CHEZ_SALTY
ID CHEZ_SALTY Reviewed; 214 AA.
AC P07800;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein phosphatase CheZ;
DE EC=3.1.3.-;
DE AltName: Full=Chemotaxis protein CheZ;
GN Name=cheZ; OrderedLocusNames=STM1915;
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=3298217; DOI=10.1128/jb.169.7.3301-3311.1987;
RA Stock A.M., Stock J.B.;
RT "Purification and characterization of the CheZ protein of bacterial
RT chemotaxis.";
RL J. Bacteriol. 169:3301-3311(1987).
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 FUNCTION.
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 [4]
RP FUNCTION, INTERACTION WITH CHEY, AND MUTAGENESIS OF ARG-54 AND VAL-166.
RX PubMed=8399392; DOI=10.1016/0167-4838(93)90019-n;
RA Huang C., Stewart R.C.;
RT "CheZ mutants with enhanced ability to dephosphorylate CheY, the response
RT regulator in bacterial chemotaxis.";
RL Biochim. Biophys. Acta 1202:297-304(1993).
RN [5]
RP MUTAGENESIS OF LEU-110; PHE-141; ASP-143 AND THR-145.
RX PubMed=8557655; DOI=10.1074/jbc.271.2.1232;
RA Blat Y., Eisenbach M.;
RT "Mutants with defective phosphatase activity show no phosphorylation-
RT dependent oligomerization of CheZ. The phosphatase of bacterial
RT chemotaxis.";
RL J. Biol. Chem. 271:1232-1236(1996).
RN [6]
RP FUNCTION, AND INTERACTION WITH CHEY.
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 [7]
RP FUNCTION, INTERACTION WITH CHEY, AND MUTAGENESIS OF ARG-54.
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 [8]
RP FUNCTION, AND INTERACTION WITH CHEY.
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 [9]
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX PubMed=20346719; DOI=10.1016/j.molcel.2010.03.001;
RA Paul K., Nieto V., Carlquist W.C., Blair D.F., Harshey R.M.;
RT "The c-di-GMP binding protein YcgR controls flagellar motor direction and
RT speed to affect chemotaxis by a 'backstop brake' mechanism.";
RL Mol. Cell 38:128-139(2010).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 200-214 IN COMPLEX WITH CHEY.
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) OF 207-214 IN COMPLEX WITH CHEY.
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: Plays an important role in bacterial chemotaxis signal
CC transduction pathway by accelerating the dephosphorylation of
CC phosphorylated CheY (CheY-P). Acts on free CheY-P.
CC {ECO:0000269|PubMed:14636076, ECO:0000269|PubMed:1902474,
CC ECO:0000269|PubMed:8399392, ECO:0000269|PubMed:8816756,
CC ECO:0000269|PubMed:9837737}.
CC -!- SUBUNIT: Homodimer. Interacts (via C-terminus) with phosphorylated CheY
CC (CheY-P). {ECO:0000269|PubMed:14636076, ECO:0000269|PubMed:16674976,
CC ECO:0000269|PubMed:18083806, ECO:0000269|PubMed:8399392,
CC ECO:0000269|PubMed:8816756, ECO:0000269|PubMed:9837737}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene display a strong
CC clockwise motor bias; in combination with a yhjH disruption and
CC overexpression of ycgR, cells switch from clockwise to a
CC counterclockwise bias. {ECO:0000269|PubMed:20346719}.
CC -!- SIMILARITY: Belongs to the CheZ family. {ECO:0000305}.
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DR EMBL; M16691; AAD15120.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20831.1; -; Genomic_DNA.
DR PIR; A27088; A27088.
DR RefSeq; NP_460872.1; NC_003197.2.
DR RefSeq; WP_000983586.1; NC_003197.2.
DR PDB; 2FKA; X-ray; 2.00 A; B=200-214.
DR PDB; 2FLK; X-ray; 2.10 A; B=200-214.
DR PDB; 2FLW; X-ray; 2.00 A; B=200-214.
DR PDB; 2FMF; X-ray; 2.00 A; B=200-214.
DR PDB; 2FMH; X-ray; 2.00 A; B=200-214.
DR PDB; 2FMI; X-ray; 2.30 A; B=200-214.
DR PDB; 2FMK; X-ray; 2.00 A; B=200-214.
DR PDB; 2PL9; X-ray; 2.60 A; D/E/F=196-214.
DR PDB; 2PMC; X-ray; 2.69 A; E/F=200-214.
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; P07800; -.
DR SMR; P07800; -.
DR STRING; 99287.STM1915; -.
DR PaxDb; P07800; -.
DR EnsemblBacteria; AAL20831; AAL20831; STM1915.
DR GeneID; 1253436; -.
DR KEGG; stm:STM1915; -.
DR PATRIC; fig|99287.12.peg.2031; -.
DR HOGENOM; CLU_080718_1_0_6; -.
DR OMA; EGPQIHA; -.
DR PhylomeDB; P07800; -.
DR BioCyc; SENT99287:STM1915-MON; -.
DR EvolutionaryTrace; P07800; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0009288; C:bacterial-type flagellum; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; 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:0050920; P:regulation of chemotaxis; IEA:InterPro.
DR InterPro; IPR007439; Chemotax_Pase_CheZ.
DR Pfam; PF04344; CheZ; 1.
DR PIRSF; PIRSF002884; CheZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Cytoplasm; Flagellar rotation; Hydrolase;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..214
FT /note="Protein phosphatase CheZ"
FT /id="PRO_0000089643"
FT REGION 176..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 147
FT /note="Enhances dephosphorylation of CheY-P"
FT /evidence="ECO:0000250"
FT MUTAGEN 54
FT /note="R->C: Constitutively active."
FT /evidence="ECO:0000269|PubMed:8399392,
FT ECO:0000269|PubMed:9837737"
FT MUTAGEN 110
FT /note="L->P: Loss of function."
FT /evidence="ECO:0000269|PubMed:8557655"
FT MUTAGEN 141
FT /note="F->I: Loss of function."
FT /evidence="ECO:0000269|PubMed:8557655"
FT MUTAGEN 143
FT /note="D->E: Loss of function."
FT /evidence="ECO:0000269|PubMed:8557655"
FT MUTAGEN 145
FT /note="T->M: Loss of function."
FT /evidence="ECO:0000269|PubMed:8557655"
FT MUTAGEN 166
FT /note="V->G: Enhanced activity."
FT /evidence="ECO:0000269|PubMed:8399392"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:2FMF"
SQ SEQUENCE 214 AA; 23920 MW; B4A34F2C11FC32FE CRC64;
MMQPSIKPAD EGSAGDIIAR IGSLTRMLRD SLRELGLDQA IAEAAEAIPD ARDRLDYVVQ
MTAQAAERAL NSVEASQPHQ DAMEKEAKAL TQRWDEWFDN PIELSDAREL VTDTRQFLRD
VPGHTSFTNA QLLDIMMAQD FQDLTGQVIK RMMDVIQEIE RQLLMVLLEN IPEQSARPKR
ENESLLNGPQ VDTSKAGVVA SQDQVDDLLD SLGF
