ID   FLGI_CAMJR              Reviewed;         348 AA.
AC   Q5HSW8;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=CJE1636;
OS   Campylobacter jejuni (strain RM1221).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195099;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RM1221;
RX   PubMed=15660156; DOI=10.1371/journal.pbio.0030015;
RA   Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A.,
RA   Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C.,
RA   Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U.,
RA   Ayodeji M.A., Shvartsbeyn A., Schatz M.C., Badger J.H., Fraser C.M.,
RA   Nelson K.E.;
RT   "Major structural differences and novel potential virulence mechanisms from
RT   the genomes of multiple Campylobacter species.";
RL   PLoS Biol. 3:72-85(2005).
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; CP000025; AAW36069.1; -; Genomic_DNA.
DR   RefSeq; WP_002826014.1; NC_003912.7.
DR   AlphaFoldDB; Q5HSW8; -.
DR   SMR; Q5HSW8; -.
DR   KEGG; cjr:CJE1636; -.
DR   HOGENOM; CLU_045235_1_0_7; -.
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..16
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT   CHAIN           17..348
FT                   /note="Flagellar P-ring protein"
FT                   /id="PRO_0000041791"
SQ   SEQUENCE   348 AA;  36981 MW;  C2F5234C25C752E0 CRC64;
     MRVLTIFLLF MTSIFAVQIK DVANTVGVRD NQLIGYGLVV GLNGSGDGTS SKFTLQSISN
     LLQGMNIKVD PNDIKSKNTA AVMVTAKLPA FAKSGDKLDI TVSSMGDAKS LQGGTLLLTA
     LRGIDGEIYA IAQGSISTGG LTPRPGGAGS HSTAATVMGG ANVEREIPQN FSQNNDLTLS
     LKVADFKTAN DIERVLNTVF GEEVAKAIDS RTVKLKKPED LSNVDFMARV LEQDIAYKPQ
     SKVIIDERTG TVIAGVDVEV EPVLITHKDI TIKIDPNNNA VANQNEIDMK DGGFVDPSSN
     TLRINNAKST VANIARMLNK LGATPNDIIA IMENLKRAGA INADLEII