Y533_STRP6
ID Y533_STRP6 Reviewed; 269 AA.
AC Q5XD45; P82560;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Putative phosphatase M6_Spy0533;
DE EC=3.1.3.-;
GN OrderedLocusNames=M6_Spy0533;
OS Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=286636;
RN [1] {ECO:0000312|EMBL:AAT86668.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-946 / MGAS10394;
RX PubMed=15272401; DOI=10.1086/422697;
RA Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT "Progress toward characterization of the group A Streptococcus metagenome:
RT complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL J. Infect. Dis. 190:727-738(2004).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 21-33, AND MASS SPECTROMETRY.
RC STRAIN=JRS4 / Serotype M6 {ECO:0000269|Ref.2};
RA Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA VanBogelen R.A.;
RT "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT proteins.";
RL Submitted (MAY-2000) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- MASS SPECTROMETRY: Mass=30142.85; Method=Electrospray;
CC Evidence={ECO:0000269|Ref.2};
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. Cof family.
CC {ECO:0000255}.
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DR EMBL; CP000003; AAT86668.1; -; Genomic_DNA.
DR RefSeq; WP_002985513.1; NC_006086.1.
DR AlphaFoldDB; Q5XD45; -.
DR SMR; Q5XD45; -.
DR EnsemblBacteria; AAT86668; AAT86668; M6_Spy0533.
DR KEGG; spa:M6_Spy0533; -.
DR HOGENOM; CLU_044146_0_1_9; -.
DR OMA; GAWIQDP; -.
DR Proteomes; UP000001167; 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 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Magnesium; Metal-binding.
FT CHAIN 1..269
FT /note="Putative phosphatase M6_Spy0533"
FT /id="PRO_0000259671"
FT ACT_SITE 9
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 43..44
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250"
SQ SEQUENCE 269 AA; 30143 MW; CDBF68293E289E5E CRC64;
MSIKLVAVDI DGTLLTDDRR ITDDVFQAVQ EAKAQGVHVV IATGRPIAGV ISLLEQLELN
HKGNHVITFN GGLVQDAETG EEIVKELMTY DDYLETEFLS RKLGVHMHAI TKEGIYTANR
NIGKYTVHES TLVNMPIFYR TPEEMTNKEI IKMMMIDEPD LLDAAIKQIP QHFFDKYTIV
KSTPFYLEFM PKTVSKGNAI KHLAKKLGLD MSQTMAIGDA ENDRAMLEVV ANPVVMENGV
PELKKIAKYI TKSNNDSGVA HAIRKWVLN