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Conserved domains on  [gi|1959262011|ref|WP_201733425|]
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flagellar export chaperone FliS [Acidithrix sp. C25]

Protein Classification

flagellar export chaperone FliS( domain architecture ID 10495230)

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

CATH:  1.20.120.340
Gene Symbol:  fliS
Gene Ontology:  GO:0044780
PubMed:  12958592

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FliS pfam02561
Flagellar protein FliS; FliS is coded for by the FliD operon and is transcribed in conjunction ...
 8-118 5.29e-24

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: 89.08  E-value: 5.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262011   8 YVKDAILTASPTQRLLMFLDRLEIDMKRAEIGFDEANVQSRNDALIHAQEIILHLRDSLRPDIW-DGAIQLASVYGFIYS 86
Cdd:pfam02561   4 YQQNSVATASPHQLILMLYDGAIKFLKQAKEAIEEGDIEKKGEAISKAQDIISELRATLDMEAGgEIAKNLDALYDYMIR 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1959262011  87 ELVYANIRADRKRFDVAYKLILQIIMAWRGAA 118
Cdd:pfam02561  84 RLLEANLKKDPEILDEVIGLLEELRDAWKEIA 115
 
Name Accession Description Interval E-value
FliS pfam02561
Flagellar protein FliS; FliS is coded for by the FliD operon and is transcribed in conjunction ...
 8-118 5.29e-24

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: 89.08  E-value: 5.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262011   8 YVKDAILTASPTQRLLMFLDRLEIDMKRAEIGFDEANVQSRNDALIHAQEIILHLRDSLRPDIW-DGAIQLASVYGFIYS 86
Cdd:pfam02561   4 YQQNSVATASPHQLILMLYDGAIKFLKQAKEAIEEGDIEKKGEAISKAQDIISELRATLDMEAGgEIAKNLDALYDYMIR 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1959262011  87 ELVYANIRADRKRFDVAYKLILQIIMAWRGAA 118
Cdd:pfam02561  84 RLLEANLKKDPEILDEVIGLLEELRDAWKEIA 115
FliS COG1516
Flagellin-specific chaperone FliS [Cell motility, Intracellular trafficking, secretion, and ...
 10-120 1.42e-22

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


Pssm-ID: 441125  Cd Length: 113  Bit Score: 85.25  E-value: 1.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262011  10 KDAILTASPTQRLLMFLDRLEIDMKRAEIGFDEANVQSRNDALIHAQEIILHLRDSLRPDIW-DGAIQLASVYGFIYSEL 88
Cdd:COG1516     1 ENSVATASPHQLILMLYDGALKFLARAKGAIERGDIEEKGEAISKAQDIISELRASLDMEKGgEIAKNLDALYDYMIRRL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1959262011  89 VYANIRADRKRFDVAYKLILQIIMAWRGAANQ 120
Cdd:COG1516    81 LEANLKNDAEILDEVIRLLEELRDAWKEIAKQ 112
FliS cd16098
flagellar export chaperone FliS; This family contains flagellar export chaperone FliS, a ...
 18-118 3.38e-19

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: 76.43  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262011  18 PTQRLLMFLDRLEIDMKRAEIGFDEANVQSRNDALIHAQEIILHLRDSLRPD-IWDGAIQLASVYGFIYSELVYANIRAD 96
Cdd:cd16098     1 PHQLVVMLYDGAIRFLKRAKEAIEEGDIEEKGEALSKAQDIIGELLSSLDFEkGGEIAKNLDALYDYMLRRLLEANLKND 80

                          90       100
                  ....*....|....*....|..
gi 1959262011  97 RKRFDVAYKLILQIIMAWRGAA 118
Cdd:cd16098    81 AEKLDEVIELLTELREAWKEAA 102
fliS TIGR00208
flagellar biosynthetic protein FliS; The function of this protein in flagellar biosynthesis is ...
 8-115 2.81e-07

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: 46.08  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262011   8 YVKDAILTASPTQRLLMFLDRLEIDMKRAEIGFDEANVQSRNDALIHAQEIILHLRDSLRPDIWDG-AIQLASVYGFIYS 86
Cdd:TIGR00208  10 YQQNSVNTASPGELTLMLYNGCLKFIRLAAQAIENDDIERKNENLIKAQNIIQELNFTLDREKNIElSASLGALYDYMYR 89

                          90       100
                  ....*....|....*....|....*....
gi 1959262011  87 ELVYANIRADRKRFDVAYKLILQIIMAWR 115
Cdd:TIGR00208  90 RLVQANIKNDTSKLAEVEGYVRDFRDAWK 118
 
Name Accession Description Interval E-value
FliS pfam02561
Flagellar protein FliS; FliS is coded for by the FliD operon and is transcribed in conjunction ...
 8-118 5.29e-24

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: 89.08  E-value: 5.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262011   8 YVKDAILTASPTQRLLMFLDRLEIDMKRAEIGFDEANVQSRNDALIHAQEIILHLRDSLRPDIW-DGAIQLASVYGFIYS 86
Cdd:pfam02561   4 YQQNSVATASPHQLILMLYDGAIKFLKQAKEAIEEGDIEKKGEAISKAQDIISELRATLDMEAGgEIAKNLDALYDYMIR 83

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1959262011  87 ELVYANIRADRKRFDVAYKLILQIIMAWRGAA 118
Cdd:pfam02561  84 RLLEANLKKDPEILDEVIGLLEELRDAWKEIA 115
FliS COG1516
Flagellin-specific chaperone FliS [Cell motility, Intracellular trafficking, secretion, and ...
 10-120 1.42e-22

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


Pssm-ID: 441125  Cd Length: 113  Bit Score: 85.25  E-value: 1.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262011  10 KDAILTASPTQRLLMFLDRLEIDMKRAEIGFDEANVQSRNDALIHAQEIILHLRDSLRPDIW-DGAIQLASVYGFIYSEL 88
Cdd:COG1516     1 ENSVATASPHQLILMLYDGALKFLARAKGAIERGDIEEKGEAISKAQDIISELRASLDMEKGgEIAKNLDALYDYMIRRL 80

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1959262011  89 VYANIRADRKRFDVAYKLILQIIMAWRGAANQ 120
Cdd:COG1516    81 LEANLKNDAEILDEVIRLLEELRDAWKEIAKQ 112
FliS cd16098
flagellar export chaperone FliS; This family contains flagellar export chaperone FliS, a ...
 18-118 3.38e-19

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: 76.43  E-value: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262011  18 PTQRLLMFLDRLEIDMKRAEIGFDEANVQSRNDALIHAQEIILHLRDSLRPD-IWDGAIQLASVYGFIYSELVYANIRAD 96
Cdd:cd16098     1 PHQLVVMLYDGAIRFLKRAKEAIEEGDIEEKGEALSKAQDIIGELLSSLDFEkGGEIAKNLDALYDYMLRRLLEANLKND 80

                          90       100
                  ....*....|....*....|..
gi 1959262011  97 RKRFDVAYKLILQIIMAWRGAA 118
Cdd:cd16098    81 AEKLDEVIELLTELREAWKEAA 102
fliS TIGR00208
flagellar biosynthetic protein FliS; The function of this protein in flagellar biosynthesis is ...
 8-115 2.81e-07

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: 46.08  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1959262011   8 YVKDAILTASPTQRLLMFLDRLEIDMKRAEIGFDEANVQSRNDALIHAQEIILHLRDSLRPDIWDG-AIQLASVYGFIYS 86
Cdd:TIGR00208  10 YQQNSVNTASPGELTLMLYNGCLKFIRLAAQAIENDDIERKNENLIKAQNIIQELNFTLDREKNIElSASLGALYDYMYR 89

                          90       100
                  ....*....|....*....|....*....
gi 1959262011  87 ELVYANIRADRKRFDVAYKLILQIIMAWR 115
Cdd:TIGR00208  90 RLVQANIKNDTSKLAEVEGYVRDFRDAWK 118
HAD_PNPase_UmpH-like cd07532
UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium ...
 4-69 9.50e-03

UmpH/NagD family phosphatase para nitrophenyl phosphate phosphatase, similar to Plasmodium falciparum PNPase; Plasmodium falciparum para nitrophenyl phosphate phosphatase (PNPase) catalyzes the dephosphorylation of thiamine monophosphate to thiamine, other substrates on which its active are nucleotides, phosphorylated sugars, pyridoxal-5-phosphate, and paranitrophenyl phosphate. This subfamily belongs to the UmpH/NagD phosphatase family, and to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319834 [Multi-domain]  Cd Length: 286  Bit Score: 34.59  E-value: 9.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1959262011   4 KPNDYVKDAILTAS--PTQRLLMFLDRLEIDMKRAEI-GFDEANVQSRNDALIHAQEIILH---LRDSLRPD 69
Cdd:cd07532   206 KPNPQILNFLMKSGviKPERTLMIGDRLKTDILFANNcGFQSLLVGTGVNSLEDAEKIKKEgdpKKKDLVPD 277
 
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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