ID   FLGI_LEPIN              Reviewed;         366 AA.
AC   Q8F2V3;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 83.
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=LA_2664;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(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}.
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DR   EMBL; AE010300; AAN49863.1; -; Genomic_DNA.
DR   RefSeq; NP_712845.1; NC_004342.2.
DR   RefSeq; WP_000838056.1; NC_004342.2.
DR   AlphaFoldDB; Q8F2V3; -.
DR   SMR; Q8F2V3; -.
DR   STRING; 189518.LA_2664; -.
DR   EnsemblBacteria; AAN49863; AAN49863; LA_2664.
DR   GeneID; 61144636; -.
DR   KEGG; lil:LA_2664; -.
DR   PATRIC; fig|189518.3.peg.2645; -.
DR   HOGENOM; CLU_045235_1_0_12; -.
DR   InParanoid; Q8F2V3; -.
DR   OMA; KTIQITR; -.
DR   Proteomes; UP000001408; 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..27
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           28..366
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000009510"
SQ   SEQUENCE   366 AA;  39512 MW;  453EF396A79C2221 CRC64;
     MKSKYSIFCM FLLRGFIFLG TVFSLNSAEL RLKDIARIEG VRENQITGYG IVVGLPGTGD
     SKTPFTSESM KNYLKNLGVE ANLKPDQTRN IASVLITATI PTYSRKGDKL NVVVSSIGDA
     KSLEGGVLLQ SPLKTAGDKT YAVASGVISF GGRQEQERGS SSRGNKKTVG VVHGGAIVEQ
     ELDQNFYASE RVQIQLENQD FTTLNAIVSK IRSILPGKHG IGPESVVPIS PSEINIVLGK
     SFENKSDAFL TLLSDIENLT VETQTKPKVV INERTGVIVM GGNITIEEVA VSRSGLNLSV
     TDKNRRRNWL GKEQEPTKSS FLIEESTSVG DVVEALNKVG ASTKDIIAIL EALKKSGALH
     AELEIQ