Y732_MYCCT
ID Y732_MYCCT Reviewed; 287 AA.
AC P53661; Q2SRC1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Putative phosphatase MCAP_0732;
DE EC=3.1.3.-;
GN OrderedLocusNames=MCAP_0732;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-267.
RX PubMed=7476192; DOI=10.1111/j.1365-2958.1995.tb02321.x;
RA Bork P., Ouzounis C., Casari G., Schneider R., Sander C., Dolan M.,
RA Gilbert W., Gillevet P.M.;
RT "Exploring the Mycoplasma capricolum genome: a minimal cell reveals its
RT physiology.";
RL Mol. Microbiol. 16:955-967(1995).
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; CP000123; ABC01445.1; -; Genomic_DNA.
DR EMBL; Z33006; CAA83689.2; -; Genomic_DNA.
DR RefSeq; WP_011387576.1; NC_007633.1.
DR AlphaFoldDB; P53661; -.
DR SMR; P53661; -.
DR PRIDE; P53661; -.
DR EnsemblBacteria; ABC01445; ABC01445; MCAP_0732.
DR GeneID; 23778314; -.
DR KEGG; mcp:MCAP_0732; -.
DR HOGENOM; CLU_044146_0_1_14; -.
DR OMA; QHIYYEV; -.
DR OrthoDB; 1374424at2; -.
DR PhylomeDB; P53661; -.
DR Proteomes; UP000001928; 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.
FT CHAIN 1..287
FT /note="Putative phosphatase MCAP_0732"
FT /id="PRO_0000054442"
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 42..43
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT CONFLICT 265
FT /note="G -> R (in Ref. 2; CAA83689)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 287 AA; 32794 MW; 21F46D385F25AB99 CRC64;
MYKIIAIDID GTVYSRKHGV HELTKLALKK AREKGIKIVI ATGRTISTTR LIAKKLDLLN
TSIPFIGQNG GQVFSYETNG KVKIRYTKKF TNKQVNQIFN IIKQHKAHAF CYTLDENIAY
KNKGISIFFW WMKKRSQRNV KVYKPNKKLE SQITKYICFG KKENMRQMRK KVEDLGFSAF
SFSYVTNAKE NIEINPIGVN KGYGLEYVAK ELNIKPEEIL FFGDGENDLE AIKFAGTGVA
MKNSKLEIVK KAADDITSLT ADQGGVGEYI FKYVLKEEIP KEFSIKK
