ID   FLGI1_VIBPA             Reviewed;         373 AA.
AC   Q87JI2;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Flagellar P-ring protein 1 {ECO:0000255|HAMAP-Rule:MF_00416};
DE   AltName: Full=Basal body P-ring protein 1 {ECO:0000255|HAMAP-Rule:MF_00416};
DE   Flags: Precursor;
GN   Name=flgI1 {ECO:0000255|HAMAP-Rule:MF_00416}; OrderedLocusNames=VPA0271;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC61614.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BA000032; BAC61614.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_799781.1; NC_004605.1.
DR   RefSeq; WP_005463987.1; NC_004605.1.
DR   AlphaFoldDB; Q87JI2; -.
DR   SMR; Q87JI2; -.
DR   STRING; 223926.28808409; -.
DR   EnsemblBacteria; BAC61614; BAC61614; BAC61614.
DR   GeneID; 1190959; -.
DR   KEGG; vpa:VPA0271; -.
DR   PATRIC; fig|223926.6.peg.3223; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; QFRPKNV; -.
DR   Proteomes; UP000002493; Chromosome 2.
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..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           26..373
FT                   /note="Flagellar P-ring protein 1"
FT                   /id="PRO_0000041806"
SQ   SEQUENCE   373 AA;  39694 MW;  2EEB5FC8D770F209 CRC64;
     MKPINTFFSS FLLALTLGLP ATSQAEVEIP IMDLVDVRGI RENQLVGYGL VVGLAGQGDR
     NQVKFTSQSI TNMLRQFGVQ IDDSMDPKLR NVASVSVTAS VDPMAGPGQT LDVVVSSIGD
     AKSLRGGTLL LTPLRGIDGE VYAIAQGSVV VGGLSAEGKS GSKVEVNTPT AGRVPNGATL
     EREIKTDFNQ RDEITLNLRK PSFTTAKNIA REINNTFGPN VAVAINKARV DMRAPKDTQQ
     RVIMMSMLEE MSVVEGRKPA RIVFNSRTGT VVIGKNVKVG EAAVSHGNLT VRISESEKVS
     QPNAFADGET KVVNQTDIDV NEELAQMVIW PPGTELNTIV DAVNSLGATP TDLMSILQAL
     NEAGALNAEL VVI