CHEZ_ECOLI
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 03-AUG-2022, entry version 116.
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; Proteobacteria; 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA23571.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; M13463; AAA23571.1; ALT_SEQ; 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 SWISS-2DPAGE; P0A9H9; -.
DR PaxDb; P0A9H9; -.
DR PRIDE; P0A9H9; -.
DR EnsemblBacteria; AAC74951; AAC74951; b1881.
DR EnsemblBacteria; BAA15697; BAA15697; BAA15697.
DR GeneID; 66674228; -.
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; EGPQIHA; -.
DR PhylomeDB; P0A9H9; -.
DR BioCyc; EcoCyc:CHEZ-MON; -.
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:0006470; P:protein dephosphorylation; IDA:EcoCyc.
DR GO; GO:1902021; P:regulation of bacterial-type flagellum-dependent cell motility; IC:ComplexPortal.
DR GO; GO:0050920; P:regulation of chemotaxis; IC:ComplexPortal.
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_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
