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FLGH_CERSP
ID   FLGH_CERSP              Reviewed;         222 AA.
AC   P58205;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Flagellar L-ring protein;
DE   AltName: Full=Basal body L-ring protein;
DE   Flags: Precursor;
GN   Name=flgH;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WS8;
RA   Gonzalez-Pedrajo B., De la Mora J., Ballado T., Camarena L., Dreyfus G.;
RT   "Isolation and complementation of a flagellar P-ring mutant of Rhodobacter
RT   sphaeroides.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
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:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}. Bacterial flagellum basal body {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FlgH family. {ECO:0000305}.
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DR   EMBL; AF205139; AAG29750.1; -; Genomic_DNA.
DR   AlphaFoldDB; P58205; -.
DR   SMR; P58205; -.
DR   GO; GO:0009427; C:bacterial-type flagellum basal body, distal rod, L ring; IEA:InterPro.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   HAMAP; MF_00415; FlgH; 1.
DR   InterPro; IPR000527; Flag_Lring.
DR   PANTHER; PTHR34933; PTHR34933; 1.
DR   Pfam; PF02107; FlgH; 1.
DR   PRINTS; PR01008; FLGLRINGFLGH.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..222
FT                   /note="Flagellar L-ring protein"
FT                   /id="PRO_0000009467"
FT   LIPID           19
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           19
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   222 AA;  23540 MW;  ABA1567F0D45D11F CRC64;
     MSRRMSLTAL ALLLAPAACS TYVEDRASEA WAPVYPVEEA ERLDSLPTGG IYSSTSRGLF
     VSDRRAARVG DIVTVDFDEK FSASKSQSAS GSRKSDYAID LPDALTLGLD DGVLDNSTDQ
     GFSGKGAASQ SNSLRGRMSV SVTRVLPGGN LEIMGQKLLT LNNGNEYVRL KGVVRPEDIG
     PDNVVTSDRI AHAEIKYIGA GDTADTANAG WLRRGLSVVS PL
 
 
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