ID   FLGI_CUPPJ              Reviewed;         377 AA.
AC   Q46PF7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   25-MAY-2022, entry version 88.
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=Reut_B5632;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ64977.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000091; AAZ64977.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q46PF7; -.
DR   SMR; Q46PF7; -.
DR   STRING; 264198.Reut_B5632; -.
DR   EnsemblBacteria; AAZ64977; AAZ64977; Reut_B5632.
DR   KEGG; reu:Reut_B5632; -.
DR   eggNOG; COG1706; Bacteria.
DR   HOGENOM; CLU_045235_1_0_4; -.
DR   OMA; KTIQITR; -.
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..30
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           31..377
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000236314"
SQ   SEQUENCE   377 AA;  38503 MW;  D43F5F50D6296BAC CRC64;
     MLARFLSSLL KASVTALAVV VAFGFAANFA RAERLKNLAT FQGVRDNPLV GYGLVVGLDN
     TGDQTMQTPF TTQSLTNMLS QLGITLPAGK NMQLKNVAAV MVTATLPAFA QPGSQLDIVV
     SSMGNAKSLR GGTLLMTPLK GADGQVYAIA QGNMLVGGAG ASANGSKVQV NQLAVGRIAN
     GAIVERAVAA FQPDGGVLNL ELKDTDFGTA ERVVEAINRS MGGGVAAALD GRVVQVRAPQ
     SPSARVGFLA RIENLDVTPA KAAAKVILNA RTGSIVMNQA VTVEDCAVAH GNLSVVINTQ
     PVISQPAPFS GGQTVVAPVS QIDMKQQGGS LQIVKAGASL AAVVKGLNAL GATPADLQTI
     LEAMRAAGAL RAELEII