ID   FLGI_RHOPT              Reviewed;         373 AA.
AC   B3QIX2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-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=Rpal_4432;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP001096; ACF02928.1; -; Genomic_DNA.
DR   RefSeq; WP_011159445.1; NC_011004.1.
DR   AlphaFoldDB; B3QIX2; -.
DR   SMR; B3QIX2; -.
DR   EnsemblBacteria; ACF02928; ACF02928; Rpal_4432.
DR   GeneID; 66895025; -.
DR   KEGG; rpt:Rpal_4432; -.
DR   HOGENOM; CLU_045235_1_0_5; -.
DR   OMA; VGPRDMI; -.
DR   OrthoDB; 693640at2; -.
DR   BioCyc; RPAL395960:RPAL_RS21925-MON; -.
DR   Proteomes; UP000001725; 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..28
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           29..373
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_5000378051"
SQ   SEQUENCE   373 AA;  38615 MW;  D2202E7332442B0A CRC64;
     MPRVSTHLVK LAAAALCALL LSAVAASATS RIKDLANIEG IRQNQLIGYG LVVGLNGTGD
     TLNNIPFTKQ SLQAMLERMG VNIRGATIRT GNVAAVMVTG NLPPFATQGT RMDVTVSALG
     DAKNLQGGTL LVTPLLGADG NVYAVAQGSL AIGGFQAEGE AAKITRGVPT VGRIANGAII
     EREIEFALNR LPNVRLALRN ADFTTAKRIA AAVNDYLGTK CAEPLDPSTV QLSIPGEFKG
     NAVALLTEIE QLQVEPDQAA KIVIDERSGI IVMGRDVRVA TVAVAQGNLT VSISESPQVS
     QPNPLGGGRT VVTPNSRIGV TEDGKKLAVV KDGVSLQQLV DGLNSLGIGP RDLIGILQAI
     KAAGAIEADI EVM