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YCDX_ECO57
ID   YCDX_ECO57              Reviewed;         245 AA.
AC   Q8X9J6; Q7AFB4;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Probable phosphatase YcdX {ECO:0000255|HAMAP-Rule:MF_01561};
DE            EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01561};
GN   Name=ycdX {ECO:0000255|HAMAP-Rule:MF_01561};
GN   OrderedLocusNames=Z1667, ECs1411;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01561};
CC       Note=Binds 3 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_01561};
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01561}.
CC   -!- SIMILARITY: Belongs to the PHP family. {ECO:0000255|HAMAP-
CC       Rule:MF_01561}.
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DR   EMBL; AE005174; AAG55780.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34834.1; -; Genomic_DNA.
DR   PIR; C90805; C90805.
DR   PIR; H85664; H85664.
DR   RefSeq; NP_309438.1; NC_002695.1.
DR   RefSeq; WP_000283664.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X9J6; -.
DR   SMR; Q8X9J6; -.
DR   STRING; 155864.EDL933_1607; -.
DR   EnsemblBacteria; AAG55780; AAG55780; Z1667.
DR   EnsemblBacteria; BAB34834; BAB34834; ECs_1411.
DR   GeneID; 66670698; -.
DR   GeneID; 912538; -.
DR   KEGG; ece:Z1667; -.
DR   KEGG; ecs:ECs_1411; -.
DR   PATRIC; fig|386585.9.peg.1510; -.
DR   eggNOG; COG1387; Bacteria.
DR   HOGENOM; CLU_061999_0_1_6; -.
DR   OMA; SEPNCRA; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01561; YcdX_phosphat; 1.
DR   InterPro; IPR023710; Phosphatase_YcdX_put.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   Pfam; PF02811; PHP; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; SSF89550; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..245
FT                   /note="Probable phosphatase YcdX"
FT                   /id="PRO_0000228692"
FT   BINDING         7
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         9
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         15
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         101
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         192
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
SQ   SEQUENCE   245 AA;  26832 MW;  ADA8D1FB462D4F15 CRC64;
     MYPVDLHMHT VASTHAYSTL SDYIAQAKQK GIKLFAITDH GPDMEDAPHH WHFINMRIWP
     RVVDGVGILR GIEANIKNVD GEIDCSGKMF DSLDLIIAGF HEPVFAPHDK ATNTQAMIAT
     IASGNVHIIS HPGNPKYEID VKAVAEAAAK HQVALEINNS SFLHSRKGSE DNCRAVAAAV
     RDAGGWVALG SDSHTAFTMG EFEECLKILD AVDFPPERIL NVSPRRLLNF LESRGMAPIA
     EFADL
 
 
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