ID   Y264_MYCPN              Reviewed;         281 AA.
AC   P75511;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Putative phosphatase MPN_264;
DE            EC=3.1.3.-;
GN   OrderedLocusNames=MPN_264; ORFNames=A65_orf281, MP569;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS   pneumoniae).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family.
CC       {ECO:0000305}.
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DR   EMBL; U00089; AAB96217.1; -; Genomic_DNA.
DR   PIR; S73895; S73895.
DR   RefSeq; NP_109952.1; NC_000912.1.
DR   RefSeq; WP_010874621.1; NC_000912.1.
DR   AlphaFoldDB; P75511; -.
DR   SMR; P75511; -.
DR   IntAct; P75511; 3.
DR   STRING; 272634.MPN_264; -.
DR   EnsemblBacteria; AAB96217; AAB96217; MPN_264.
DR   KEGG; mpn:MPN_264; -.
DR   PATRIC; fig|272634.6.peg.283; -.
DR   HOGENOM; CLU_044146_3_1_14; -.
DR   OMA; IANIYPT; -.
DR   BioCyc; MPNE272634:G1GJ3-415-MON; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR000150; Cof.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR00099; Cof-subfamily; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR   PROSITE; PS01228; COF_1; 1.
DR   PROSITE; PS01229; COF_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..281
FT                   /note="Putative phosphatase MPN_264"
FT                   /id="PRO_0000054436"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         9
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         44..45
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         228
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         231
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   281 AA;  32614 MW;  BF44564E7C7FBF11 CRC64;
     MIDLLGLDLD GTLLSRTRQI NDPTKQALAN LIQKKPSLKV MILTGRSLFS TLKYVQELNE
     LCKKPLVEYF CCYGGAKLYQ LNNNQPQEQY KFLIDSRQVK TVFEIVEQHK GLFLAYLDKP
     KAPYIILGAN QFYAWLIKQF WYKQRCEYFK NDHLTDGILK INVYFACPLR LKKVYQIIKR
     QFQDTLNVVN FSKHLIEITH KDGNKGYAIE AIAKKQGLSL KRMAVIGDSL NDRSMFEKVQ
     YSFAMSKSPD ELKLLATEIG TKTNRFRFSS LVDLITEKII N