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Conserved domains on  [gi|299856721|pdb|3K1I|D]
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Chain D, Crystal strcture of FliS-HP1076 complex in H. pylori

Protein Classification

flagellar FLiS export co-chaperone( domain architecture ID 11243648)

flagellar FLiS export co-chaperone similar to Helicobacter pylori HP1076

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FliS_cochap pfam16522
Flagellar FLiS export co-chaperone, HP1076; FliS_cochap is a family of largely ...
 13-155 7.87e-62

Flagellar FLiS export co-chaperone, HP1076; FliS_cochap is a family of largely Campylobacterales proteins that are co-chaperones for FliS, one of the type III secretion system flagellar chaperones. The HP1076 (Flis_cochap) and FliS complex together prevents premature polymerization of flagellins and is critical for flagellar assembly and bacterial colonization. The HP1076 shows co-chaperone activity that promotes protein folding of FliS with mutations in the flagellin binding pocket and enhances the chaperone activity of FliS.


:

Pssm-ID: 435395  Cd Length: 146  Bit Score: 188.11  E-value: 7.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K1I_D         13 TLQKHLGDVETSDFTTNAIEKSQQIAKFSRDMKNINESVGALQVLQIACKKLFN--KSMGLEDKDAlQASIIKQELREIV 90
Cdd:pfam16522   1 TLQKHLGDIETQEFEINTGQNSRKIHKFSEDIKGANEFIGALQVLDIALKKILKlaKSIGEESSDD-QKSQVKATMQEII 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3K1I_D         91 ENCQFLASPLFDTQLNIAINDEIFSMIVVNPLDLLENVGE--FQAYLEEKLNEIKELLGYLSESLSN 155
Cdd:pfam16522  80 ENCSFMGVALFDTQLNTYLNKKSFEFEIANPLLLLETSGYesLIAYIEDKREEIKQMLSELSEALSE 146
 
Name Accession Description Interval E-value
FliS_cochap pfam16522
Flagellar FLiS export co-chaperone, HP1076; FliS_cochap is a family of largely ...
 13-155 7.87e-62

Flagellar FLiS export co-chaperone, HP1076; FliS_cochap is a family of largely Campylobacterales proteins that are co-chaperones for FliS, one of the type III secretion system flagellar chaperones. The HP1076 (Flis_cochap) and FliS complex together prevents premature polymerization of flagellins and is critical for flagellar assembly and bacterial colonization. The HP1076 shows co-chaperone activity that promotes protein folding of FliS with mutations in the flagellin binding pocket and enhances the chaperone activity of FliS.


Pssm-ID: 435395  Cd Length: 146  Bit Score: 188.11  E-value: 7.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K1I_D         13 TLQKHLGDVETSDFTTNAIEKSQQIAKFSRDMKNINESVGALQVLQIACKKLFN--KSMGLEDKDAlQASIIKQELREIV 90
Cdd:pfam16522   1 TLQKHLGDIETQEFEINTGQNSRKIHKFSEDIKGANEFIGALQVLDIALKKILKlaKSIGEESSDD-QKSQVKATMQEII 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3K1I_D         91 ENCQFLASPLFDTQLNIAINDEIFSMIVVNPLDLLENVGE--FQAYLEEKLNEIKELLGYLSESLSN 155
Cdd:pfam16522  80 ENCSFMGVALFDTQLNTYLNKKSFEFEIANPLLLLETSGYesLIAYIEDKREEIKQMLSELSEALSE 146
 
Name Accession Description Interval E-value
FliS_cochap pfam16522
Flagellar FLiS export co-chaperone, HP1076; FliS_cochap is a family of largely ...
 13-155 7.87e-62

Flagellar FLiS export co-chaperone, HP1076; FliS_cochap is a family of largely Campylobacterales proteins that are co-chaperones for FliS, one of the type III secretion system flagellar chaperones. The HP1076 (Flis_cochap) and FliS complex together prevents premature polymerization of flagellins and is critical for flagellar assembly and bacterial colonization. The HP1076 shows co-chaperone activity that promotes protein folding of FliS with mutations in the flagellin binding pocket and enhances the chaperone activity of FliS.


Pssm-ID: 435395  Cd Length: 146  Bit Score: 188.11  E-value: 7.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3K1I_D         13 TLQKHLGDVETSDFTTNAIEKSQQIAKFSRDMKNINESVGALQVLQIACKKLFN--KSMGLEDKDAlQASIIKQELREIV 90
Cdd:pfam16522   1 TLQKHLGDIETQEFEINTGQNSRKIHKFSEDIKGANEFIGALQVLDIALKKILKlaKSIGEESSDD-QKSQVKATMQEII 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
3K1I_D         91 ENCQFLASPLFDTQLNIAINDEIFSMIVVNPLDLLENVGE--FQAYLEEKLNEIKELLGYLSESLSN 155
Cdd:pfam16522  80 ENCSFMGVALFDTQLNTYLNKKSFEFEIANPLLLLETSGYesLIAYIEDKREEIKQMLSELSEALSE 146
 
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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