ID   FLGI_THESQ              Reviewed;         331 AA.
AC   B1LB48;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 62.
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=TRQ2_1202;
OS   Thermotoga sp. (strain RQ2).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga;
OC   unclassified Thermotoga.
OX   NCBI_TaxID=126740;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RQ2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA   Richardson P.;
RT   "Complete sequence of Thermotoga sp. RQ2.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000969; ACB09546.1; -; Genomic_DNA.
DR   RefSeq; WP_011943753.1; NC_010483.1.
DR   AlphaFoldDB; B1LB48; -.
DR   SMR; B1LB48; -.
DR   EnsemblBacteria; ACB09546; ACB09546; TRQ2_1202.
DR   KEGG; trq:TRQ2_1202; -.
DR   HOGENOM; CLU_045235_1_0_0; -.
DR   OMA; KTIQITR; -.
DR   OrthoDB; 693640at2; -.
DR   Proteomes; UP000001687; 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; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           26..331
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_1000123984"
SQ   SEQUENCE   331 AA;  35432 MW;  7B988307118BB43D CRC64;
     MKKRLAVLLV IVLTITFSFS VTTRIKDIAF FRGARDNQLF GIGLVVGLNG TGDSGNVNSP
     LLLEMMKKFG VQVSENDLKS KNTALVMVLA DIPPFAKEGM RIDCVVASIA DAKSLAGGYL
     LQTPLYGADG KVYAVAQGSV IIGGEDVKLS SNLQKRYRVV GYLPEGAIVE RDIPSDMLDG
     DSVTILLRQP DITTAARVAR AINEKFEMDL AKAIDPSAIK LTVPNAFQDD LITFLSLVEE
     IEVQPDVPAR IVVNERTGTV LFGGDVKLSD FVISYGNFTI SVTGGKIGDK DATISNLVSA
     LKAAGATPQD IIAILQVIYE SGYITGELII M