ID   FLGI_MARN8              Reviewed;         365 AA.
AC   A1TZN2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=Maqu_1109;
OS   Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS   aquaeolei).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Marinobacteraceae; Marinobacter.
OX   NCBI_TaxID=351348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX   PubMed=21335390; DOI=10.1128/aem.01866-10;
RA   Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA   Edwards K.J.;
RT   "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT   'opportunitroph'.";
RL   Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM18201.1; -; Genomic_DNA.
DR   RefSeq; WP_011784618.1; NC_008740.1.
DR   AlphaFoldDB; A1TZN2; -.
DR   SMR; A1TZN2; -.
DR   STRING; 351348.Maqu_1109; -.
DR   EnsemblBacteria; ABM18201; ABM18201; Maqu_1109.
DR   KEGG; maq:Maqu_1109; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; FTEQSFR; -.
DR   OrthoDB; 693640at2; -.
DR   Proteomes; UP000000998; 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; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           23..365
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_5000208906"
SQ   SEQUENCE   365 AA;  38443 MW;  BC4C18A1E7ED565C CRC64;
     MSVRRFLVWI LALTVGAAPV MADRLKDLSR IKGVRNNQLV GYGLVVGLDG TGDKAPFTNQ
     TFRNMMNQFG ITLPDGVNPK LANVAAVTVS ATLPAFAKAG QELDITVSSI GNADSLRGGT
     LLMTPLKGAD GQVYAMAQGS LVVGGFGAQG QDGSRITVNV PSVGRIPNGA TIEREVESPF
     NRGDTITFNL LRSDFTTARR VVEAINGRLG PDMAYAHDAT SISVRAPRDP SQRVSFLSIL
     ENIEVDPAQE AARVVINSRT GTIVVGQNVK VSPAAITHGN LTVTIQENPE VVQPNPLAQG
     DTAVQQNTQI AVTEDPARMF QFGPATTLNE IVQAVNQVGA APGDVMAVLE ALKQAGALRA
     ELIVI