ID   FLIN_BUCAI              Reviewed;         133 AA.
AC   P57183;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   04-NOV-2026, entry version 114.
DE   RecName: Full=Flagellar motor switch protein FliN;
GN   Name=fliN; OrderedLocusNames=BU081;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- FUNCTION: FliN is one of three proteins (FliG, FliN, FliM) that form
CC       the rotor-mounted switch complex (C ring), located at the base of the
CC       basal body. This complex interacts with the CheY and CheZ chemotaxis
CC       proteins, in addition to contacting components of the motor that
CC       determine the direction of flagellar rotation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Bacterial
CC       flagellum basal body {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FliN/MopA/SpaO family. {ECO:0000305}.
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DR   EMBL; BA000003; BAB12801.1; -; Genomic_DNA.
DR   RefSeq; WP_010895934.1; NC_002528.1.
DR   AlphaFoldDB; P57183; -.
DR   SMR; P57183; -.
DR   STRING; 563178.BUAP5A_080; -.
DR   EnsemblBacteria; BAB12801; BAB12801; BAB12801.
DR   KEGG; buc:BU081; -.
DR   PATRIC; fig|107806.10.peg.87; -.
DR   eggNOG; COG1886; Bacteria.
DR   HOGENOM; CLU_097058_2_0_6; -.
DR   OMA; AEDMWAD; -.
DR   Proteomes; UP000001806; Chromosome.
DR   GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   Gene3D; 2.30.330.10; SpoA-like; 1.
DR   InterPro; IPR012826; FliN.
DR   InterPro; IPR001543; FliN-like_C.
DR   InterPro; IPR051469; FliN/MopA/SpaO.
DR   InterPro; IPR001172; FliN_T3SS_HrcQb.
DR   InterPro; IPR036429; SpoA-like_sf.
DR   NCBIfam; TIGR02480; fliN; 1.
DR   PANTHER; PTHR43484; -; 1.
DR   PANTHER; PTHR43484:SF1; FLAGELLAR MOTOR SWITCH PROTEIN FLIN; 1.
DR   Pfam; PF01052; FliMN_C; 1.
DR   PRINTS; PR00956; FLGMOTORFLIN.
DR   SUPFAM; SSF101801; Surface presentation of antigens (SPOA); 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell membrane; Chemotaxis; Flagellar rotation;
KW   Membrane; Reference proteome.
FT   CHAIN           1..133
FT                   /note="Flagellar motor switch protein FliN"
FT                   /id="PRO_0000184114"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   133 AA;  14898 MW;  C16754AF0A166FB5 CRC64;
     MSKIQKNSDN DKLIDSEKKI PTDQDVDKNL LPQENSKNST LDNTIDIVDS KKTILNVPVN
     ITVELGTSRI KIKDFLKFSK GSMLILNESI KEPLNIFMNG HLIASGEIVV LEEKYGIRIT
     NIKNSLKTIN ISS
//