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FLGH1_VIBPA
ID   FLGH1_VIBPA             Reviewed;         259 AA.
AC   Q9X9J5;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Flagellar L-ring protein 1;
DE   AltName: Full=Basal body L-ring protein 1;
DE   Flags: Precursor;
GN   Name=flgH1; Synonyms=flgH; OrderedLocusNames=VP0782;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BB22;
RA   McCarter L.L.;
RT   "Polar flagellar region I.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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; U12817; AAD42918.1; -; Genomic_DNA.
DR   EMBL; BA000031; BAC59045.1; -; Genomic_DNA.
DR   RefSeq; NP_797161.1; NC_004603.1.
DR   RefSeq; WP_005462288.1; NC_004603.1.
DR   AlphaFoldDB; Q9X9J5; -.
DR   SMR; Q9X9J5; -.
DR   STRING; 223926.28805768; -.
DR   EnsemblBacteria; BAC59045; BAC59045; BAC59045.
DR   GeneID; 1188279; -.
DR   KEGG; vpa:VP0782; -.
DR   PATRIC; fig|223926.6.peg.747; -.
DR   eggNOG; COG2063; Bacteria.
DR   HOGENOM; CLU_069313_0_2_6; -.
DR   OMA; ITQQPMT; -.
DR   Proteomes; UP000002493; Chromosome 1.
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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000255"
FT   CHAIN           16..259
FT                   /note="Flagellar L-ring protein 1"
FT                   /id="PRO_0000009478"
FT   REGION          38..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           16
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
FT   LIPID           16
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   259 AA;  27988 MW;  C9C5B60AE417171A CRC64;
     MKRICLLALI TTMSGCAMLE PIETDEVTQA TTVVDAVEGD KSKDESSGIV DTLRGRNDPV
     AGDPAWAPIH PKQKPEHYAA ATGSLFSPEH ITDLYDDSKP RGIGDIITVT LDETTSATKS
     ANADLSKTNE AQMDPLQVGG EELKVGGKYN FSYDLNNTNT FAGDSSAKQS NSISGYITVE
     VIEVLANGNL VIRGEKWMTL NTGDEYIRLS GTIRPDDINF DNTIASNRVS NARIQYSGTG
     LSQDMQEPGF LARFFNVAL
 
 
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