FLGI_ECOL5
ID FLGI_ECOL5 Reviewed; 365 AA.
AC Q0TIZ4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=ECP_1072;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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; CP000247; ABG69085.1; -; Genomic_DNA.
DR RefSeq; WP_000589300.1; NC_008253.1.
DR AlphaFoldDB; Q0TIZ4; -.
DR SMR; Q0TIZ4; -.
DR STRING; 362663.ECP_1072; -.
DR EnsemblBacteria; ABG69085; ABG69085; ECP_1072.
DR KEGG; ecp:ECP_1072; -.
DR HOGENOM; CLU_045235_1_0_6; -.
DR OMA; KTIQITR; -.
DR Proteomes; UP000009182; 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_1000050109"
SQ SEQUENCE 365 AA; 38182 MW; CDAA9334837C4340 CRC64;
MIKFLSALIL LLVITAAQAE RIRDLTSVQG VRQNSLIGYG LVVGLDGTGD QTTQTPFTTQ
TLNNMLSQLG ITVPTGTNMQ LKNVAAVMVT ASLPPFGRQG QTIDVVVSSM GNAKSLRGGT
LLMTPLKGVD SQVYALAQGN ILVGGAGASA GGSSVQVNQL NGGRITNGAV IERELPSQFG
VGNTLNLQLN DEDFSMAQQI ADTINRVRGY GSATALDART IQVRVPSGNS SQVRFLADIQ
NMQVNVTPQD AKVVINSRTG SVVMNREVTL DSCAVAQGNL SVTVNRQANV SQPDTPFGGG
QTVVTPQTQI DLRQSGGSLQ SVRSSASLNN VVRALNALGA TPMDLMSILQ SMQSAGCLRA
KLEII