ID   FLGI_MARMS              Reviewed;         362 AA.
AC   A6W199;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 63.
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=Mmwyl1_3576;
OS   Marinomonas sp. (strain MWYL1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=400668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWYL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Johnston A.W.B., Todd J.D., Rogers R., Wexler M., Bond P.L., Li Y.,
RA   Richardson P.;
RT   "Complete sequence of Marinomonas sp. MWYL1.";
RL   Submitted (JUN-2007) 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}.
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DR   EMBL; CP000749; ABR72478.1; -; Genomic_DNA.
DR   RefSeq; WP_012071243.1; NC_009654.1.
DR   AlphaFoldDB; A6W199; -.
DR   SMR; A6W199; -.
DR   STRING; 400668.Mmwyl1_3576; -.
DR   PRIDE; A6W199; -.
DR   EnsemblBacteria; ABR72478; ABR72478; Mmwyl1_3576.
DR   KEGG; mmw:Mmwyl1_3576; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; FTEQSFR; -.
DR   OrthoDB; 693640at2; -.
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; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           19..362
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_5000259656"
SQ   SEQUENCE   362 AA;  37371 MW;  D66DC15E59C64258 CRC64;
     MKHIALIVLY FLSFSVQAER LKDIASVQGV RENQLFGYGL VIGLNGTGDS TAFTNQSFVS
     MLSRFGVTLP EGVNATSKNV AAVSLTATLP AFSKPGQKID VTVSSIGNAS ALRGGTLLLS
     TLKGADGAVY AIAQGNLVVG GLGANGADGS RTTGNVPTVG RIPNGASVER IVPSSFNTGD
     TLTFNLNRPD FTTAKQVTDK INNLLGPGVA TTLDATSIRV SAPRDSSQRV TYLSILENLD
     VEVAEERARI VVNSRTGTII IGQHVKVSPA AITHGSLTVT IKEVPPVVGK DGTITGGQTI
     VSPREGIEIA PNSGHMFVFD PGASLDDIVR AVNQVGAAPG DVMAILEGLK QAGAINADLV
     VI