FLGI_VIBC3
ID FLGI_VIBC3 Reviewed; 361 AA.
AC A5F677; C3M3F0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=VC0395_A1785, VC395_2309;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ20487.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10299.1; -; Genomic_DNA.
DR RefSeq; WP_001225051.1; NZ_JAACZH010000022.1.
DR AlphaFoldDB; A5F677; -.
DR SMR; A5F677; -.
DR STRING; 345073.VC395_2309; -.
DR EnsemblBacteria; ABQ20487; ABQ20487; VC0395_A1785.
DR KEGG; vco:VC0395_A1785; -.
DR KEGG; vcr:VC395_2309; -.
DR PATRIC; fig|345073.21.peg.2225; -.
DR eggNOG; COG1706; Bacteria.
DR HOGENOM; CLU_045235_1_0_6; -.
DR OMA; KTIQITR; -.
DR Proteomes; UP000000249; Chromosome 2.
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..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00416"
FT CHAIN 19..361
FT /note="Flagellar P-ring protein"
FT /id="PRO_1000072289"
SQ SEQUENCE 361 AA; 37663 MW; E370E7591562C117 CRC64;
MRKFTILLML LLASSAQAAR IKDVAQVAGV RNNQLVGYGL VTGLPGTGES TPFTDQSFNA
MLQSFGIQLP PGTKPKTKNV AAVIVTADLP AFSKQGQTID ITVSSIGSAK SLRGGTLMQT
FLKGLDGQVY AVAQGNLVVS GFSATGADGS KIVGNNPTVG MISSGAIVER EVPNPFGRGD
YITFNLFESD FTTAQRLADA VNQFLGPQMA SAVDAASIKV RAPRDLSQRV AFLSAIENLE
FNPADSAAKI IVNSRTGTIV VGQNVRLKPA AVTHGGMTVA IKENLNVSQP NALGGGQTVV
VPNTEIEVTE KQGKMFKLEP GVTLDDLVRA VNEVGAAPSD LMAILQALKQ AGAIEGQLII
I