Y2019_YERPS
ID Y2019_YERPS Reviewed; 245 AA.
AC Q66AW1;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable phosphatase YPTB2019 {ECO:0000255|HAMAP-Rule:MF_01561};
DE EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01561};
GN OrderedLocusNames=YPTB2019;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH21257.1; -; Genomic_DNA.
DR RefSeq; WP_002211221.1; NZ_CP009712.1.
DR AlphaFoldDB; Q66AW1; -.
DR SMR; Q66AW1; -.
DR EnsemblBacteria; CAH21257; CAH21257; YPTB2019.
DR GeneID; 66841548; -.
DR KEGG; ypo:BZ17_446; -.
DR KEGG; yps:YPTB2019; -.
DR PATRIC; fig|273123.14.peg.476; -.
DR OMA; SEPNCRA; -.
DR Proteomes; UP000001011; 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; Zinc.
FT CHAIN 1..245
FT /note="Probable phosphatase YPTB2019"
FT /id="PRO_0000228714"
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; 26930 MW; F2927806F668F762 CRC64;
MYPVDLHMHT VASTHAYSTL HDYIAEAKLK NIKLFAITDH GPDMADAPHY WHFMNMRVWP
RLVDGVGILR GIEANIKNLD GDIDCTGPML DAVDLLIAGF HEPVFPPQDK AANTQAMIAT
MAQGNVHIIS HPGNPKYPVD IPAIAQAAAK YNVALELNNS SFAHSRKGSE ANCRAIAAAV
RDAGGWLALG SDSHIAYALG IFEHCERIIA EVNFPQERIL NVSPRRLLDY LEQRGRPAIP
ELAEL