ID   FLGI_RHOPS              Reviewed;         373 AA.
AC   Q13AH6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=RPD_1677;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) 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; CP000283; ABE38913.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q13AH6; -.
DR   SMR; Q13AH6; -.
DR   STRING; 316057.RPD_1677; -.
DR   EnsemblBacteria; ABE38913; ABE38913; RPD_1677.
DR   KEGG; rpd:RPD_1677; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_5; -.
DR   OMA; VGPRDMI; -.
DR   OrthoDB; 693640at2; -.
DR   BioCyc; RPAL316057:RPD_RS08455-MON; -.
DR   Proteomes; UP000001818; 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..27
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           28..373
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_1000050117"
SQ   SEQUENCE   373 AA;  38642 MW;  E3349FB32311E195 CRC64;
     MPSFSPTLLK LAAAALSALL LSGVAASATS RIKDLANIEG VRQNQLIGYG LVVGLNGTGD
     TLNNIPFTKQ SLQAMLERMG VNIRGATIRT GNVAAVMVTG NLPAFATQGT RMDVTVSALG
     DAKNLQGGTL LVTPLLGADG NVYAVAQGSL AIGGFQAEGE AAKITRGVPT VGRIANGAII
     EREIEFALNR LPNVRLALRN ADFTTAKRIA AAVNDFLGTK SAEPIDPSTV QLSIPAEFKG
     NAVAFLTEIE QLQVEPDQAA KIIIDERSGI IVMGRDVRVA TVAVAQGNLT VSISESPQVS
     QPNPLSRGRT TVTPNSRIGV TEDGKKLALV KDGVSLQQLV DGLNGLGIGP RDLIGILQAI
     KAAGAIEADI EVM