ID   PP2C_STRP6              Reviewed;         246 AA.
AC   Q5XAP6; P82576;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Putative protein phosphatase 2C-type;
DE            EC=3.1.3.16;
GN   OrderedLocusNames=M6_Spy1382;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1] {ECO:0000312|EMBL:AAT87517.1}
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 28-57; 85-120 AND 217-227, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O14156};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:O14156};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250|UniProtKB:O14156};
CC   -!- MASS SPECTROMETRY: Mass=27020.19; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.2};
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DR   EMBL; CP000003; AAT87517.1; -; Genomic_DNA.
DR   RefSeq; WP_002983660.1; NC_006086.1.
DR   AlphaFoldDB; Q5XAP6; -.
DR   SMR; Q5XAP6; -.
DR   GeneID; 69900502; -.
DR   KEGG; spa:M6_Spy1382; -.
DR   HOGENOM; CLU_034545_4_1_9; -.
DR   BRENDA; 3.1.3.16; 16491.
DR   Proteomes; UP000001167; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   NCBIfam; NF033484; Stp1_PP2C_phos; 1.
DR   PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1.
DR   PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF13672; PP2C_2; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Protein phosphatase.
FT   CHAIN           1..246
FT                   /note="Putative protein phosphatase 2C-type"
FT                   /id="PRO_0000273577"
FT   DOMAIN          2..240
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT   BINDING         36
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O14156"
FT   BINDING         36
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O14156"
FT   BINDING         37
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O14156"
FT   BINDING         231
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O14156"
SQ   SEQUENCE   246 AA;  27020 MW;  EF253B14CCE2AEA0 CRC64;
     MKISLKTDIG QKRSNNQDFI NKFDNKKGIT LVILADGMGG HRAGNIASEM TVTDLGREWV
     KTDFTELSQI RDWLFETIQS ENQRIYDLGQ SEDFKGMGTT VEAVALVESS AIYAHIGDSR
     IGLVHDGHYT LLTSDHSLVN ELVKAGQITE EEAASHPQRN IITQSIGQAS PVEPDLGVRV
     LEPGDYLVIN SDGLTNMISN DEIVTILGSK VSLDEKNQEM IDLANLRGGL DNITIALVHN
     ESEDVE
//