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Conserved domains on  [gi|550724705|ref|WP_022648506|]
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MULTISPECIES: molecular chaperone [Enterobacter]

Protein Classification

molecular chaperone( domain architecture ID 11459711)

molecular chaperone belonging to the periplasmic pilus chaperone family may be involved in fimbrial biogenesis; similar to Escherichia coli fimbrial chaperones, YraI, YqiH, YbgP and ElfD

CATH:  2.60.40.10
Gene Ontology:  GO:0061077|GO:0030288|GO:0043711
PubMed:  1683764|8670884
SCOP:  4002248|4007561

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FimC COG3121
P pilus assembly protein, chaperone PapD [Extracellular structures];
7-241 1.63e-58

P pilus assembly protein, chaperone PapD [Extracellular structures];


:

Pssm-ID: 442355 [Multi-domain]  Cd Length: 237  Bit Score: 185.58  E-value: 1.63e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550724705   7 RSGLLSLLGITALTAVKAQAAATILLWPIDPWLSADARATELWIQNQGNSATTMQIRIVRWKQEGGYEryTAQQDVVASP 86
Cdd:COG3121    2 KRLLRLLLLALLLLLASAAAAAGISISPTRVIYPAGDKEASLTLTNTGDTPYLVQSWVDDWDQDAGPD--KATAPFVVTP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550724705  87 PIVTIAKGSKQLIRLIKQG-TIPSGVEQAYRIIVDEIPQPDAKAEPSMGLKLQMRYSIPLFVYGQGIPTLNEGEhhalan 165
Cdd:COG3121   80 PLFRLEPGKSQTVRIIRTGpPLPQDRESLFRLNVDEIPPKDASEEGKNTLQIALRTRIKLFYRPAGLKGSPEDA------ 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550724705 166 TQQLNWRVIqeegKPALEVRNQGQVHVRLSQVAVEQGGQKrtvAEGLLGYVLPGSTRSWPLPAGIYQPNRMS---AQIN 241
Cdd:COG3121  154 AEKLTWSLV----GNGLTVTNPGPYYVTLSDLSLGAGGKK---LKKGLGMVLPGSTRRWPLPAGASLAAGGKvtwATIN 225
 
Name Accession Description Interval E-value
FimC COG3121
P pilus assembly protein, chaperone PapD [Extracellular structures];
7-241 1.63e-58

P pilus assembly protein, chaperone PapD [Extracellular structures];


Pssm-ID: 442355 [Multi-domain]  Cd Length: 237  Bit Score: 185.58  E-value: 1.63e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550724705   7 RSGLLSLLGITALTAVKAQAAATILLWPIDPWLSADARATELWIQNQGNSATTMQIRIVRWKQEGGYEryTAQQDVVASP 86
Cdd:COG3121    2 KRLLRLLLLALLLLLASAAAAAGISISPTRVIYPAGDKEASLTLTNTGDTPYLVQSWVDDWDQDAGPD--KATAPFVVTP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550724705  87 PIVTIAKGSKQLIRLIKQG-TIPSGVEQAYRIIVDEIPQPDAKAEPSMGLKLQMRYSIPLFVYGQGIPTLNEGEhhalan 165
Cdd:COG3121   80 PLFRLEPGKSQTVRIIRTGpPLPQDRESLFRLNVDEIPPKDASEEGKNTLQIALRTRIKLFYRPAGLKGSPEDA------ 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550724705 166 TQQLNWRVIqeegKPALEVRNQGQVHVRLSQVAVEQGGQKrtvAEGLLGYVLPGSTRSWPLPAGIYQPNRMS---AQIN 241
Cdd:COG3121  154 AEKLTWSLV----GNGLTVTNPGPYYVTLSDLSLGAGGKK---LKKGLGMVLPGSTRRWPLPAGASLAAGGKvtwATIN 225
PapD_N pfam00345
Pili and flagellar-assembly chaperone, PapD N-terminal domain; C2 domain-like beta-sandwich ...
39-153 3.70e-18

Pili and flagellar-assembly chaperone, PapD N-terminal domain; C2 domain-like beta-sandwich fold. This domain is the n-terminal part of the PapD chaperone protein for pilus and flagellar assembly.


Pssm-ID: 425623  Cd Length: 123  Bit Score: 77.63  E-value: 3.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550724705   39 LSADARATELWIQNQGNSATTMQIRIVRWKQEGGYEryTAQQDVVASPPIVTIAKGSKQLIRLIKQG-TIPSGVEQAYRI 117
Cdd:pfam00345  10 YPAGEKEASVTVSNTGDNPYLVQSWVDDGNEEGTDE--KAKAPFIVTPPLFRLEPGQEQVLRIYTTGpPLPTDRESLFWL 87
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 550724705  118 IVDEIPQPDAKAEPSMGLKLQMRYSIPLFVYGQGIP 153
Cdd:pfam00345  88 NVLEIPPKDKPKGGQNGLQLALRSRIKLFYRPAGLA 123
PRK09926 PRK09926
fimbrial chaperone;
83-208 4.52e-09

fimbrial chaperone;


Pssm-ID: 236634 [Multi-domain]  Cd Length: 246  Bit Score: 55.50  E-value: 4.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550724705  83 VASPPIVTIAKGSKQLIRLI--KQGTIPSGVEQAYRIIVDEIP-QPDAKAEPSMG-LKLQMRYSIPLFVYGQGIPTlNEG 158
Cdd:PRK09926  78 TATPPVSRIDPKRGQTIKLMytASTALPKDRESVFWFNVLEVPpKPDAEKVANQSlLQLAFRTRIKLFYRPDGLKG-NPS 156
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 550724705 159 EHHAlantqQLNWRVIQEEGKPALEVRNQGQVHVRLSQVAVEQGGQKRTV 208
Cdd:PRK09926 157 EAPL-----ALKWSWAGSEGKASLRVTNPTPYYVSFSSGDLEAGGKRYPV 201
 
Name Accession Description Interval E-value
FimC COG3121
P pilus assembly protein, chaperone PapD [Extracellular structures];
7-241 1.63e-58

P pilus assembly protein, chaperone PapD [Extracellular structures];


Pssm-ID: 442355 [Multi-domain]  Cd Length: 237  Bit Score: 185.58  E-value: 1.63e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550724705   7 RSGLLSLLGITALTAVKAQAAATILLWPIDPWLSADARATELWIQNQGNSATTMQIRIVRWKQEGGYEryTAQQDVVASP 86
Cdd:COG3121    2 KRLLRLLLLALLLLLASAAAAAGISISPTRVIYPAGDKEASLTLTNTGDTPYLVQSWVDDWDQDAGPD--KATAPFVVTP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550724705  87 PIVTIAKGSKQLIRLIKQG-TIPSGVEQAYRIIVDEIPQPDAKAEPSMGLKLQMRYSIPLFVYGQGIPTLNEGEhhalan 165
Cdd:COG3121   80 PLFRLEPGKSQTVRIIRTGpPLPQDRESLFRLNVDEIPPKDASEEGKNTLQIALRTRIKLFYRPAGLKGSPEDA------ 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550724705 166 TQQLNWRVIqeegKPALEVRNQGQVHVRLSQVAVEQGGQKrtvAEGLLGYVLPGSTRSWPLPAGIYQPNRMS---AQIN 241
Cdd:COG3121  154 AEKLTWSLV----GNGLTVTNPGPYYVTLSDLSLGAGGKK---LKKGLGMVLPGSTRRWPLPAGASLAAGGKvtwATIN 225
PapD_N pfam00345
Pili and flagellar-assembly chaperone, PapD N-terminal domain; C2 domain-like beta-sandwich ...
39-153 3.70e-18

Pili and flagellar-assembly chaperone, PapD N-terminal domain; C2 domain-like beta-sandwich fold. This domain is the n-terminal part of the PapD chaperone protein for pilus and flagellar assembly.


Pssm-ID: 425623  Cd Length: 123  Bit Score: 77.63  E-value: 3.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550724705   39 LSADARATELWIQNQGNSATTMQIRIVRWKQEGGYEryTAQQDVVASPPIVTIAKGSKQLIRLIKQG-TIPSGVEQAYRI 117
Cdd:pfam00345  10 YPAGEKEASVTVSNTGDNPYLVQSWVDDGNEEGTDE--KAKAPFIVTPPLFRLEPGQEQVLRIYTTGpPLPTDRESLFWL 87
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 550724705  118 IVDEIPQPDAKAEPSMGLKLQMRYSIPLFVYGQGIP 153
Cdd:pfam00345  88 NVLEIPPKDKPKGGQNGLQLALRSRIKLFYRPAGLA 123
PRK09926 PRK09926
fimbrial chaperone;
83-208 4.52e-09

fimbrial chaperone;


Pssm-ID: 236634 [Multi-domain]  Cd Length: 246  Bit Score: 55.50  E-value: 4.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550724705  83 VASPPIVTIAKGSKQLIRLI--KQGTIPSGVEQAYRIIVDEIP-QPDAKAEPSMG-LKLQMRYSIPLFVYGQGIPTlNEG 158
Cdd:PRK09926  78 TATPPVSRIDPKRGQTIKLMytASTALPKDRESVFWFNVLEVPpKPDAEKVANQSlLQLAFRTRIKLFYRPDGLKG-NPS 156
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 550724705 159 EHHAlantqQLNWRVIQEEGKPALEVRNQGQVHVRLSQVAVEQGGQKRTV 208
Cdd:PRK09926 157 EAPL-----ALKWSWAGSEGKASLRVTNPTPYYVSFSSGDLEAGGKRYPV 201
PRK09918 PRK09918
putative fimbrial chaperone protein; Provisional
82-226 3.78e-05

putative fimbrial chaperone protein; Provisional


Pssm-ID: 236632 [Multi-domain]  Cd Length: 230  Bit Score: 43.49  E-value: 3.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550724705  82 VVASPPIVTIAKGSKQLIRLIKQGTIPSGVEQAYRIIVDEIPQ-PDAKAEPSMGLklqmRYSIPLFVYGQGIPTlnegeh 160
Cdd:PRK09918  71 LLVTPPVARVEPGQSQQVRFILKSGSPLNTEHLLRVSFEGVPPkPGGKNKVVMPI----RQDLPVLIQPAALPV------ 140
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550724705 161 hALANTQQLNWRViqeEGKpALEVRNQGQVHVRLSQVAVEQGGQKrtvaEGLLG--YVLPGSTRSWPL 226
Cdd:PRK09918 141 -VRDPWKLLVWSI---SGN-NLVVSNPSPYVVRLGQQVILLPSGK----VVALPkpYILPGESLTVAI 199
PRK15195 PRK15195
molecular chaperone FimC;
13-230 8.61e-04

molecular chaperone FimC;


Pssm-ID: 185117 [Multi-domain]  Cd Length: 229  Bit Score: 39.46  E-value: 8.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550724705  13 LLGITALTAVKAQAAATILLWPIDPWLSADARATELWIQnqgNSATTMQIRIVRWKQEGGYERytaQQDVVASPPIVTIA 92
Cdd:PRK15195  10 IIIFYLIISASVHAAGGIALGATRVIYPADAKQTSLAIR---NSHTNERYLVNSWIENSSGVK---EKSFIVTPPLFVSE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550724705  93 KGSKQLIRLIKQG-TIPSGVEQAYRIIVDEIPQPD-AKAEPSMGLKLQMRYSIPLFVYGQGIPTLNEgehHALAntqQLN 170
Cdd:PRK15195  84 PKSENTLRIIYAGpPLAADRESLFWMNVKAIPSVDkNALEGRNVLQLAILSRIKLFVRPINLQELPE---EAPD---TLK 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 550724705 171 WrviqEEGKPALEVRNQGQVHVRLsqVAVEQGGQKrtvaeglLGYVL--PGSTRSWPLPAGI 230
Cdd:PRK15195 158 F----SRSGNHLKVHNPSPYYVTL--VNLQVGSQK-------LGNAMiaPKVNSQIPLPSGV 206
 
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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