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CHEC1_HALS3
ID   CHEC1_HALS3             Reviewed;         195 AA.
AC   B0R4J8; Q48298; Q7LY98;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Putative CheY-P phosphatase CheC1;
GN   Name=cheC1; Synonyms=cheJ; OrderedLocusNames=OE_2414R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R1 / S9;
RX   PubMed=7882970; DOI=10.1002/j.1460-2075.1995.tb07045.x;
RA   Rudolph J., Oesterhelt D.;
RT   "Chemotaxis and phototaxis require a CheA histidine kinase in the archaeon
RT   Halobacterium salinarium.";
RL   EMBO J. 14:667-673(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=8636990; DOI=10.1006/jmbi.1996.0267;
RA   Rudolph J., Oesterhelt D.;
RT   "Deletion analysis of the che operon in the archaeon Halobacterium
RT   salinarium.";
RL   J. Mol. Biol. 258:548-554(1996).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of CheY-P. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Deletion causes a reduction in chemo- and
CC       phototactic ability. Mutant has a 88:12 distribution of forward and
CC       reverse swimming (distribution is 50:50 for the wild-type).
CC       {ECO:0000269|PubMed:8636990}.
CC   -!- SIMILARITY: Belongs to the CheC family. {ECO:0000305}.
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DR   EMBL; X82645; CAA57971.1; -; Genomic_DNA.
DR   EMBL; AM774415; CAP13663.1; -; Genomic_DNA.
DR   PIR; D84253; D84253.
DR   PIR; S54305; S54305.
DR   RefSeq; WP_010902689.1; NC_010364.1.
DR   AlphaFoldDB; B0R4J8; -.
DR   SMR; B0R4J8; -.
DR   EnsemblBacteria; CAP13663; CAP13663; OE_2414R.
DR   GeneID; 5953635; -.
DR   GeneID; 62886519; -.
DR   KEGG; hsl:OE_2414R; -.
DR   HOGENOM; CLU_087860_3_1_2; -.
DR   OMA; LYIETEI; -.
DR   PhylomeDB; B0R4J8; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1550.10; -; 1.
DR   InterPro; IPR007597; CheC.
DR   InterPro; IPR028976; CheC-like_sf.
DR   Pfam; PF04509; CheC; 1.
DR   SUPFAM; SSF103039; SSF103039; 1.
PE   3: Inferred from homology;
KW   Chemotaxis; Hydrolase.
FT   CHAIN           1..195
FT                   /note="Putative CheY-P phosphatase CheC1"
FT                   /id="PRO_0000429070"
SQ   SEQUENCE   195 AA;  20959 MW;  9843F74C64679F42 CRC64;
     MSTMIDIRRL QTVNELAREG ASTVAENMSQ LTGVETQMQI TKINVIDVED LGAHLGAAKQ
     VGVSVPLKEQ PYGSVLVLFD DESARRVAGT MMGGIESEGG GYSDMERSAI REVGNIMTSG
     FIDGWANVLG RTIDISTPQL IRASGEDIAS HCVDPGEHEI AMVFDAELHA PDANVEAKIY
     SFPDIEAFVS MINSI
 
 
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