FLGI_CAMJD
ID FLGI_CAMJD Reviewed; 348 AA.
AC A7H5I4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
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};
GN OrderedLocusNames=JJD26997_1810;
OS Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 /
OS 269.97).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1458 / RM4099 / 269.97;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., Lastovica A.J., Nelson K.E.;
RT "Complete genome sequence of Campylobacter jejuni subsp doylei 269.97
RT isolated from human blood.";
RL Submitted (JUL-2007) 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; CP000768; ABS44488.1; -; Genomic_DNA.
DR AlphaFoldDB; A7H5I4; -.
DR SMR; A7H5I4; -.
DR EnsemblBacteria; ABS44488; ABS44488; JJD26997_1810.
DR KEGG; cjd:JJD26997_1810; -.
DR HOGENOM; CLU_045235_1_0_7; -.
DR OMA; KTIQITR; -.
DR Proteomes; UP000002302; 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..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT CHAIN 17..348
FT /note="Flagellar P-ring protein"
FT /id="PRO_1000050106"
SQ SEQUENCE 348 AA; 36971 MW; C2F5234E6EAAE670 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 DGGFVDSSSN
TLRINNAKST VANIARMLNK LGATPNDIIA IMENLKRAGA INADLEII