ID A0A1U7GFR9_9BACT Unreviewed; 339 AA.
AC A0A1U7GFR9;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=BGO49_16915 {ECO:0000313|EMBL:OJW14672.1};
OS Planctomycetales bacterium 71-10.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales.
OX NCBI_TaxID=1895807 {ECO:0000313|EMBL:OJW14672.1, ECO:0000313|Proteomes:UP000185848};
RN [1] {ECO:0000313|EMBL:OJW14672.1, ECO:0000313|Proteomes:UP000185848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=71-10 {ECO:0000313|EMBL:OJW14672.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJW14672.1}.
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DR EMBL; MKTT01000103; OJW14672.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1U7GFR9; -.
DR STRING; 1895807.BGO49_16915; -.
DR Proteomes; UP000185848; Unassembled WGS sequence.
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 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;
FT DOMAIN 67..306
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 339 AA; 37349 MW; CBCDE633D18D8537 CRC64;
MTAMPVNIET SQFEFLVSPL SSSTRPAPRE PHSTSVKVDL AATSHPGKVR NRNEDHYMVS
RVSRHMEVLM DNLPAGEIPH DVGETGYCMV VADGMGGMNA GDVASMMAIS TGVRLADKSV
KWGFKINEKE ARELLNRMSM YFQEIDRRLT VKSEADRRLF GMGTTLTLAY SVGAHLFLIH
VGDSRAYLWR RGEMKQLTRD HTVAQALADA GQIKPEDVRT HARRNTLTNY LGGHRGKIQA
DVRWTRLEDG DRLLLCSDGL NDMVDDAGIL EVLNRREDSK RTTEILLDKA MQAGGKDNIT
IVLAGYTIPA FVVPPAERPE GVAPHLIDTD DLPGGAGAN
//
