ID   FLGI_AQUAE              Reviewed;         360 AA.
AC   O67608;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Flagellar P-ring protein;
DE   AltName: Full=Basal body P-ring protein;
DE   Flags: Precursor;
GN   Name=flgI; OrderedLocusNames=aq_1713;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC07571.1; -; Genomic_DNA.
DR   PIR; F70447; F70447.
DR   RefSeq; NP_214174.1; NC_000918.1.
DR   RefSeq; WP_010881111.1; NC_000918.1.
DR   AlphaFoldDB; O67608; -.
DR   SMR; O67608; -.
DR   STRING; 224324.aq_1713; -.
DR   EnsemblBacteria; AAC07571; AAC07571; aq_1713.
DR   KEGG; aae:aq_1713; -.
DR   PATRIC; fig|224324.8.peg.1315; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_0; -.
DR   InParanoid; O67608; -.
DR   OMA; KTIQITR; -.
DR   OrthoDB; 693640at2; -.
DR   Proteomes; UP000000798; 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; 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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..360
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000009493"
SQ   SEQUENCE   360 AA;  38382 MW;  BDE0045BC2DE3F38 CRC64;
     MACKNIRYIV SLLILVSLTF GARIKDIATI EGNRYNYLIG YGLVVGLKGT GDGKATQFTV
     QSLANMLRRM GIPVDPRRIT VKNVAAVMVT AKVPPYAKAG MRFDVEVSSI GDAKSLEGGT
     LLMTPLRGPD GKVYAIAQGQ VIVGGYEARG RGAAQVKNVP TVGRIPNGAI LEKDLPFSAD
     FKEVNIYLDE PDFTTAKNVQ DVINRAFGKN IAKAVDSATI RVKIPEGYSP VDFLAKVENL
     EVSTSSVAKV VIDGRSGIVL LGGNVSIEPV AVAVGSLVVE IKERPEVVQP PPLSPGETKV
     VPRTEVKVKE EKKRLVQIKG TTVSELVDAL NSIGATPREI IQVLQAIKSA GALKAKLEVL