ID   FLGI_ALIF1              Reviewed;         373 AA.
AC   Q5E3N1;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Flagellar P-ring protein {ECO:0000255|HAMAP-Rule:MF_00416};
DE   AltName: Full=Basal body P-ring protein {ECO:0000255|HAMAP-Rule:MF_00416};
DE   Flags: Precursor;
GN   Name=flgI {ECO:0000255|HAMAP-Rule:MF_00416}; OrderedLocusNames=VF_1870;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
CC   -!- FUNCTION: Assembles around the rod to form the L-ring and probably
CC       protects the motor/basal body from shearing forces during rotation.
CC       {ECO:0000255|HAMAP-Rule:MF_00416}.
CC   -!- SUBUNIT: The basal body constitutes a major portion of the flagellar
CC       organelle and consists of four rings (L,P,S, and M) mounted on a
CC       central rod. {ECO:0000255|HAMAP-Rule:MF_00416}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00416}.
CC       Bacterial flagellum basal body {ECO:0000255|HAMAP-Rule:MF_00416}.
CC   -!- SIMILARITY: Belongs to the FlgI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00416}.
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DR   EMBL; CP000020; AAW86365.1; -; Genomic_DNA.
DR   RefSeq; WP_011262372.1; NC_006840.2.
DR   RefSeq; YP_205253.1; NC_006840.2.
DR   AlphaFoldDB; Q5E3N1; -.
DR   SMR; Q5E3N1; -.
DR   STRING; 312309.VF_1870; -.
DR   EnsemblBacteria; AAW86365; AAW86365; VF_1870.
DR   GeneID; 64242029; -.
DR   KEGG; vfi:VF_1870; -.
DR   PATRIC; fig|312309.11.peg.1897; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; KTIQITR; -.
DR   OrthoDB; 693640at2; -.
DR   Proteomes; UP000000537; Chromosome I.
DR   GO; GO:0009428; C:bacterial-type flagellum basal body, distal rod, P ring; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   HAMAP; MF_00416; FlgI; 1.
DR   InterPro; IPR001782; Flag_FlgI.
DR   PANTHER; PTHR30381; PTHR30381; 1.
DR   Pfam; PF02119; FlgI; 1.
DR   PRINTS; PR01010; FLGPRINGFLGI.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           31..373
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000041805"
SQ   SEQUENCE   373 AA;  39163 MW;  62059D7C7CCD4D9B CRC64;
     MTNRWSFDVN KNLVTVLFTW LCLSISTAHA ARIKDVAEVA GVRSNQLIGY GLVSGLPGTG
     ESTPFTDQSF NAMLQNFGIQ LPPGTKPKTK NVAAVMVTAT LPPFSKQGQV VDVTVSSVGS
     AKSLRGGTLL QTFLKGLDGK TYAIAQGNLI VSGFSATGAD GSKIVGNNPT VGRISGGAMV
     EREVPSPFGR GDFITFNLLE SDFTTAQRMA DAVNNFLGPN MASAVDATSV RVRAPRDISQ
     RVAFLSAVEN VDFDPADGSA KIIVNSRTGT IVVGKHVKLK PAAVTHGGMT VAIKENLQVS
     QPGPFSDGQT VVTPDSDIEV TEEQGKMFKF EPGLTLDDLV RAVNEVGAAP SDLMAILQAL
     KQAGAIEGQL III