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Protein

Flagellar motor switch protein FliG

Gene

fliG

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei172 – 1721Part of the EHPQR-motif

GO - Molecular functioni

GO - Biological processi

  • bacterial-type flagellum-dependent swarming motility Source: UniProtKB
  • chemotaxis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Chemotaxis, Flagellar rotation

Enzyme and pathway databases

BioCyciHPY:HP0352-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Flagellar motor switch protein FliGBy similarityImported
Alternative name(s):
Flagellar motor switch protein GImported
Gene namesi
Name:fliGImported
Ordered Locus Names:C694_01785, HP_0352
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000429 Componenti: Chromosome

Subcellular locationi

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

GO - Cellular componenti

  • bacterial-type flagellum Source: UniProtKB
  • bacterial-type flagellum basal body Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Bacterial flagellum, Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi209 – 2091R → 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. 1 Publication
Mutagenesisi217 – 2171R → 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. 1 Publication
Mutagenesisi222 – 2221S → 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. 1 Publication
Mutagenesisi243 – 2431E → 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. 1 Publication
Mutagenesisi325 – 3251Q → 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. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 343343Flagellar motor switch protein FliGPRO_0000421839Add
BLAST

Proteomic databases

PRIDEiO25119.

Interactioni

Protein-protein interaction databases

DIPiDIP-3534N.
IntActiO25119. 5 interactions.
MINTiMINT-166826.
STRINGi85962.HP0352.

Structurei

Secondary structure

1
343
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni116 – 1194Combined sources
Helixi120 – 1245Combined sources
Helixi127 – 1348Combined sources
Helixi139 – 1468Combined sources
Helixi151 – 1588Combined sources
Helixi163 – 17311Combined sources
Helixi181 – 19414Combined sources
Helixi196 – 1994Combined sources
Helixi208 – 2169Combined sources
Helixi220 – 23314Combined sources
Helixi235 – 24410Combined sources
Helixi248 – 2536Combined sources
Helixi256 – 26510Combined sources
Helixi268 – 2747Combined sources
Helixi275 – 2773Combined sources
Helixi280 – 2889Combined sources
Helixi292 – 30514Combined sources
Helixi310 – 32920Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3USWX-ray2.60A86-343[»]
3USYX-ray2.71A/B116-343[»]
4FQ0X-ray2.82C/D116-205[»]
ProteinModelPortaliO25119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi137 – 1404Part of the EHPQR-motif
Motifi245 – 2484M-F-X-F motif; its intrinsic flexibility is probably coupled to flagellar rotation1 Publication

Sequence similaritiesi

Belongs to the FliG family.Sequence Analysis

Phylogenomic databases

KOiK02410.
OMAiFIEEMAY.
OrthoDBiEOG683S79.

Family and domain databases

Gene3Di1.10.220.30. 3 hits.
InterProiIPR000090. Flg_Motor_Flig.
IPR011002. FliG_a-hlx.
IPR028263. FliG_N.
[Graphical view]
PANTHERiPTHR30534. PTHR30534. 1 hit.
PfamiPF14842. FliG_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003161. FliG. 1 hit.
PRINTSiPR00954. FLGMOTORFLIG.
SUPFAMiSSF48029. SSF48029. 2 hits.
TIGRFAMsiTIGR00207. fliG. 1 hit.

Sequencei

Sequence statusi: Complete.

O25119-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATKLTPKQK AQLDELSMSE KIAILLIQVG EDTTGEILRH LDIDSITEIS
60 70 80 90 100
KQIVQLNGTD KQIGAAVLEE FFAIFQSNQY INTGGLEYAR ELLTRTLGSE
110 120 130 140 150
EAKKVMDKLT KSLQTQKNFA YLGKIKPQQL ADFIINEHPQ TIALILAHME
160 170 180 190 200
APNAAETLSY FPDEMKAEIS IRMANLGEIS PQVVKRVSTV LENKLESLTS
210 220 230 240 250
YKIEVGGLRA VAEIFNRLGQ KSAKTTLARI ESVDNKLAGA IKEMMFTFED
260 270 280 290 300
IVKLDNFAIR EILKVADKKD LSLALKTSTK DLTDKFLNNM SSRAAEQFVE
310 320 330 340
EMQYLGAVKI KDVDVAQRKI IEIVQSLQEK GVIQTGEEED VIE
Length:343
Mass (Da):38,326
Last modified:January 1, 1998 - v1
Checksum:i861214ED1782980A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD07420.1.
CP003904 Genomic DNA. Translation: AFV41574.1.
PIRiH64563.
RefSeqiNP_207150.1. NC_000915.1.
WP_000201853.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD07420; AAD07420; HP_0352.
AFV41574; AFV41574; C694_01785.
GeneIDi899214.
KEGGiheo:C694_01785.
hpy:HP0352.
PATRICi20591937. VBIHelPyl33062_0365.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000511 Genomic DNA. Translation: AAD07420.1.
CP003904 Genomic DNA. Translation: AFV41574.1.
PIRiH64563.
RefSeqiNP_207150.1. NC_000915.1.
WP_000201853.1. NC_018939.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3USWX-ray2.60A86-343[»]
3USYX-ray2.71A/B116-343[»]
4FQ0X-ray2.82C/D116-205[»]
ProteinModelPortaliO25119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-3534N.
IntActiO25119. 5 interactions.
MINTiMINT-166826.
STRINGi85962.HP0352.

Proteomic databases

PRIDEiO25119.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD07420; AAD07420; HP_0352.
AFV41574; AFV41574; C694_01785.
GeneIDi899214.
KEGGiheo:C694_01785.
hpy:HP0352.
PATRICi20591937. VBIHelPyl33062_0365.

Phylogenomic databases

KOiK02410.
OMAiFIEEMAY.
OrthoDBiEOG683S79.

Enzyme and pathway databases

BioCyciHPY:HP0352-MONOMER.

Family and domain databases

Gene3Di1.10.220.30. 3 hits.
InterProiIPR000090. Flg_Motor_Flig.
IPR011002. FliG_a-hlx.
IPR028263. FliG_N.
[Graphical view]
PANTHERiPTHR30534. PTHR30534. 1 hit.
PfamiPF14842. FliG_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003161. FliG. 1 hit.
PRINTSiPR00954. FLGMOTORFLIG.
SUPFAMiSSF48029. SSF48029. 2 hits.
TIGRFAMsiTIGR00207. fliG. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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 / 26695Imported.
  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: SS11 Publication.
  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 / 266951 Publication.

Entry informationi

Entry nameiFLIG_HELPY
AccessioniPrimary (citable) accession number: O25119
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2013
Last sequence update: January 1, 1998
Last modified: July 22, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Helicobacter pylori
    Helicobacter pylori (strain 26695): entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.