLGPEN-----AHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDY 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738093748 248 LPlVAEKLMKAYIARGQAAEGAELLTDYADRYPSNDLLDVAFQYVAELRGADAAHTLARTQMQK 311
Cdd:COG2956  212 LP-ALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEGLEAALALLERQLRR 274
Rubredoxin_2 pfam18073
Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found ...
354-381 4.75e-09

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: 51.39  E-value: 4.75e-09
                          10        20
                  ....*....|....*....|....*...
gi 738093748  354 YTCHDCGFRARLFYWQCPGCSGWETYAP 381
Cdd:pfam18073   1 YRCSQCGFESPQWFGRCPSCGSWGTLVE 28
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
50-314 7.47e-09

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 57.79  E-value: 7.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748   50 EQPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDRAIRVHQNLLNRDDLPVNERdhalYELGQDFLKAGLLDRAEE 129
Cdd:TIGR02917 513 GNPDDAIQRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPA----LALAQYYLGKGQLKKALA 588
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  130 SFHRLADGdYALGAQ--RALLTIYGIEKDWNKSIQTARKIETMSGSSlsteiAQFHCELAGEALARKDGAAAAQQLREAL 207
Cdd:TIGR02917 589 ILNEAADA-APDSPEawLMLGRAQLAAGDLNKAVSSFKKLLALQPDS-----ALALLLLADAYAVMKNYAKAITSLKRAL 662
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  208 AVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQN---AAYLPLVAE-----------------------------KL 255
Cdd:TIGR02917 663 ELKPDNTEAQIGLAQLLLAAKRTESAKKIAKSLQKQHpkaALGFELEGDlylrqkdypaaiqayrkalkrapssqnaiKL 742
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  256 MKAYIARGQAAEGAELLTDYADRYPSNDLLDVAFQYVAELRG-ADAAHTLARTQMQKAPN 314
Cdd:TIGR02917 743 HRALLASGNTAEAVKTLEAWLKTHPNDAVLRTALAELYLAQKdYDKAIKHYQTVVKKAPD 802
 
Name Accession Description Interval E-value
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
2-388 0e+00

tetratricopeptide repeat protein; Provisional


Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 548.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748   2 DLDFWWLLaIPVAFAFGWAASRYDLKK-LLSENANLPRSYFRGLNFLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLF 80
Cdd:PRK11788   1 MLELLFLL-LPVAAAYGWYMGRRSARQdQQKESNRLSRDYFKGLNFLLNEQPDKAIDLFIEMLKVDPETVELHLALGNLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  81 RRRGETDRAIRVHQNLLNRDDLPVNERDHALYELGQDFLKAGLLDRAEESFHRLAD-GDYALGAQRALLTIYGIEKDWNK 159
Cdd:PRK11788  80 RRRGEVDRAIRIHQNLLSRPDLTREQRLLALQELGQDYLKAGLLDRAEELFLQLVDeGDFAEGALQQLLEIYQQEKDWQK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 160 SIQTARKIETMSGSSLSTEIAQFHCELAGEALARKDGAAAAQQLREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRR 239
Cdd:PRK11788 160 AIDVAERLEKLGGDSLRVEIAHFYCELAQQALARGDLDAARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEALER 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 240 VEQQNAAYLPLVAEKLMKAYIARGQAAEGAELLTDYADRYPSNDLLDVAFQYVAELRGADAAHTLARTQMQKAPNLSGML 319
Cdd:PRK11788 240 VEEQDPEYLSEVLPKLMECYQALGDEAEGLEFLRRALEEYPGADLLLALAQLLEEQEGPEAAQALLREQLRRHPSLRGFH 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 320 HLLDAQIATADEPRRGE-LEMMRALVKQRTKNLPRYTCHDCGFRARLFYWQCPGCSGWETYAPRRVEAGV 388
Cdd:PRK11788 320 RLLDYHLAEAEEGRAKEsLLLLRDLVGEQLKRKPRYRCRNCGFTARTLYWHCPSCKAWETIKPIRGLDGE 389
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
9-311 2.27e-73

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: 230.00  E-value: 2.27e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748   9 LAIPVAFAFGWaasrydlkkllsenanlprsYFRGLNFLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDR 88
Cdd:COG2956    1 LLLPVAAALGW--------------------YFKGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDR 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  89 AIRVHQNLLNRDDlpvnERDHALYELGQDFLKAGLLDRAEESFHRLADGD-YALGAQRALLTIYGIEKDWNKSIQTARKI 167
Cdd:COG2956   61 AIRIHQKLLERDP----DRAEALLELAQDYLKAGLLDRAEELLEKLLELDpDDAEALRLLAEIYEQEGDWEKAIEVLERL 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 168 ETMSGSSlsteiAQFHCELAGEALARKDGAAAAQQLREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQNAAY 247
Cdd:COG2956  137 LKLGPEN-----AHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDY 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 738093748 248 LPlVAEKLMKAYIARGQAAEGAELLTDYADRYPSNDLLDVAFQYVAELRGADAAHTLARTQMQK 311
Cdd:COG2956  212 LP-ALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEGLEAALALLERQLRR 274
Rubredoxin_2 pfam18073
Rubredoxin metal binding domain; This is the C-terminal rubredoxin metal binding domain found ...
354-381 4.75e-09

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: 51.39  E-value: 4.75e-09
                          10        20
                  ....*....|....*....|....*...
gi 738093748  354 YTCHDCGFRARLFYWQCPGCSGWETYAP 381
Cdd:pfam18073   1 YRCSQCGFESPQWFGRCPSCGSWGTLVE 28
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
50-314 7.47e-09

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


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 57.79  E-value: 7.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748   50 EQPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDRAIRVHQNLLNRDDLPVNERdhalYELGQDFLKAGLLDRAEE 129
Cdd:TIGR02917 513 GNPDDAIQRFEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLEKAAELNPQEIEPA----LALAQYYLGKGQLKKALA 588
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  130 SFHRLADGdYALGAQ--RALLTIYGIEKDWNKSIQTARKIETMSGSSlsteiAQFHCELAGEALARKDGAAAAQQLREAL 207
Cdd:TIGR02917 589 ILNEAADA-APDSPEawLMLGRAQLAAGDLNKAVSSFKKLLALQPDS-----ALALLLLADAYAVMKNYAKAITSLKRAL 662
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  208 AVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQN---AAYLPLVAE-----------------------------KL 255
Cdd:TIGR02917 663 ELKPDNTEAQIGLAQLLLAAKRTESAKKIAKSLQKQHpkaALGFELEGDlylrqkdypaaiqayrkalkrapssqnaiKL 742
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  256 MKAYIARGQAAEGAELLTDYADRYPSNDLLDVAFQYVAELRG-ADAAHTLARTQMQKAPN 314
Cdd:TIGR02917 743 HRALLASGNTAEAVKTLEAWLKTHPNDAVLRTALAELYLAQKdYDKAIKHYQTVVKKAPD 802
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
64-301 3.84e-08

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 53.86  E-value: 3.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  64 KLDPETVELHFALGNLFRRRGETDRAIRVHQNLLNRDDlpvnERDHALYELGQDFLKAGLLDRAEESFHR-LADGDYALG 142
Cdd:COG0457    2 ELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDP----DDAEALYNLGLAYLRLGRYEEALADYEQaLELDPDDAE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 143 AQRALLTIYGIEKDWNKSIQTARKIetmsgSSLSTEIAQFHCELAGEALARKDGAAAAQQLREALAVNPHNVRATILSGE 222
Cdd:COG0457   78 ALNNLGLALQALGRYEEALEDYDKA-----LELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGI 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738093748 223 AAEAAGDHQAAIAHWRRVEQQNAAYLPLVAEKLMKAYIARGQAAEGAELLTDYADRYPSNDLLDVAFQYVAELRGADAA 301
Cdd:COG0457  153 ALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLL 231
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
89-283 5.42e-08

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 54.61  E-value: 5.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  89 AIRVHQNLLNRDDLPVNERDHALYELGQDFLKAGLLDRAEESFHRLADGDYALGAQRALLT---IYGIEKDWNKSIQTAR 165
Cdd:COG3914   23 AAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELaalLLQALGRYEEALALYR 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 166 KIetmsgSSLSTEIAQFHCELAGEALARKDGAAAAQQLREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQNA 245
Cdd:COG3914  103 RA-----LALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDP 177
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 738093748 246 AYLPLVAEkLMKAYIARGQAAEGAELLTDYADRYPSND 283
Cdd:COG3914  178 DNAEALNN-LGNALQDLGRLEEAIAAYRRALELDPDNA 214
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
43-282 1.26e-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: 53.93  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748   43 GLNFLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDRAIRVHQNLLNRDdlPVNERDHALyeLGQDFLKAG 122
Cdd:TIGR02917 404 GISKLSQGDPSEAIADLETAAQLDPELGRADLLLILSYLRSGQFDKALAAAKKLEKKQ--PDNASLHNL--LGAIYLGKG 479
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  123 LLDRAEESFhrladgdyalgaqralltiygiekdwnksiQTARKIETMSGSSLSteiaqfhcELAGEALARKDGAAAAQQ 202
Cdd:TIGR02917 480 DLAKAREAF------------------------------EKALSIEPDFFPAAA--------NLARIDIQEGNPDDAIQR 521
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  203 LREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRR-VEQQNAAYLPLVAekLMKAYIARGQAAEGAELLTDYADRYPS 281
Cdd:TIGR02917 522 FEKVLTIDPKNLRAILALAGLYLRTGNEEEAVAWLEKaAELNPQEIEPALA--LAQYYLGKGQLKKALAILNEAADAAPD 599

                  .
gi 738093748  282 N 282
Cdd:TIGR02917 600 S 600
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
19-133 1.73e-07

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 53.07  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  19 WAASRYDLKKLLSENANLPRSYF-RGLNFLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDRAIRVHQNLL 97
Cdd:COG3914   94 YEEALALYRRALALNPDNAEALFnLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRAL 173
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 738093748  98 NRDDlpvnERDHALYELGQDFLKAGLLDRAEESFHR 133
Cdd:COG3914  174 ELDP----DNAEALNNLGNALQDLGRLEEAIAAYRR 205
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
43-306 1.85e-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: 53.16  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748   43 GLNFLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDRAIRVHQNLLNRDDlpvnERDHALYELGQDFLKAG 122
Cdd:TIGR02917 608 GRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALELKP----DNTEAQIGLAQLLLAAK 683
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  123 LLDRAEESFHRLADGDYALGAQRALL-TIYGIEKDWNKSIQTARKIETMSGSSLSTeiaqfhCELAGEALARKDGAAAAQ 201
Cdd:TIGR02917 684 RTESAKKIAKSLQKQHPKAALGFELEgDLYLRQKDYPAAIQAYRKALKRAPSSQNA------IKLHRALLASGNTAEAVK 757
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  202 QLREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQ---------NAAYL-----------------------P 249
Cdd:TIGR02917 758 TLEAWLKTHPNDAVLRTALAELYLAQKDYDKAIKHYQTVVKKapdnavvlnNLAWLylelkdpraleyaeralklapniP 837
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 738093748  250 LVAEKLMKAYIARGQAAEGAELLTDYADRYPSNDL--LDVAFQYVAELRGADAAHTLAR 306
Cdd:TIGR02917 838 AILDTLGWLLVEKGEADRALPLLRKAVNIAPEAAAirYHLALALLATGRKAEARKELDK 896
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
26-136 5.71e-07

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: 48.08  E-value: 5.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  26 LKKLLSENANLPRSYFR-GLNFLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDRAIRVHQNLLNRDdlPV 104
Cdd:COG4235    6 LRQALAANPNDAEGWLLlGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALD--PD 83
                         90       100       110
                 ....*....|....*....|....*....|..
gi 738093748 105 NERdhALYELGQDFLKAGLLDRAEESFHRLAD 136
Cdd:COG4235   84 NPE--ALYLLGLAAFQQGDYAEAIAAWQKLLA 113
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
19-140 7.54e-06

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 46.83  E-value: 7.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  19 WAASRYDLKKLLSENANLPRSY-FRGLNFLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDRAIRVHQNLL 97
Cdd:COG4785   89 YDLAIADFDQALELDPDLAEAYnNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKAL 168
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 738093748  98 NRD-DLPVNERDHALYELGQDFLKAGLLDRAEESFHRLADGDYA 140
Cdd:COG4785  169 ELDpNDPERALWLYLAERKLDPEKALALLLEDWATAYLLQGDTE 212
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
180-282 8.16e-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: 45.18  E-value: 8.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 180 AQFHCELAGEALARKDGAAAAQQLREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQNAAYlPLVAEKLMKAY 259
Cdd:COG4783   38 PEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEH-PEAYLRLARAY 116
                         90       100
                 ....*....|....*....|...
gi 738093748 260 IARGQAAEGAELLTDYADRYPSN 282
Cdd:COG4783  117 RALGRPDEAIAALEKALELDPDD 139
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
54-250 1.07e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 47.68  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  54 QAIDAFIEVAKLDPETVELHFALGNLFRRRGETDRAIRVHQNLLN-----RDDLPVNERDHALYELGQDFLKAGLLDRAE 128
Cdd:COG3914   19 AAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAageaaAAAAALLLLAALLELAALLLQALGRYEEAL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 129 ESFHRL--ADGDYALgAQRALLTIYGIEKDWNKSIQTARKIEtmsgsSLSTEIAQFHCELAGEALARKDGAAAAQQLREA 206
Cdd:COG3914   99 ALYRRAlaLNPDNAE-ALFNLGNLLLALGRLEEALAALRRAL-----ALNPDFAEAYLNLGEALRRLGRLEEAIAALRRA 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 738093748 207 LAVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQNAAYLPL 250
Cdd:COG3914  173 LELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADA 216
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
188-246 1.63e-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: 44.23  E-value: 1.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 188 GEALARKDGAAAAQQ-LREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQNAA 246
Cdd:COG4235   58 AEALLAAGDTEEAEElLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPA 117
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
25-243 2.00e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.77  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  25 DLKKLLSENANLPRSYF-RGLNFLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDRAIRVHQNLLNRDdlp 103
Cdd:COG0457   30 DYEKALELDPDDAEALYnLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELD--- 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 104 vNERDHALYELGQDFLKAGLLDRAEESFHRLADGDYALG-AQRALLTIYGIEKDWNKSIQTARKIEtMSGSSLSTEIAQF 182
Cdd:COG0457  107 -PDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDAdALYNLGIALEKLGRYEEALELLEKLE-AAALAALLAAALG 184
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738093748 183 HCELAGEALARKDGAAAAQQLREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQ 243
Cdd:COG0457  185 EAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALALYQYRA 245
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
25-138 4.17e-05

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 43.26  E-value: 4.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  25 DLKKLLSENANLPRSYF-RGLNFLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDRAIRVHQNLLNRDDlp 103
Cdd:COG4783   26 LLEKALELDPDNPEAFAlLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDP-- 103
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 738093748 104 vnERDHALYELGQDFLKAGLLDRAEESFHRLADGD 138
Cdd:COG4783  104 --EHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
51-254 5.00e-05

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 45.37  E-value: 5.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  51 QPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDRAIRVHQNLLNRDDlpvnERDHALYELGQDFLKAGLLDRAEES 130
Cdd:COG3914   93 RYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNP----DFAEAYLNLGEALRRLGRLEEAIAA 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 131 FHRL--ADGDYALgAQRALLTIYGIEKDWNKSIQTARKIETMSGSSlstEIAQFHCELAGEALARKDGAAAAQQLREALA 208
Cdd:COG3914  169 LRRAleLDPDNAE-ALNNLGNALQDLGRLEEAIAAYRRALELDPDN---ADAHSNLLFALRQACDWEVYDRFEELLAALA 244
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 738093748 209 VNPHNVRATILSGEAAEAAGDHQAAIAHW-RRVEQQNAAYLPLVAEK 254
Cdd:COG3914  245 RGPSELSPFALLYLPDDDPAELLALARAWaQLVAAAAAPELPPPPNP 291
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
40-136 1.01e-04

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 42.10  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  40 YFRGLNFLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDRAIRVHQNLLNRDdlpvNERDHALYELGQDFL 119
Cdd:COG4783    8 YALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELD----PDEPEARLNLGLALL 83
                         90
                 ....*....|....*..
gi 738093748 120 KAGLLDRAEESFHRLAD 136
Cdd:COG4783   84 KAGDYDEALALLEKALK 100
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
177-314 1.37e-04

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 41.72  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 177 TEIAQFHCELAGEALARKDGAAAAQQLREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQNAAYlPLVAEKLM 256
Cdd:COG4783    1 AACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDE-PEARLNLG 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 738093748 257 KAYIARGQAAEGAELLTDYADRYPSN-DLLDVAFQYVAELRGADAAHTLARTQMQKAPN 314
Cdd:COG4783   80 LALLKAGDYDEALALLEKALKLDPEHpEAYLRLARAYRALGRPDEAIAALEKALELDPD 138
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
189-295 3.01e-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: 39.97  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 189 EALARKDGAAAAQQLREALAVNPHNV---RATILSGEAAEAAGDHQAAIAHWRRVEQQ--NAAYLPLVAEKLMKAYIARG 263
Cdd:COG1729    2 ALLKAGDYDEAIAAFKAFLKRYPNSPlapDALYWLGEAYYALGDYDEAAEAFEKLLKRypDSPKAPDALLKLGLSYLELG 81
                         90       100       110
                 ....*....|....*....|....*....|..
gi 738093748 264 QAAEGAELLTDYADRYPSNDLLDVAFQYVAEL 295
Cdd:COG1729   82 DYDKARATLEELIKKYPDSEAAKEARARLARL 113
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
44-147 8.02e-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: 38.82  E-value: 8.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  44 LNFLLNEQPDQAIDAFIEVAKLDPE---TVELHFALGNLFRRRGETDRAIRVHQNLLNRDdlPVNER-DHALYELGQDFL 119
Cdd:COG1729    1 KALLKAGDYDEAIAAFKAFLKRYPNsplAPDALYWLGEAYYALGDYDEAAEAFEKLLKRY--PDSPKaPDALLKLGLSYL 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 738093748 120 KAGLLDRAEESFHRLA----DGDYALGAQRAL 147
Cdd:COG1729   79 ELGDYDKARATLEELIkkypDSEAAKEARARL 110
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
46-141 8.23e-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: 8.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  46 FLLNEQPDQAIDAFIEVAKLDPETVELHFALGNLFRRRGETDRAIRVHQNLLNRDDLPvnerdHALYELGQDFLKAGLLD 125
Cdd:COG3063    2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIALEKALKLDPNNA-----EALLNLAELLLELGDYD 76
                         90
                 ....*....|....*.
gi 738093748 126 RAEESFHRLADGDYAL 141
Cdd:COG3063   77 EALAYLERALELDPSA 92
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
198-282 9.64e-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: 38.83  E-value: 9.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748 198 AAAQQLREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQNAAYlPLVAEKLMKAYIARGQAAEGAELLTDYAD 277
Cdd:COG4235    1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDN-ADALLDLAEALLAAGDTEEAEELLERALA 79

                 ....*
gi 738093748 278 RYPSN 282
Cdd:COG4235   80 LDPDN 84
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
180-275 1.47e-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: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738093748  180 AQFHCELAGEALARKDGAAAAQQLREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQN---AAYLPLVAeklm 256
Cdd:TIGR02917  22 PEELIEAAKSYLQKNKYKAAIIQLKNALQKDPNDAEARFLLGKIYLALGDYAAAEKELRKALSLGypkNQVLPLLA---- 97
                          90
                  ....*....|....*....
gi 738093748  257 KAYIARGQAAEGAELLTDY 275
Cdd:TIGR02917  98 RAYLLQGKFQQVLDELPGK 116
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
188-248 8.73e-03

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 35.53  E-value: 8.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738093748 188 GEALARKDGAAAAQQLREALAVNPHNVRATILSGEAAEAAGDHQAAIAHWRRVEQQNAAYL 248
Cdd:COG3063   33 GLLLLEQGRYDEAIALEKALKLDPNNAEALLNLAELLLELGDYDEALAYLERALELDPSAL 93
 
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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