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P06974

- FLIM_ECOLI

UniProt

P06974 - FLIM_ECOLI

Protein

Flagellar motor switch protein FliM

Gene

fliM

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    Functioni

    FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation.

    GO - Molecular functioni

    1. motor activity Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. bacterial-type flagellum-dependent cell motility Source: InterPro
    2. chemotaxis Source: UniProtKB-KW

    Keywords - Biological processi

    Chemotaxis, Flagellar rotation

    Enzyme and pathway databases

    BioCyciEcoCyc:FLIM-FLAGELLAR-C-RING-SWITCH.
    ECOL316407:JW1929-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Flagellar motor switch protein FliM
    Gene namesi
    Name:fliM
    Synonyms:cheC2, fla AII, fla QII
    Ordered Locus Names:b1945, JW1929
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10323. fliM.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Bacterial flagellum, Cell inner membrane, Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi153 – 1531V → D: Decreases binding to YcgR. 1 Publication
    Mutagenesisi155 – 1551N → E: Decreases binding to YcgR. 1 Publication
    Mutagenesisi156 – 1561R → D: Obviates binding to YcgR. 1 Publication
    Mutagenesisi160 – 1601L → E: Obviates binding to YcgR. 1 Publication
    Mutagenesisi167 – 1671D → R: Decreases binding to YcgR. 1 Publication
    Mutagenesisi176 – 1761E → R: Decreases binding to YcgR. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 334334Flagellar motor switch protein FliMPRO_0000180928Add
    BLAST

    Proteomic databases

    PaxDbiP06974.
    PRIDEiP06974.

    Expressioni

    Gene expression databases

    GenevestigatoriP06974.

    Interactioni

    Subunit structurei

    Interacts with flagellar brake protein YcgR.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    fliGP0ABZ116EBI-560439,EBI-1126524
    fliNP150707EBI-560439,EBI-2011987
    ycgRP760103EBI-560439,EBI-554507

    Protein-protein interaction databases

    DIPiDIP-1100N.
    IntActiP06974. 18 interactions.
    MINTiMINT-1301311.
    STRINGi511145.b1945.

    Structurei

    Secondary structure

    1
    334
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 158

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F4VX-ray2.22D/E/F1-16[»]
    1U8TX-ray1.50E/F1-16[»]
    2B1JX-ray2.40C/D1-16[»]
    ProteinModelPortaliP06974.
    SMRiP06974. Positions 48-229.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06974.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the FliM family.Curated

    Phylogenomic databases

    eggNOGiCOG1868.
    HOGENOMiHOG000253580.
    KOiK02416.
    OMAiLFNMMRR.
    OrthoDBiEOG68M4DH.
    PhylomeDBiP06974.

    Family and domain databases

    InterProiIPR028976. CheC-like_dom.
    IPR001689. Flag_FliM.
    IPR001543. SpoA.
    [Graphical view]
    PfamiPF02154. FliM. 1 hit.
    PF01052. SpoA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002888. FliM. 1 hit.
    PRINTSiPR00955. FLGMOTORFLIM.
    SUPFAMiSSF101801. SSF101801. 1 hit.
    SSF103039. SSF103039. 1 hit.
    TIGRFAMsiTIGR01397. fliM_switch. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P06974-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDSILSQAE IDALLNGDSE VKDEPTASVS GESDIRPYDP NTQRRVVRER    50
    LQALEIINER FARHFRMGLF NLLRRSPDIT VGAIRIQPYH EFARNLPVPT 100
    NLNLIHLKPL RGTGLVVFSP SLVFIAVDNL FGGDGRFPTK VEGREFTHTE 150
    QRVINRMLKL ALEGYSDAWK AINPLEVEYV RSEMQVKFTN ITTSPNDIVV 200
    NTPFHVEIGN LTGEFNICLP FSMIEPLREL LVNPPLENSR NEDQNWRDNL 250
    VRQVQHSQLE LVANFADISL RLSQILKLNP GDVLPIEKPD RIIAHVDGVP 300
    VLTSQYGTLN GQYALRIEHL INPILNSLNE EQPK 334
    Length:334
    Mass (Da):37,849
    Last modified:April 1, 1988 - v1
    Checksum:i05DC012B9364BFD6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12784 Genomic DNA. Translation: AAA23786.1.
    U00096 Genomic DNA. Translation: AAC75012.1.
    AP009048 Genomic DNA. Translation: BAA15770.1.
    M26294 Unassigned DNA. No translation available.
    PIRiB29842. XMECF2.
    RefSeqiNP_416455.1. NC_000913.3.
    YP_490199.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75012; AAC75012; b1945.
    BAA15770; BAA15770; BAA15770.
    GeneIDi12932576.
    946442.
    KEGGiecj:Y75_p1915.
    eco:b1945.
    PATRICi32119219. VBIEscCol129921_2024.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12784 Genomic DNA. Translation: AAA23786.1 .
    U00096 Genomic DNA. Translation: AAC75012.1 .
    AP009048 Genomic DNA. Translation: BAA15770.1 .
    M26294 Unassigned DNA. No translation available.
    PIRi B29842. XMECF2.
    RefSeqi NP_416455.1. NC_000913.3.
    YP_490199.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F4V X-ray 2.22 D/E/F 1-16 [» ]
    1U8T X-ray 1.50 E/F 1-16 [» ]
    2B1J X-ray 2.40 C/D 1-16 [» ]
    ProteinModelPortali P06974.
    SMRi P06974. Positions 48-229.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-1100N.
    IntActi P06974. 18 interactions.
    MINTi MINT-1301311.
    STRINGi 511145.b1945.

    Proteomic databases

    PaxDbi P06974.
    PRIDEi P06974.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75012 ; AAC75012 ; b1945 .
    BAA15770 ; BAA15770 ; BAA15770 .
    GeneIDi 12932576.
    946442.
    KEGGi ecj:Y75_p1915.
    eco:b1945.
    PATRICi 32119219. VBIEscCol129921_2024.

    Organism-specific databases

    EchoBASEi EB0319.
    EcoGenei EG10323. fliM.

    Phylogenomic databases

    eggNOGi COG1868.
    HOGENOMi HOG000253580.
    KOi K02416.
    OMAi LFNMMRR.
    OrthoDBi EOG68M4DH.
    PhylomeDBi P06974.

    Enzyme and pathway databases

    BioCyci EcoCyc:FLIM-FLAGELLAR-C-RING-SWITCH.
    ECOL316407:JW1929-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P06974.
    PROi P06974.

    Gene expression databases

    Genevestigatori P06974.

    Family and domain databases

    InterProi IPR028976. CheC-like_dom.
    IPR001689. Flag_FliM.
    IPR001543. SpoA.
    [Graphical view ]
    Pfami PF02154. FliM. 1 hit.
    PF01052. SpoA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002888. FliM. 1 hit.
    PRINTSi PR00955. FLGMOTORFLIM.
    SUPFAMi SSF101801. SSF101801. 1 hit.
    SSF103039. SSF103039. 1 hit.
    TIGRFAMsi TIGR01397. fliM_switch. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the flaA (cheC) locus of Escherichia coli and discovery of a new gene."
      Kuo S.C., Koshland D.E. Jr.
      J. Bacteriol. 166:1007-1012(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "DNA sequence analysis, gene product identification, and localization of flagellar motor components of Escherichia coli."
      Malakooti J., Komeda Y., Matsumura P.
      J. Bacteriol. 171:2728-2734(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 327-334.
      Strain: K12.
    6. "The c-di-GMP binding protein YcgR controls flagellar motor direction and speed to affect chemotaxis by a 'backstop brake' mechanism."
      Paul K., Nieto V., Carlquist W.C., Blair D.F., Harshey R.M.
      Mol. Cell 38:128-139(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YCRG, MUTAGENESIS OF VAL-153; ASN-155; ARG-156; LEU-160; ASP-167 AND GLU-176.
      Strain: K12 / RP3098.
    7. "Flagellar motility in bacteria structure and function of flagellar motor."
      Terashima H., Kojima S., Homma M.
      Int. Rev. Cytol. 270:39-85(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiFLIM_ECOLI
    AccessioniPrimary (citable) accession number: P06974
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 132 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. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    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