ID   A8AVV5_STRGC            Unreviewed;       246 AA.
AC   A8AVV5;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=SGO_0599 {ECO:0000313|EMBL:ABV09792.1};
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705 {ECO:0000313|EMBL:ABV09792.1, ECO:0000313|Proteomes:UP000001131};
RN   [1] {ECO:0000313|EMBL:ABV09792.1, ECO:0000313|Proteomes:UP000001131}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288
RC   {ECO:0000313|Proteomes:UP000001131};
RX   PubMed=17720781; DOI=10.1128/JB.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
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         Evidence={ECO:0000256|ARBA:ARBA00001512};
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         Evidence={ECO:0000256|ARBA:ARBA00001482};
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DR   EMBL; CP000725; ABV09792.1; -; Genomic_DNA.
DR   RefSeq; WP_012000093.1; NC_009785.1.
DR   AlphaFoldDB; A8AVV5; -.
DR   STRING; 467705.SGO_0599; -.
DR   KEGG; sgo:SGO_0599; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_4_1_9; -.
DR   Proteomes; UP000001131; Chromosome.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
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   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ABV09792.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001131}.
FT   DOMAIN          2..240
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   246 AA;  26870 MW;  0F9FE3EF1A5669EC CRC64;
     MEIALLTDVG KKRTNNQDFV NHFVNRSGMP LIVLADGMGG HRAGNIASEM AVTDLGAAWV
     DTQIDSVNGV RDWFAEHLEA ENKKIHEVGQ SDEYKGMGTT LEAIAIIGNQ AIYAHIGDSR
     IGLVRGEEYK QLTSDHSLVN ALLKAGQITA EEAERHPQRN IITQSIGQKD EIQPDFGIIT
     LEEGDYIVIN SDGLSNMVAG SEIYDILKSD LTLSEKAQTL IRFANNAGGL DNITVALVYF
     DKEEEA
//