Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O25119

- FLIG_HELPY

UniProt

O25119 - FLIG_HELPY

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Flagellar motor switch protein FliG

Gene

fliG

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed - Annotation score: 4 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

  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 FliGImportedBy similarity
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: Chromosome, UP000010112: 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

  1. bacterial-type flagellum Source: UniProtKB
  2. plasma membrane Source: UniProtKB-KW
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.
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

        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.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 / 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: October 29, 2014
This is version 77 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