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