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O25119 (FLIG_HELPY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Flagellar motor switch protein FliG
Alternative name(s):
Flagellar motor switch protein G
Gene names
Name:fliG
Ordered Locus Names:C694_01785, HP_0352
OrganismHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]
Taxonomic identifier85962 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length343 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation. Required for flagellum synthesis and motility. In H.pylori four flagellar switch proteins are encoded, FliG, FliM, FliN and FliY. Ref.3 Ref.4

Subcellular location

Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Bacterial flagellum basal body By similarity.

Disruption phenotype

Nonflagellate. Forms dense colonies without swarming in contrast to the wild-type which forms diffuse colonies with large, swarming halos. Expression of flagellins FlaA and FlaB and the hook protein FlgE greatly reduced. Ref.3

Sequence similarities

Belongs to the FliG family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 343343Flagellar motor switch protein FliG
PRO_0000421839

Regions

Motif137 – 1404Part of the EHPQR-motif
Motif245 – 2484M-F-X-F motif; its intrinsic flexibility is probably coupled to flagellar rotation

Sites

Site1721Part of the EHPQR-motif

Experimental info

Mutagenesis2091R → C: A prominent downward mobility shift in SDS-PAGE and a reduction in the fluorescence intensity upon 5-iodoacetamidofluorescein (5-IAF) haloalkylation after cysteine cross-linking suggest formation of disulfide bonds, hence closeness of corresponding wild-type residues; when associated with C-325. Ref.4
Mutagenesis2171R → C: A slight downward mobility shift in SDS-PAGE and a reduction in the fluorescence intensity upon 5-iodoacetamidofluorescein (5-IAF) haloalkylation after cysteine cross-linking suggest formation of disulfide bonds, hence closeness of corresponding wild-type residues; when associated with C-325. Ref.4
Mutagenesis2221S → C: A prominent downward mobility shift in SDS-PAGE and a reduction in the fluorescence intensity upon 5-iodoacetamidofluorescein (5-IAF) haloalkylation after cysteine cross-linking suggest formation of disulfide bonds, hence closeness of corresponding wild-type residues; when associated with C-325. Ref.4
Mutagenesis2431E → C: A complete upward mobility shift in SDS-PAGE and a reduction in the fluorescence intensity upon 5-iodoacetamidofluorescein (5-IAF) haloalkylation after cysteine cross-linking suggest formation of disulfide bonds, hence closeness of corresponding wild-type residues; when associated with C-325. Ref.4
Mutagenesis3251Q → C: No mobility shift in SDS-PAGE nor reduction in the fluorescence intensity upon 5-iodoacetamidofluorescein (5-IAF) haloalkylation after cysteine cross-linking. A mobility shift and reduction in the fluorescence intensity after cysteine cross-linking suggest formation of disulfide bonds, hence closeness of corresponding wild-type residues; when associated either with C-209; C-217; C-222 or C-243. Ref.4

Secondary structure

................................... 343
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O25119 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 861214ED1782980A

FASTA34338,326
        10         20         30         40         50         60 
MATKLTPKQK AQLDELSMSE KIAILLIQVG EDTTGEILRH LDIDSITEIS KQIVQLNGTD 

        70         80         90        100        110        120 
KQIGAAVLEE FFAIFQSNQY INTGGLEYAR ELLTRTLGSE EAKKVMDKLT KSLQTQKNFA 

       130        140        150        160        170        180 
YLGKIKPQQL ADFIINEHPQ TIALILAHME APNAAETLSY FPDEMKAEIS IRMANLGEIS 

       190        200        210        220        230        240 
PQVVKRVSTV LENKLESLTS YKIEVGGLRA VAEIFNRLGQ KSAKTTLARI ESVDNKLAGA 

       250        260        270        280        290        300 
IKEMMFTFED IVKLDNFAIR EILKVADKKD LSLALKTSTK DLTDKFLNNM SSRAAEQFVE 

       310        320        330        340 
EMQYLGAVKI KDVDVAQRKI IEIVQSLQEK GVIQTGEEED VIE 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of the gastric pathogen Helicobacter pylori."
Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. expand/collapse author list , Khalak H.G., Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.
Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700392 / 26695.
[2]"Draft genome of Helicobacter pylori."
Manolov A., Prihodko E., Larin A., Karpova I., Semashko T., Alexeev D., Kostrjukova E., Govorun V.
Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700392 / 26695.
[3]"Mutational analysis of genes encoding the early flagellar components of Helicobacter pylori: evidence for transcriptional regulation of flagellin A biosynthesis."
Allan E., Dorrell N., Foynes S., Anyim M., Wren B.W.
J. Bacteriol. 182:5274-5277(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
Strain: SS1.
[4]"Multiple conformations of the FliG C-terminal domain provide insight into flagellar motor switching."
Lam K.H., Ip W.S., Lam Y.W., Chan S.O., Ling T.K., Au S.W.
Structure 20:315-325(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 86-343, FUNCTION, MOTIF, MUTAGENESIS OF ARG-209; ARG-217; SER-222; GLU-243 AND GLN-325.
Strain: ATCC 700392 / 26695.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000511 Genomic DNA. Translation: AAD07420.1.
CP003904 Genomic DNA. Translation: AFV41574.1.
PIRH64563.
RefSeqNP_207150.1. NC_000915.1.
YP_006934277.1. NC_018939.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3USWX-ray2.60A86-343[»]
3USYX-ray2.71A/B116-343[»]
4FQ0X-ray2.82C/D116-205[»]
ProteinModelPortalO25119.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-3534N.
IntActO25119. 1 interaction.
MINTMINT-166826.
STRING85962.HP0352.

Proteomic databases

PRIDEO25119.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD07420; AAD07420; HP_0352.
AFV41574; AFV41574; C694_01785.
GeneID13869536.
899214.
KEGGheo:C694_01785.
hpy:HP0352.
PATRIC20591937. VBIHelPyl33062_0365.

Phylogenomic databases

KOK02410.
OMAKERNDIM.
OrthoDBEOG683S79.
ProtClustDBPRK05686.

Enzyme and pathway databases

BioCycHPY:HP0352-MONOMER.

Family and domain databases

Gene3D1.10.220.30. 3 hits.
InterProIPR000090. Flg_Motor_Flig.
IPR011002. FliG_a-hlx.
IPR028263. FliG_N.
[Graphical view]
PANTHERPTHR30534. PTHR30534. 1 hit.
PfamPF14842. FliG_N. 1 hit.
[Graphical view]
PIRSFPIRSF003161. FliG. 1 hit.
PRINTSPR00954. FLGMOTORFLIG.
SUPFAMSSF48029. SSF48029. 2 hits.
TIGRFAMsTIGR00207. fliG. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFLIG_HELPY
AccessionPrimary (citable) accession number: O25119
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names