ID   FLGI_THEMA              Reviewed;         331 AA.
AC   Q9X1M5;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Flagellar P-ring protein;
DE   AltName: Full=Basal body P-ring protein;
DE   Flags: Precursor;
GN   Name=flgI; OrderedLocusNames=TM_1539;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAD36606.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000512; AAD36606.1; ALT_INIT; Genomic_DNA.
DR   PIR; G72242; G72242.
DR   RefSeq; NP_229339.1; NC_000853.1.
DR   RefSeq; WP_004081923.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9X1M5; -.
DR   SMR; Q9X1M5; -.
DR   STRING; 243274.THEMA_06590; -.
DR   EnsemblBacteria; AAD36606; AAD36606; TM_1539.
DR   KEGG; tma:TM1539; -.
DR   PATRIC; fig|243274.5.peg.1557; -.
DR   eggNOG; COG1706; Bacteria.
DR   InParanoid; Q9X1M5; -.
DR   OMA; KTIQITR; -.
DR   Proteomes; UP000008183; Chromosome.
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; 2.
DR   Pfam; PF02119; FlgI; 2.
DR   PRINTS; PR01010; FLGPRINGFLGI.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..331
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000009525"
SQ   SEQUENCE   331 AA;  35421 MW;  97E6CABB1F1B47F9 CRC64;
     MKKRLAVLLV IVLTITFSFS VTTRIKDIAF FRGARDNQLF GIGLVVGLNG TGDSGNVNSP
     LLLEMMKKFG VQVSENDLKS KNTALVMVLA DIPPFAKEGM RIDCVVASIA DAKSLAGGYL
     LQTPLYGADG KVYAVAQGSV IIGGEDVKLS SNLQKRYRVV GYLLEGAIVE RDIPSDMLDG
     DSVTILLRQP DITTAARVAR AINEKFEMDL AKAIDPSAIK LTVPSAFQDD LITFLSLVEE
     IEVQPDVPAR IVVNERTGTV LFGGDVKLSD FVISYGNFTI SVTGGKIGDK DATISNLVSA
     LKAAGATPQD IIAILQVIYE SGYITGELII M