ID   CHEZ_ECOLI              Reviewed;         214 AA.
AC   P0A9H9; P07366;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Protein phosphatase CheZ;
DE            EC=3.1.3.-;
DE   AltName: Full=Chemotaxis protein CheZ;
GN   Name=cheZ; OrderedLocusNames=b1881, JW1870;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3510184; DOI=10.1128/jb.165.1.161-166.1986;
RA   Mutoh N., Simon M.I.;
RT   "Nucleotide sequence corresponding to five chemotaxis genes in Escherichia
RT   coli.";
RL   J. Bacteriol. 165:161-166(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RX   PubMed=6090423; DOI=10.1128/jb.160.1.36-41.1984;
RA   Matsumura P., Rydel J.J., Linzmeier R., Vacante D.;
RT   "Overexpression and sequence of the Escherichia coli cheY gene and
RT   biochemical activities of the CheY protein.";
RL   J. Bacteriol. 160:36-41(1984).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH CHEA AND CHEY.
RX   PubMed=8820640; DOI=10.1046/j.1365-2958.1996.393934.x;
RA   Wang H., Matsumura P.;
RT   "Characterization of the CheAS/CheZ complex: a specific interaction
RT   resulting in enhanced dephosphorylating activity on CheY-phosphate.";
RL   Mol. Microbiol. 19:695-703(1996).
RN   [7]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [8]
RP   FUNCTION, INTERACTION WITH CHEY, AND MUTAGENESIS OF ALA-65; LEU-90;
RP   PHE-117; ASP-143; GLY-188 AND VAL-205.
RX   PubMed=10852888; DOI=10.1128/jb.182.12.3544-3552.2000;
RA   Boesch K.C., Silversmith R.E., Bourret R.B.;
RT   "Isolation and characterization of nonchemotactic CheZ mutants of
RT   Escherichia coli.";
RL   J. Bacteriol. 182:3544-3552(2000).
RN   [9]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-90; TRP-94 AND PHE-117.
RX   PubMed=12644507; DOI=10.1128/jb.185.7.2354-2361.2003;
RA   Cantwell B.J., Draheim R.R., Weart R.B., Nguyen C., Stewart R.C.,
RA   Manson M.D.;
RT   "CheZ phosphatase localizes to chemoreceptor patches via CheA-short.";
RL   J. Bacteriol. 185:2354-2361(2003).
RN   [10]
RP   MUTAGENESIS OF ILE-21, AND INTERACTION WITH CHEY.
RX   PubMed=17998207; DOI=10.1074/jbc.m704400200;
RA   Silversmith R.E., Levin M.D., Schilling E., Bourret R.B.;
RT   "Kinetic characterization of catalysis by the chemotaxis phosphatase CheZ.
RT   Modulation of activity by the phosphorylated CheY substrate.";
RL   J. Biol. Chem. 283:756-765(2008).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH CHEY, SUBUNIT, AND
RP   MUTAGENESIS OF GLN-147.
RX   PubMed=12080332; DOI=10.1038/nsb816;
RA   Zhao R., Collins E.J., Bourret R.B., Silversmith R.E.;
RT   "Structure and catalytic mechanism of the E. coli chemotaxis phosphatase
RT   CheZ.";
RL   Nat. Struct. Biol. 9:570-575(2002).
CC   -!- FUNCTION: Plays an important role in bacterial chemotaxis signal
CC       transduction pathway by accelerating the dephosphorylation of
CC       phosphorylated CheY (CheY-P). {ECO:0000269|PubMed:10852888,
CC       ECO:0000269|PubMed:8820640}.
CC   -!- SUBUNIT: Homodimer. Interacts with CheA isoform CheA(short). Interacts
CC       (via C-terminus) with phosphorylated CheY (CheY-P).
CC       {ECO:0000269|PubMed:10852888, ECO:0000269|PubMed:12080332,
CC       ECO:0000269|PubMed:17998207, ECO:0000269|PubMed:8820640}.
CC   -!- INTERACTION:
CC       P0A9H9; P07363: cheA; NbExp=3; IntAct=EBI-546726, EBI-1026773;
CC       P0A9H9; P0AE67: cheY; NbExp=6; IntAct=EBI-546726, EBI-546693;
CC       P0A9H9; P0A9H9: cheZ; NbExp=2; IntAct=EBI-546726, EBI-546726;
CC       P0A9H9; P0A9B2: gapA; NbExp=2; IntAct=EBI-546726, EBI-368904;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12644507}.
CC       Note=Colocalizes with CheA chemoreceptor patches near the cell poles,
CC       which requires CheA(short).
CC   -!- SIMILARITY: Belongs to the CheZ family. {ECO:0000305}.
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DR   EMBL; AH000879; AAA23571.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74951.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15697.1; -; Genomic_DNA.
DR   EMBL; K02175; AAA23578.1; -; Genomic_DNA.
DR   PIR; F25195; QRECCZ.
DR   RefSeq; NP_416395.1; NC_000913.3.
DR   RefSeq; WP_000983609.1; NZ_STEB01000026.1.
DR   PDB; 1KMI; X-ray; 2.90 A; Z=1-214.
DR   PDBsum; 1KMI; -.
DR   AlphaFoldDB; P0A9H9; -.
DR   SMR; P0A9H9; -.
DR   BioGRID; 4259554; 392.
DR   BioGRID; 850749; 2.
DR   ComplexPortal; CPX-1088; Chemotaxis phosphorelay complex CheY-CheZ.
DR   DIP; DIP-9275N; -.
DR   IntAct; P0A9H9; 22.
DR   STRING; 511145.b1881; -.
DR   PaxDb; 511145-b1881; -.
DR   EnsemblBacteria; AAC74951; AAC74951; b1881.
DR   GeneID; 75171954; -.
DR   GeneID; 946392; -.
DR   KEGG; ecj:JW1870; -.
DR   KEGG; eco:b1881; -.
DR   PATRIC; fig|511145.12.peg.1962; -.
DR   EchoBASE; EB0149; -.
DR   eggNOG; COG3143; Bacteria.
DR   HOGENOM; CLU_080718_1_0_6; -.
DR   InParanoid; P0A9H9; -.
DR   OMA; IHADKRE; -.
DR   OrthoDB; 9773007at2; -.
DR   PhylomeDB; P0A9H9; -.
DR   BioCyc; EcoCyc:CHEZ-MONOMER; -.
DR   EvolutionaryTrace; P0A9H9; -.
DR   PRO; PR:P0A9H9; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0009288; C:bacterial-type flagellum; IEA:InterPro.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0098561; C:methyl accepting chemotaxis protein complex; IDA:CAFA.
DR   GO; GO:0005886; C:plasma membrane; IDA:CAFA.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:EcoCyc.
DR   GO; GO:0071978; P:bacterial-type flagellum-dependent swarming motility; IDA:EcoCyc.
DR   GO; GO:0006935; P:chemotaxis; IMP:EcoCyc.
DR   GO; GO:1902021; P:regulation of bacterial-type flagellum-dependent cell motility; NAS:ComplexPortal.
DR   GO; GO:0050920; P:regulation of chemotaxis; NAS:ComplexPortal.
DR   Gene3D; 1.10.287.500; Helix hairpin bin; 1.
DR   Gene3D; 1.20.5.590; Single helix bin; 1.
DR   InterPro; IPR007439; Chemotax_Pase_CheZ.
DR   PANTHER; PTHR43693; PROTEIN PHOSPHATASE CHEZ; 1.
DR   PANTHER; PTHR43693:SF1; PROTEIN PHOSPHATASE CHEZ; 1.
DR   Pfam; PF04344; CheZ; 1.
DR   PIRSF; PIRSF002884; CheZ; 1.
DR   SUPFAM; SSF75708; Chemotaxis phosphatase CheZ; 1.
DR   SWISS-2DPAGE; P0A9H9; -.
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_0000089641"
FT   REGION          174..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..199
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            147
FT                   /note="Enhances dephosphorylation of CheY-P"
FT   MUTAGEN         21
FT                   /note="I->T: Gain of function, increased counterclockwise
FT                   rotation of flagella."
FT                   /evidence="ECO:0000269|PubMed:17998207"
FT   MUTAGEN         65
FT                   /note="A->V: Loss of function, fails to oligomerize."
FT                   /evidence="ECO:0000269|PubMed:10852888"
FT   MUTAGEN         90
FT                   /note="L->S: Loss of localization to the cell pole. Fails
FT                   to oligomerize."
FT                   /evidence="ECO:0000269|PubMed:10852888,
FT                   ECO:0000269|PubMed:12644507"
FT   MUTAGEN         94
FT                   /note="W->R: Loss of localization to the cell pole."
FT                   /evidence="ECO:0000269|PubMed:12644507"
FT   MUTAGEN         117
FT                   /note="F->S: Loss of localization to the cell pole."
FT                   /evidence="ECO:0000269|PubMed:10852888,
FT                   ECO:0000269|PubMed:12644507"
FT   MUTAGEN         143
FT                   /note="D->G: Loss of function. Fails to oligomerize."
FT                   /evidence="ECO:0000269|PubMed:10852888"
FT   MUTAGEN         147
FT                   /note="Q->A: Severely diminished function, exclusive
FT                   clockwise flagellar rotation."
FT                   /evidence="ECO:0000269|PubMed:12080332"
FT   MUTAGEN         188
FT                   /note="G->E: Diminished ability to stimulate
FT                   dephosphorylation of CheY-P."
FT                   /evidence="ECO:0000269|PubMed:10852888"
FT   MUTAGEN         205
FT                   /note="V->E: Severely impairs the interaction the
FT                   interaction with CheY-P."
FT                   /evidence="ECO:0000269|PubMed:10852888"
FT   CONFLICT        119
FT                   /note="A -> P (in Ref. 1; AAA23571)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="A -> G (in Ref. 1; AAA23571)"
FT                   /evidence="ECO:0000305"
FT   HELIX           14..35
FT                   /evidence="ECO:0007829|PDB:1KMI"
FT   HELIX           37..43
FT                   /evidence="ECO:0007829|PDB:1KMI"
FT   TURN            44..47
FT                   /evidence="ECO:0007829|PDB:1KMI"
FT   HELIX           48..54
FT                   /evidence="ECO:0007829|PDB:1KMI"
FT   TURN            55..57
FT                   /evidence="ECO:0007829|PDB:1KMI"
FT   HELIX           58..64
FT                   /evidence="ECO:0007829|PDB:1KMI"
FT   TURN            65..67
FT                   /evidence="ECO:0007829|PDB:1KMI"
FT   HELIX           68..97
FT                   /evidence="ECO:0007829|PDB:1KMI"
FT   HELIX           104..138
FT                   /evidence="ECO:0007829|PDB:1KMI"
FT   HELIX           141..161
FT                   /evidence="ECO:0007829|PDB:1KMI"
FT   TURN            162..167
FT                   /evidence="ECO:0007829|PDB:1KMI"
FT   HELIX           204..212
FT                   /evidence="ECO:0007829|PDB:1KMI"
SQ   SEQUENCE   214 AA;  23976 MW;  42308F5AC0685D27 CRC64;
     MMQPSIKPAD EHSAGDIIAR IGSLTRMLRD SLRELGLDQA IAEAAEAIPD ARDRLYYVVQ
     MTAQAAERAL NSVEASQPHQ DQMEKSAKAL TQRWDDWFAD PIDLADAREL VTDTRQFLAD
     VPAHTSFTNA QLLEIMMAQD FQDLTGQVIK RMMDVIQEIE RQLLMVLLEN IPEQESRPKR
     ENQSLLNGPQ VDTSKAGVVA SQDQVDDLLD SLGF
//