ID   MOTY_VIBAN              Reviewed;         293 AA.
AC   Q9S3P9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Sodium-type flagellar protein MotY {ECO:0000250|UniProtKB:P46233};
DE   AltName: Full=Polar flagellum motor protein {ECO:0000303|PubMed:10735880};
DE   Flags: Precursor;
GN   Name=motY {ECO:0000303|PubMed:10735880};
OS   Vibrio anguillarum (Listonella anguillarum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=55601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=NB10 / Serotype O1;
RX   PubMed=10735880; DOI=10.1128/jb.182.8.2326-2328.2000;
RA   Ormonde P., Hoerstedt P., O'Toole R., Milton D.L.;
RT   "Role of motility in adherence to and invasion of a fish cell line by
RT   Vibrio anguillarum.";
RL   J. Bacteriol. 182:2326-2328(2000).
CC   -!- FUNCTION: May play the role of a stator in the sodium flagellar motor,
CC       stabilizing the force-generating unit through direct interaction with
CC       the cell wall (By similarity). Involved in adherence and invasion of
CC       fish cell line (PubMed:10735880). {ECO:0000250|UniProtKB:P46233,
CC       ECO:0000269|PubMed:10735880}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Mutant is nonmotile. It has an intact but
CC       paralyzed flagellum, and shows a decrease in virulence.
CC       {ECO:0000269|PubMed:10735880}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF176946; AAD51752.1; -; Genomic_DNA.
DR   RefSeq; WP_013857286.1; NZ_VSLF01000025.1.
DR   AlphaFoldDB; Q9S3P9; -.
DR   SMR; Q9S3P9; -.
DR   STRING; 55601.VANGNB10_cI0878; -.
DR   GeneID; 63947331; -.
DR   OMA; PMGETRN; -.
DR   OrthoDB; 583204at2; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0097588; P:archaeal or bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-KW.
DR   CDD; cd07185; OmpA_C-like; 1.
DR   Gene3D; 3.30.1330.60; -; 1.
DR   InterPro; IPR041544; MotY_N.
DR   InterPro; IPR006665; OmpA-like.
DR   InterPro; IPR006690; OMPA-like_CS.
DR   InterPro; IPR036737; OmpA-like_sf.
DR   Pfam; PF18393; MotY_N; 1.
DR   Pfam; PF00691; OmpA; 1.
DR   SUPFAM; SSF103088; SSF103088; 1.
DR   PROSITE; PS01068; OMPA_1; 1.
DR   PROSITE; PS51123; OMPA_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Flagellar rotation; Membrane; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..293
FT                   /note="Sodium-type flagellar protein MotY"
FT                   /id="PRO_0000020135"
FT   DOMAIN          175..292
FT                   /note="OmpA-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00473"
SQ   SEQUENCE   293 AA;  33725 MW;  5618435B49F40D3B CRC64;
     MNKWVTATIV MTSILTSFAP MAMDKRYVAT PQQSTWQMVT NTPLECRLVH PIPNYGDAEF
     SSRANKKINL DFELKMRRPM GETRNVSLVS LPPSWRPGES ADRITNLQFF KQFDGYIGGQ
     TAWSLLSELE KGRYPTFSYQ DWQSRDQRIE VALSSVLFQE KYNVFSDCVS NLLTYSFEDI
     SFTILHYDRD NVQLNKASQK RLAQIADYIR YNQDIDLVLV STYTDSVDSR GVSQDLSERR
     AEVLRDYFKS LGLPEDRIQV QGYGKRRPIA DNASPIGKDK NRRVVISLGR TII