CHEY_SALTY
ID CHEY_SALTY Reviewed; 129 AA.
AC P0A2D5; P06657;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Chemotaxis protein CheY;
GN Name=cheY; OrderedLocusNames=STM1916;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2999789; DOI=10.1073/pnas.82.23.7989;
RA Stock A., Koshland D.E. Jr., Stock J.;
RT "Homologies between the Salmonella typhimurium CheY protein and proteins
RT involved in the regulation of chemotaxis, membrane protein synthesis, and
RT sporulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:7989-7993(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP PHOSPHORYLATION AT ASP-57.
RX PubMed=3280143; DOI=10.1016/0092-8674(88)90489-8;
RA Hess J.F., Oosawa K., Kaplan N., Simon M.I.;
RT "Phosphorylation of three proteins in the signaling pathway of bacterial
RT chemotaxis.";
RL Cell 53:79-87(1988).
RN [4]
RP PHOSPHORYLATION AT ASP-57, AND MUTAGENESIS OF ASP-13; ASP-57 AND LYS-109.
RX PubMed=1902474; DOI=10.1016/s0021-9258(18)92982-0;
RA Lukat G.S., Lee B.H., Mottonen J.M., Stock A.M., Stock J.B.;
RT "Roles of the highly conserved aspartate and lysine residues in the
RT response regulator of bacterial chemotaxis.";
RL J. Biol. Chem. 266:8348-8354(1991).
RN [5]
RP DEPHOSPHORYLATION BY CHEZ.
RX PubMed=8816756; DOI=10.1073/pnas.93.19.10090;
RA Bren A., Welch M., Blat Y., Eisenbach M.;
RT "Signal termination in bacterial chemotaxis: CheZ mediates
RT dephosphorylation of free rather than switch-bound CheY.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10090-10093(1996).
RN [6]
RP INTERACTION WITH CHEZ.
RX PubMed=9837737; DOI=10.1006/jmbi.1998.2224;
RA Blat Y., Gillespie B., Bren A., Dahlquist F.W., Eisenbach M.;
RT "Regulation of phosphatase activity in bacterial chemotaxis.";
RL J. Mol. Biol. 284:1191-1199(1998).
RN [7]
RP DEPHOSPHORYLATION BY CHEZ.
RX PubMed=14636076; DOI=10.1021/bi034883t;
RA Wolanin P.M., Webre D.J., Stock J.B.;
RT "Mechanism of phosphatase activity in the chemotaxis response regulator
RT CheY.";
RL Biochemistry 42:14075-14082(2003).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=2645526; DOI=10.1038/337745a0;
RA Stock A.M., Mottonen J.M., Stock J.B., Schutt C.E.;
RT "Three-dimensional structure of CheY, the response regulator of bacterial
RT chemotaxis.";
RL Nature 337:745-749(1989).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8257674; DOI=10.1021/bi00212a001;
RA Stock A.M., Martinez-Hackert E., Rasmussen B.F., West A.H., Stock J.B.,
RA Ringe D., Petsko G.A.;
RT "Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl
RT transfer in bacterial chemotaxis.";
RL Biochemistry 32:13375-13380(1993).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CHEZ, AND MUTAGENESIS
RP OF PHE-14 AND ASN-59.
RX PubMed=16674976; DOI=10.1016/j.jmb.2006.03.050;
RA Guhaniyogi J., Robinson V.L., Stock A.M.;
RT "Crystal structures of beryllium fluoride-free and beryllium fluoride-bound
RT CheY in complex with the conserved C-terminal peptide of CheZ reveal dual
RT binding modes specific to CheY conformation.";
RL J. Mol. Biol. 359:624-645(2006).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS) IN COMPLEX WITH CHEZ.
RX PubMed=18083806; DOI=10.1128/jb.01414-07;
RA Guhaniyogi J., Wu T., Patel S.S., Stock A.M.;
RT "Interaction of CheY with the C-terminal peptide of CheZ.";
RL J. Bacteriol. 190:1419-1428(2008).
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. Shows autophosphatase
CC activity which is enhanced by CheZ.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 1 Mg(2+) ion per subunit.;
CC -!- SUBUNIT: Interacts (phosphorylated CheY) with CheZ (via C-terminus).
CC {ECO:0000269|PubMed:16674976, ECO:0000269|PubMed:18083806,
CC ECO:0000269|PubMed:9837737}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated by CheA or acetylated by acetyl-CoA synthetase,
CC depending on which acetate metabolism pathway is available (By
CC similarity). Dephosphorylated (inactivated) by CheZ. {ECO:0000250,
CC ECO:0000269|PubMed:1902474, ECO:0000269|PubMed:3280143}.
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DR EMBL; M12131; AAA27037.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20832.1; -; Genomic_DNA.
DR PIR; A23567; QREBCY.
DR RefSeq; NP_460873.1; NC_003197.2.
DR RefSeq; WP_000763861.1; NC_003197.2.
DR PDB; 2CHE; X-ray; 1.80 A; A=2-129.
DR PDB; 2CHF; X-ray; 1.80 A; A=2-129.
DR PDB; 2CHY; X-ray; 2.70 A; A=2-129.
DR PDB; 2FKA; X-ray; 2.00 A; A=1-129.
DR PDB; 2FLK; X-ray; 2.10 A; A=1-129.
DR PDB; 2FLW; X-ray; 2.00 A; A=1-129.
DR PDB; 2FMF; X-ray; 2.00 A; A=1-129.
DR PDB; 2FMH; X-ray; 2.00 A; A=1-129.
DR PDB; 2FMI; X-ray; 2.30 A; A=1-129.
DR PDB; 2FMK; X-ray; 2.00 A; A=1-129.
DR PDB; 2PL9; X-ray; 2.60 A; A/B/C=2-129.
DR PDB; 2PMC; X-ray; 2.69 A; A/B/C/D=2-129.
DR PDBsum; 2CHE; -.
DR PDBsum; 2CHF; -.
DR PDBsum; 2CHY; -.
DR PDBsum; 2FKA; -.
DR PDBsum; 2FLK; -.
DR PDBsum; 2FLW; -.
DR PDBsum; 2FMF; -.
DR PDBsum; 2FMH; -.
DR PDBsum; 2FMI; -.
DR PDBsum; 2FMK; -.
DR PDBsum; 2PL9; -.
DR PDBsum; 2PMC; -.
DR AlphaFoldDB; P0A2D5; -.
DR BMRB; P0A2D5; -.
DR SMR; P0A2D5; -.
DR STRING; 99287.STM1916; -.
DR PaxDb; P0A2D5; -.
DR EnsemblBacteria; AAL20832; AAL20832; STM1916.
DR GeneID; 1253437; -.
DR GeneID; 66756437; -.
DR KEGG; stm:STM1916; -.
DR PATRIC; fig|99287.12.peg.2032; -.
DR HOGENOM; CLU_000445_69_12_6; -.
DR OMA; AAGAHEY; -.
DR PhylomeDB; P0A2D5; -.
DR BioCyc; SENT99287:STM1916-MON; -.
DR EvolutionaryTrace; P0A2D5; -.
DR PHI-base; PHI:8732; -.
DR Proteomes; UP000001014; Chromosome.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chemotaxis; Cytoplasm; Flagellar rotation;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome;
KW Two-component regulatory system.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..129
FT /note="Chemotaxis protein CheY"
FT /id="PRO_0000081045"
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 BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00169,
FT ECO:0000269|PubMed:1902474, ECO:0000269|PubMed:3280143"
FT MOD_RES 92
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 109
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 13
FT /note="D->N: Abolishes function, reduced rate of
FT phosphorylation and affinity for magnesium ion."
FT /evidence="ECO:0000269|PubMed:1902474"
FT MUTAGEN 14
FT /note="F->A: Diminished rate of phosphorylation."
FT /evidence="ECO:0000269|PubMed:16674976"
FT MUTAGEN 57
FT /note="D->N: Abolishes function and phosphorylation."
FT /evidence="ECO:0000269|PubMed:1902474"
FT MUTAGEN 59
FT /note="N->A: Diminished rate of phosphorylation."
FT /evidence="ECO:0000269|PubMed:16674976"
FT MUTAGEN 109
FT /note="K->R: Abolishes function, decreased autophosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:1902474"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:2CHE"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:2CHE"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:2CHE"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:2CHE"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:2CHE"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2CHE"
FT HELIX 65..74
FT /evidence="ECO:0007829|PDB:2CHE"
FT TURN 76..80
FT /evidence="ECO:0007829|PDB:2CHE"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:2CHE"
FT HELIX 92..100
FT /evidence="ECO:0007829|PDB:2CHE"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:2CHE"
FT HELIX 113..127
FT /evidence="ECO:0007829|PDB:2CHE"
SQ SEQUENCE 129 AA; 14125 MW; A0B4712E18626207 CRC64;
MADKELKFLV VDDFSTMRRI VRNLLKELGF NNVEEAEDGV DALNKLQAGG FGFIISDWNM
PNMDGLELLK TIRADSAMSA LPVLMVTAEA KKENIIAAAQ AGASGYVVKP FTAATLEEKL
NKIFEKLGM
