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O25119

- FLIG_HELPY

UniProt

O25119 - FLIG_HELPY

Protein

Flagellar motor switch protein FliG

Gene

fliG

Organism
Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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

    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. bacterial-type flagellum basal body Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB-SubCell

    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 – 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.
    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

    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

    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 1, 2014
    This is version 76 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