ID   FLGI_RHOP2              Reviewed;         373 AA.
AC   Q2ITH2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=RPB_3794;
OS   Rhodopseudomonas palustris (strain HaA2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HaA2;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA   Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL   Submitted (JAN-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}.
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; CP000250; ABD08488.1; -; Genomic_DNA.
DR   RefSeq; WP_011442672.1; NC_007778.1.
DR   AlphaFoldDB; Q2ITH2; -.
DR   SMR; Q2ITH2; -.
DR   STRING; 316058.RPB_3794; -.
DR   EnsemblBacteria; ABD08488; ABD08488; RPB_3794.
DR   KEGG; rpb:RPB_3794; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_5; -.
DR   OMA; VGPRDMI; -.
DR   OrthoDB; 693640at2; -.
DR   Proteomes; UP000008809; 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_5000107642"
SQ   SEQUENCE   373 AA;  38550 MW;  F322241061796C9C CRC64;
     MPSVSAVILK LAAAALSALL LSGVAANATS RIKDLANIEG VRQNQLIGYG LVVGLNGTGD
     TLNNIPFTKQ SLQAMLERMG VNIRGATIRT GNVAAVMVTG NLPAFATQGT RMDVTVSALG
     DAKNLQGGTL LVTPLLGADG NVYAVAQGSL AIGGFQAEGE AAKITRGVPT VGRIANGAII
     EREIEFALNR LPMVRLALRN ADFTTAKRIA AAVNDFLGTK SAEPIDPSTV QLTIPAEFKG
     NAVAFVTEIE QLQVEPDQAA KIIIDERSGI IVMGRDVRVA TVAVAQGNLT VSISESPQVS
     QPNPLANGRT VVTPNSRIGV TEDGKKLALV KDGVSLQQLV DGLNGLGIGP RDLIGILQAI
     KAAGAIEADI EVM