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FLGI_ECOBW
ID   FLGI_ECOBW              Reviewed;         365 AA.
AC   C4ZS20;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 57.
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=BWG_0928;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/jb.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA   Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational events
RT   in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
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; CP001396; ACR64411.1; -; Genomic_DNA.
DR   RefSeq; WP_000589326.1; NC_012759.1.
DR   AlphaFoldDB; C4ZS20; -.
DR   SMR; C4ZS20; -.
DR   GeneID; 66670653; -.
DR   KEGG; ebw:BWG_0928; -.
DR   HOGENOM; CLU_045235_1_0_6; -.
DR   OMA; KTIQITR; -.
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_1000206021"
SQ   SEQUENCE   365 AA;  38169 MW;  DE243BDA61629E51 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
     NMQVNVTPQD AKVVINSRTG SVVMNREVTL DSCAVAQGNL SVTVNRQANV SQPDTPFGGG
     QTVVTPQTQI DLRQSGGSLQ SVRSSASLNN VVRALNALGA TPMDLMSILQ SMQSAGCLRA
     KLEII
 
 
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