FLGI_SALDC
ID FLGI_SALDC Reviewed; 365 AA.
AC B5FKC5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 58.
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=SeD_A2191;
OS Salmonella dublin (strain CT_02021853).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=439851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT_02021853;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001144; ACH75685.1; -; Genomic_DNA.
DR RefSeq; WP_001518955.1; NC_011205.1.
DR AlphaFoldDB; B5FKC5; -.
DR SMR; B5FKC5; -.
DR KEGG; sed:SeD_A2191; -.
DR HOGENOM; CLU_045235_1_0_6; -.
DR OMA; KTIQITR; -.
DR Proteomes; UP000008322; 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..365
FT /note="Flagellar P-ring protein"
FT /id="PRO_1000123979"
SQ SEQUENCE 365 AA; 38168 MW; 7DAAD3BAD7FD05BD CRC64;
MFKALAGIVL ALVATLAHAE RIRDLTSVQG VRENSLIGYG LVVGLDGTGD QTTQTPFTTQ
TLNNMLSQLG ITVPTGTNMQ LKNVAAVMVT ASYPPFARQG QTIDVVVSSM GNAKSLRGGT
LLMTPLKGVD SQVYALAQGN ILVGGAGASA GGSSVQVNQL NGGRITNGAI IERELPTQFG
AGNTINLQLN DEDFTMAQQI TDAINRARGY GSATALDART VQVRVPSGNS SQVRFLADIQ
NMEVNVTPQD AKVVINSRTG SVVMNREVTL DSCAVAQGNL SVTVNRQLNV NQPNTPFGGG
QTVVTPQTQI DLRQSGGSLQ SVRSSANLNS VVRALNALGA TPMDLMSILQ SMQSAGCLRA
KLEII