ID   Y3987_ALISL             Reviewed;         247 AA.
AC   B6ESF2;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Probable phosphatase VSAL_II0887 {ECO:0000255|HAMAP-Rule:MF_01561};
DE            EC=3.1.3.- {ECO:0000255|HAMAP-Rule:MF_01561};
GN   OrderedLocusNames=VSAL_II0887;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the PHP family. {ECO:0000255|HAMAP-
CC       Rule:MF_01561}.
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DR   EMBL; FM178380; CAQ81641.1; -; Genomic_DNA.
DR   RefSeq; WP_012552156.1; NC_011313.1.
DR   AlphaFoldDB; B6ESF2; -.
DR   SMR; B6ESF2; -.
DR   STRING; 316275.VSAL_II0887; -.
DR   EnsemblBacteria; CAQ81641; CAQ81641; VSAL_II0887.
DR   KEGG; vsa:VSAL_II0887; -.
DR   eggNOG; COG1387; Bacteria.
DR   HOGENOM; CLU_061999_0_1_6; -.
DR   OMA; SEPNCRA; -.
DR   OrthoDB; 1615112at2; -.
DR   Proteomes; UP000001730; Chromosome 2.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   HAMAP; MF_01561; YcdX_phosphat; 1.
DR   InterPro; IPR023710; Phosphatase_YcdX_put.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   SUPFAM; SSF89550; SSF89550; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN           1..247
FT                   /note="Probable phosphatase VSAL_II0887"
FT                   /id="PRO_0000382654"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         130
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
FT   BINDING         194
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01561"
SQ   SEQUENCE   247 AA;  27370 MW;  A488D0002A65CA91 CRC64;
     MRIQVDTHTY ASGHAYSTIS ENAFSASTLG LPMFCTTDHA SSMPGAPHYW FFSNQRVLPR
     FLHGVAILRG CEVNICNLEG DIDIPLSVDQ NLDWIIASFH EPVFPPKNKL VHTQALIKII
     SSGRVDALGH LGNPNFDFDF KEVIQEAVKH NVAIEINNTS LKGTSRVGSV DRCYEIAKIA
     KELGAYITTG SDAHFCQDIG KFEKVEQLID ALDFPFDKII THSPKQFLAF LALRGHAPIA
     EFEALSK