FLGI_ECOHS
ID FLGI_ECOHS Reviewed; 365 AA.
AC A7ZZ38;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 59.
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=EcHS_A1203;
OS Escherichia coli O9:H4 (strain HS).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(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; CP000802; ABV05542.1; -; Genomic_DNA.
DR RefSeq; WP_000589315.1; NC_009800.1.
DR AlphaFoldDB; A7ZZ38; -.
DR SMR; A7ZZ38; -.
DR KEGG; ecx:EcHS_A1203; -.
DR HOGENOM; CLU_045235_1_0_6; -.
DR OMA; KTIQITR; -.
DR Proteomes; UP000001123; 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_1000060076"
SQ SEQUENCE 365 AA; 38178 MW; C91435EA78629E51 CRC64;
MIKFLSALIL LLVTTAAQAE RIRDLTSVQG VRQNSLIGYG LVVGLDGTGD QTTQTPFTTQ
TLNNMLSQLG ITVPTGTNMQ LKNVAAVMVT ASLPPFGRQG QTIDVVVSSM GNAKSLRGGT
LLMTPLKGVD SQVYALAQGN ILVGGAGASA GGSSVQVNQL NGGRITNGAV IERELPSQFG
VGNTLNLQLN DEDFSMAQQI ADTINRVRGY GSATALDART IQVRVPSGNS SQVRFLADIQ
NMHVNVTPQD AKVVINSRTG SVVMNREVTL DSCAVAQGNL SVTVNRQANV SQPDTPFGGG
QTVVTPQTQI DLRQSGGSLQ SVRSSASLNN VVRALNALGA TPMDLMSILQ SMQSAGCLRA
KLEII