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CHEY_YEREN
ID   CHEY_YEREN              Reviewed;         129 AA.
AC   Q93P00;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Chemotaxis protein CheY;
GN   Name=cheY;
OS   Yersinia enterocolitica.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=630;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11371518; DOI=10.1128/jb.183.12.3556-3563.2001;
RA   Heusipp G., Young G.M., Miller V.L.;
RT   "HreP, an in vivo-expressed protease of Yersinia enterocolitica, is a new
RT   member of the family of Subtilisin/Kexin-like proteases.";
RL   J. Bacteriol. 183:3556-3563(2001).
CC   -!- FUNCTION: Involved in the transmission of sensory signals from the
CC       chemoreceptors to the flagellar motors. In its active (phosphorylated
CC       or acetylated) form, CheY exhibits enhanced binding to a switch
CC       component, FliM, at the flagellar motor which induces a change from
CC       counterclockwise to clockwise flagellar rotation (By similarity).
CC       {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 1 Mg(2+) ion per subunit.;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: Phosphorylated by CheA or acetylated by acetyl-CoA synthetase,
CC       depending on which acetate metabolism pathway is available.
CC       {ECO:0000250}.
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DR   EMBL; AF354753; AAK40116.1; -; Genomic_DNA.
DR   RefSeq; WP_005164479.1; NZ_UHIX01000001.1.
DR   AlphaFoldDB; Q93P00; -.
DR   SMR; Q93P00; -.
DR   STRING; 1443113.LC20_02144; -.
DR   GeneID; 67421573; -.
DR   eggNOG; COG0745; Bacteria.
DR   OMA; AAGAHEY; -.
DR   OrthoDB; 1630092at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0097588; P:archaeal or bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Acetylation; Chemotaxis; Cytoplasm; Flagellar rotation; Magnesium;
KW   Metal-binding; Phosphoprotein; Two-component regulatory system.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..129
FT                   /note="Chemotaxis protein CheY"
FT                   /id="PRO_0000081047"
FT   DOMAIN          7..124
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         57
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00169"
FT   MOD_RES         92
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         109
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   129 AA;  14164 MW;  DE2F97644C040337 CRC64;
     MADKNLRFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLRTGG FDFVVSDWNM
     PNMDGLDLLK TIRADGALGT LPVLMVTAEA KKENIIAAAQ AGASGYVVKP FTAATLEEKL
     NKIFEKLGM
 
 
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