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Conserved domains on  [gi|120350|sp|P26608|]
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RecName: Full=Flagellar secretion chaperone FliS

Protein Classification

flagellar protein FliS( domain architecture ID 10015536)

FliS is a flagellin specific chaperone that facilitates the formation of alpha-helical secondary structure and prevents premature polymerization of flagellin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
fliS TIGR00208
flagellar biosynthetic protein FliS; The function of this protein in flagellar biosynthesis is ...
1-129 1.07e-56

flagellar biosynthetic protein FliS; The function of this protein in flagellar biosynthesis is unknown, but appears to be regulatory. The member of this family in Vibrio parahaemolyticus is designated FlaJ (creating a synonym for FliS) and was shown essential for flagellin biosynthesis. [Cellular processes, Chemotaxis and motility]


:

Pssm-ID: 188033  Cd Length: 124  Bit Score: 172.42  E-value: 1.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120350       1 MYAAKGTQAYAQIgvesAVMSASQQQLVTMLFDGVLSALVRASLFMQDNNQQGKGVSLSKAINIIEnGLRVSLDEESKDE 80
Cdd:TIGR00208   1 MAIANPYQAYQQN----SVNTASPGELTLMLYNGCLKFIRLAAQAIENDDIERKNENLIKAQNIIQ-ELNFTLDREKNIE 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 120350      81 LTQNLIALYSYMVRRLLQANLRNDVSAVEEVEALMRNIADAWKESLLSP 129
Cdd:TIGR00208  76 LSASLGALYDYMYRRLVQANIKNDTSKLAEVEGYVRDFRDAWKEAIQSE 124
 
Name Accession Description Interval E-value
fliS TIGR00208
flagellar biosynthetic protein FliS; The function of this protein in flagellar biosynthesis is ...
1-129 1.07e-56

flagellar biosynthetic protein FliS; The function of this protein in flagellar biosynthesis is unknown, but appears to be regulatory. The member of this family in Vibrio parahaemolyticus is designated FlaJ (creating a synonym for FliS) and was shown essential for flagellin biosynthesis. [Cellular processes, Chemotaxis and motility]


Pssm-ID: 188033  Cd Length: 124  Bit Score: 172.42  E-value: 1.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120350       1 MYAAKGTQAYAQIgvesAVMSASQQQLVTMLFDGVLSALVRASLFMQDNNQQGKGVSLSKAINIIEnGLRVSLDEESKDE 80
Cdd:TIGR00208   1 MAIANPYQAYQQN----SVNTASPGELTLMLYNGCLKFIRLAAQAIENDDIERKNENLIKAQNIIQ-ELNFTLDREKNIE 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 120350      81 LTQNLIALYSYMVRRLLQANLRNDVSAVEEVEALMRNIADAWKESLLSP 129
Cdd:TIGR00208  76 LSASLGALYDYMYRRLVQANIKNDTSKLAEVEGYVRDFRDAWKEAIQSE 124
FliS COG1516
Flagellin-specific chaperone FliS [Cell motility, Intracellular trafficking, secretion, and ...
16-124 1.19e-39

Flagellin-specific chaperone FliS [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441125  Cd Length: 113  Bit Score: 128.78  E-value: 1.19e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120350    16 ESAVMSASQQQLVTMLFDGVLSALVRASLFMQDNNQQGKGVSLSKAINIIeNGLRVSLDEESKDELTQNLIALYSYMVRR 95
Cdd:COG1516   1 ENSVATASPHQLILMLYDGALKFLARAKGAIERGDIEEKGEAISKAQDII-SELRASLDMEKGGEIAKNLDALYDYMIRR 79
                        90       100
                ....*....|....*....|....*....
gi 120350    96 LLQANLRNDVSAVEEVEALMRNIADAWKE 124
Cdd:COG1516  80 LLEANLKNDAEILDEVIRLLEELRDAWKE 108
FliS pfam02561
Flagellar protein FliS; FliS is coded for by the FliD operon and is transcribed in conjunction ...
8-124 9.27e-39

Flagellar protein FliS; FliS is coded for by the FliD operon and is transcribed in conjunction with FliD and FliT, however this protein has no known function.


Pssm-ID: 460591  Cd Length: 115  Bit Score: 126.83  E-value: 9.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120350       8 QAYAQigveSAVMSASQQQLVTMLFDGVLSALVRASLFMQDNNQQGKGVSLSKAINIIeNGLRVSLDEESKDELTQNLIA 87
Cdd:pfam02561   2 QAYQQ----NSVATASPHQLILMLYDGAIKFLKQAKEAIEEGDIEKKGEAISKAQDII-SELRATLDMEAGGEIAKNLDA 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 120350      88 LYSYMVRRLLQANLRNDVSAVEEVEALMRNIADAWKE 124
Cdd:pfam02561  77 LYDYMIRRLLEANLKKDPEILDEVIGLLEELRDAWKE 113
FliS cd16098
flagellar export chaperone FliS; This family contains flagellar export chaperone FliS, a ...
25-124 6.25e-31

flagellar export chaperone FliS; This family contains flagellar export chaperone FliS, a protein critical for flagellar assembly and bacterial colonization. FliS prevents premature polymerization of flagellins, the major protein of the filament, by regulating interactions between structural components of the bacterial flagellum in the cytosol. It binds specifically to FliC (flagellin) which is sequentially secreted in large numbers through the central channel of the flagellum and polymerized to form the tail filament. FliS protects FliC from degradation and aggregation by binding to the FliC C-terminal helical domain, which contributes to stabilization of flagellin subunit interactions during polymerization. FliS has been shown to interact specifically with FlgM, whose role is to inhibit FliA, a flagellum-specific RNA polymerase responsible for flagellin transcription; FliA competes with FliS for FlgM binding.


Pssm-ID: 294015  Cd Length: 102  Bit Score: 106.48  E-value: 6.25e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120350    25 QQLVTMLFDGVLSALVRASLFMQDNNQQGKGVSLSKAINIIeNGLRVSLDEESKDELTQNLIALYSYMVRRLLQANLRND 104
Cdd:cd16098   2 HQLVVMLYDGAIRFLKRAKEAIEEGDIEEKGEALSKAQDII-GELLSSLDFEKGGEIAKNLDALYDYMLRRLLEANLKND 80
                        90       100
                ....*....|....*....|
gi 120350   105 VSAVEEVEALMRNIADAWKE 124
Cdd:cd16098  81 AEKLDEVIELLTELREAWKE 100
 
Name Accession Description Interval E-value
fliS TIGR00208
flagellar biosynthetic protein FliS; The function of this protein in flagellar biosynthesis is ...
1-129 1.07e-56

flagellar biosynthetic protein FliS; The function of this protein in flagellar biosynthesis is unknown, but appears to be regulatory. The member of this family in Vibrio parahaemolyticus is designated FlaJ (creating a synonym for FliS) and was shown essential for flagellin biosynthesis. [Cellular processes, Chemotaxis and motility]


Pssm-ID: 188033  Cd Length: 124  Bit Score: 172.42  E-value: 1.07e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120350       1 MYAAKGTQAYAQIgvesAVMSASQQQLVTMLFDGVLSALVRASLFMQDNNQQGKGVSLSKAINIIEnGLRVSLDEESKDE 80
Cdd:TIGR00208   1 MAIANPYQAYQQN----SVNTASPGELTLMLYNGCLKFIRLAAQAIENDDIERKNENLIKAQNIIQ-ELNFTLDREKNIE 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 120350      81 LTQNLIALYSYMVRRLLQANLRNDVSAVEEVEALMRNIADAWKESLLSP 129
Cdd:TIGR00208  76 LSASLGALYDYMYRRLVQANIKNDTSKLAEVEGYVRDFRDAWKEAIQSE 124
FliS COG1516
Flagellin-specific chaperone FliS [Cell motility, Intracellular trafficking, secretion, and ...
16-124 1.19e-39

Flagellin-specific chaperone FliS [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 441125  Cd Length: 113  Bit Score: 128.78  E-value: 1.19e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120350    16 ESAVMSASQQQLVTMLFDGVLSALVRASLFMQDNNQQGKGVSLSKAINIIeNGLRVSLDEESKDELTQNLIALYSYMVRR 95
Cdd:COG1516   1 ENSVATASPHQLILMLYDGALKFLARAKGAIERGDIEEKGEAISKAQDII-SELRASLDMEKGGEIAKNLDALYDYMIRR 79
                        90       100
                ....*....|....*....|....*....
gi 120350    96 LLQANLRNDVSAVEEVEALMRNIADAWKE 124
Cdd:COG1516  80 LLEANLKNDAEILDEVIRLLEELRDAWKE 108
FliS pfam02561
Flagellar protein FliS; FliS is coded for by the FliD operon and is transcribed in conjunction ...
8-124 9.27e-39

Flagellar protein FliS; FliS is coded for by the FliD operon and is transcribed in conjunction with FliD and FliT, however this protein has no known function.


Pssm-ID: 460591  Cd Length: 115  Bit Score: 126.83  E-value: 9.27e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120350       8 QAYAQigveSAVMSASQQQLVTMLFDGVLSALVRASLFMQDNNQQGKGVSLSKAINIIeNGLRVSLDEESKDELTQNLIA 87
Cdd:pfam02561   2 QAYQQ----NSVATASPHQLILMLYDGAIKFLKQAKEAIEEGDIEKKGEAISKAQDII-SELRATLDMEAGGEIAKNLDA 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 120350      88 LYSYMVRRLLQANLRNDVSAVEEVEALMRNIADAWKE 124
Cdd:pfam02561  77 LYDYMIRRLLEANLKKDPEILDEVIGLLEELRDAWKE 113
FliS cd16098
flagellar export chaperone FliS; This family contains flagellar export chaperone FliS, a ...
25-124 6.25e-31

flagellar export chaperone FliS; This family contains flagellar export chaperone FliS, a protein critical for flagellar assembly and bacterial colonization. FliS prevents premature polymerization of flagellins, the major protein of the filament, by regulating interactions between structural components of the bacterial flagellum in the cytosol. It binds specifically to FliC (flagellin) which is sequentially secreted in large numbers through the central channel of the flagellum and polymerized to form the tail filament. FliS protects FliC from degradation and aggregation by binding to the FliC C-terminal helical domain, which contributes to stabilization of flagellin subunit interactions during polymerization. FliS has been shown to interact specifically with FlgM, whose role is to inhibit FliA, a flagellum-specific RNA polymerase responsible for flagellin transcription; FliA competes with FliS for FlgM binding.


Pssm-ID: 294015  Cd Length: 102  Bit Score: 106.48  E-value: 6.25e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 120350    25 QQLVTMLFDGVLSALVRASLFMQDNNQQGKGVSLSKAINIIeNGLRVSLDEESKDELTQNLIALYSYMVRRLLQANLRND 104
Cdd:cd16098   2 HQLVVMLYDGAIRFLKRAKEAIEEGDIEEKGEALSKAQDII-GELLSSLDFEKGGEIAKNLDALYDYMLRRLLEANLKND 80
                        90       100
                ....*....|....*....|
gi 120350   105 VSAVEEVEALMRNIADAWKE 124
Cdd:cd16098  81 AEKLDEVIELLTELREAWKE 100
 
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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