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O25119

- FLIG_HELPY

UniProt

O25119 - FLIG_HELPY

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Protein
Flagellar motor switch protein FliG
Gene
fliG, C694_01785, HP_0352
Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed - 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.2 Publications

Sites

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

GO - Molecular functioni

  1. motor activity Source: InterPro

GO - Biological processi

  1. bacterial-type flagellum-dependent swarming motility Source: UniProtKB
  2. 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 FliG
Alternative name(s):
Flagellar motor switch protein G
Gene namesi
Name:fliG
Ordered Locus Names:C694_01785, HP_0352
OrganismiHelicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Taxonomic identifieri85962 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000429: Chromosome, UP000010112: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. bacterial-type flagellum Source: UniProtKB
  2. bacterial-type flagellum basal body Source: UniProtKB-SubCell
  3. 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 FliG
PRO_0000421839Add
BLAST

Proteomic databases

PRIDEiO25119.

Interactioni

Protein-protein interaction databases

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

Structurei

Secondary structure

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

3D structure databases

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

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 rotation

Sequence similaritiesi

Belongs to the FliG family.

Phylogenomic databases

KOiK02410.
OMAiLRRMATI.
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

MATKLTPKQK AQLDELSMSE KIAILLIQVG EDTTGEILRH LDIDSITEIS    50
KQIVQLNGTD KQIGAAVLEE FFAIFQSNQY INTGGLEYAR ELLTRTLGSE 100
EAKKVMDKLT KSLQTQKNFA YLGKIKPQQL ADFIINEHPQ TIALILAHME 150
APNAAETLSY FPDEMKAEIS IRMANLGEIS PQVVKRVSTV LENKLESLTS 200
YKIEVGGLRA VAEIFNRLGQ KSAKTTLARI ESVDNKLAGA IKEMMFTFED 250
IVKLDNFAIR EILKVADKKD LSLALKTSTK DLTDKFLNNM SSRAAEQFVE 300
EMQYLGAVKI KDVDVAQRKI IEIVQSLQEK GVIQTGEEED VIE 343
Length:343
Mass (Da):38,326
Last modified:January 1, 1998 - v1
Checksum:i861214ED1782980A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000511 Genomic DNA. Translation: AAD07420.1.
CP003904 Genomic DNA. Translation: AFV41574.1.
PIRiH64563.
RefSeqiNP_207150.1. NC_000915.1.
YP_006934277.1. NC_018939.1.

Genome annotation databases

EnsemblBacteriaiAAD07420; AAD07420; HP_0352.
AFV41574; AFV41574; C694_01785.
GeneIDi13869536.
899214.
KEGGiheo:C694_01785.
hpy:HP0352.
PATRICi20591937. VBIHelPyl33062_0365.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE000511 Genomic DNA. Translation: AAD07420.1 .
CP003904 Genomic DNA. Translation: AFV41574.1 .
PIRi H64563.
RefSeqi NP_207150.1. NC_000915.1.
YP_006934277.1. NC_018939.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3USW X-ray 2.60 A 86-343 [» ]
3USY X-ray 2.71 A/B 116-343 [» ]
4FQ0 X-ray 2.82 C/D 116-205 [» ]
ProteinModelPortali O25119.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-3534N.
IntActi O25119. 5 interactions.
MINTi MINT-166826.
STRINGi 85962.HP0352.

Proteomic databases

PRIDEi O25119.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAD07420 ; AAD07420 ; HP_0352 .
AFV41574 ; AFV41574 ; C694_01785 .
GeneIDi 13869536.
899214.
KEGGi heo:C694_01785.
hpy:HP0352.
PATRICi 20591937. VBIHelPyl33062_0365.

Phylogenomic databases

KOi K02410.
OMAi LRRMATI.
OrthoDBi EOG683S79.

Enzyme and pathway databases

BioCyci HPY:HP0352-MONOMER.

Family and domain databases

Gene3Di 1.10.220.30. 3 hits.
InterProi IPR000090. Flg_Motor_Flig.
IPR011002. FliG_a-hlx.
IPR028263. FliG_N.
[Graphical view ]
PANTHERi PTHR30534. PTHR30534. 1 hit.
Pfami PF14842. FliG_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF003161. FliG. 1 hit.
PRINTSi PR00954. FLGMOTORFLIG.
SUPFAMi SSF48029. SSF48029. 2 hits.
TIGRFAMsi TIGR00207. fliG. 1 hit.
ProtoNeti Search...

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 / 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.

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: September 3, 2014
This is version 75 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

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