ID   FLGI2_VIBPA             Reviewed;         363 AA.
AC   Q9X9J4;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2003, sequence version 2.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Flagellar P-ring protein 2;
DE   AltName: Full=Basal body P-ring protein 2;
DE   Flags: Precursor;
GN   Name=flgI2; OrderedLocusNames=VP0783;
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 [GENOMIC DNA].
RC   STRAIN=BB22;
RA   McCarter L.L.;
RT   "Polar flagellar region I.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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:0000250}.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. Bacterial flagellum
CC       basal body {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FlgI family. {ECO:0000305}.
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DR   EMBL; U12817; AAD42919.1; -; Genomic_DNA.
DR   EMBL; BA000031; BAC59046.1; -; Genomic_DNA.
DR   RefSeq; NP_797162.1; NC_004603.1.
DR   RefSeq; WP_005454020.1; NC_004603.1.
DR   AlphaFoldDB; Q9X9J4; -.
DR   SMR; Q9X9J4; -.
DR   STRING; 223926.28805769; -.
DR   EnsemblBacteria; BAC59046; BAC59046; BAC59046.
DR   GeneID; 1188280; -.
DR   KEGG; vpa:VP0783; -.
DR   PATRIC; fig|223926.6.peg.748; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; KTIQITR; -.
DR   Proteomes; UP000002493; Chromosome 1.
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..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..363
FT                   /note="Flagellar P-ring protein 2"
FT                   /id="PRO_0000009527"
FT   CONFLICT        329
FT                   /note="L -> F (in Ref. 1; AAD42919)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   363 AA;  37901 MW;  91213A17D2569966 CRC64;
     MKRIVLLLMS VALFSTAAQA ARIKDVAQVA GVRSNQLVGY GLVSGLPGTG EANPFTEQSF
     AAMLQNFGIQ LPPGTKPKIK NVAAVMVTAE LPPFSKPGQQ VDVTVSSIGS AKSLRGGTLL
     QTFLKGLDGQ VYAVAQGNLV VSGFSAEGAD GSKIVGNNPT VGLISSGATV EREIPNPFGR
     GDYITFNLLE SDFTTAQRMA DAVNNFLGPQ MASAVDATSV RVRAPRDVSQ RVAFLSAIEN
     LEFDPADGAA KIIVNSRTGT IVVGKHVRLK PAAVTHGGMT VAIKENLNVS QPNSFSGGQT
     VVVPDSDIEV TEEKGKMFKF EPGLTLDDLV RAVNEVGAAP SDLMAILQAL KQAGAIEGQL
     III