ID   FLGI_HELP2              Reviewed;         342 AA.
AC   B6JKH7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 55.
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=HPP12_0246;
OS   Helicobacter pylori (strain P12).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=570508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P12;
RA   Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT   "The complete genome sequence of Helicobacter pylori strain P12.";
RL   Submitted (OCT-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; CP001217; ACJ07405.1; -; Genomic_DNA.
DR   RefSeq; WP_000832059.1; NC_011498.1.
DR   AlphaFoldDB; B6JKH7; -.
DR   SMR; B6JKH7; -.
DR   EnsemblBacteria; ACJ07405; ACJ07405; HPP12_0246.
DR   KEGG; hpp:HPP12_0246; -.
DR   HOGENOM; CLU_045235_1_0_7; -.
DR   OMA; KTIQITR; -.
DR   OrthoDB; 693640at2; -.
DR   Proteomes; UP000008198; 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..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           20..342
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_1000123974"
SQ   SEQUENCE   342 AA;  36671 MW;  87D67C47B8160165 CRC64;
     MKRVFLWLIF VLAFHKLLAE KIGDIASVVG VRDNQLIGYG LVIGLNGTGD KSGSKFTMQS
     ISNMLESVNV KISADDIKSK NVAAVMITAS LPPFARQGDK IDIHISSIGD AKSIQGGTLV
     MTPLNAVDGN IYALAQGAIT SGNSNNLLSA NIINGATIER EVSYDLFHKN AMVLSLKSPN
     FKNAIQVQNT LNKVFGNKVA IALDPKTIQI TRPERFSMVE FLALVQEIPI NYSAKNKIIV
     DEKSGTIISG VDIMVHPIVV TSQDITLKIT KEPLNNSKNT QDLDNNMSLD TAHNTLSSNG
     KNITIAGVVK ALQKIGVSAK GMVSILQALK KSGAISAEME IL