ID D7C3F9_STRBB Unreviewed; 468 AA.
AC D7C3F9;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN OrderedLocusNames=SBI_07064 {ECO:0000313|EMBL:ADI10184.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI10184.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI10184.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI10184.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
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; CP002047; ADI10184.1; -; Genomic_DNA.
DR RefSeq; WP_014179634.1; NC_016582.1.
DR AlphaFoldDB; D7C3F9; -.
DR STRING; 749414.SBI_07064; -.
DR KEGG; sbh:SBI_07064; -.
DR PATRIC; fig|749414.3.peg.7266; -.
DR eggNOG; COG0631; Bacteria.
DR HOGENOM; CLU_034545_2_0_11; -.
DR Proteomes; UP000000377; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000000377}.
FT DOMAIN 198..458
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 39..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 468 AA; 47219 MW; 23E83B06A0C6BB9B CRC64;
MSQMPQLPGV AACPTCEEPL ESGDNFCGVC GADLASAAPD AAVAADRPAP PVNGAARAGR
QEPEDYPLPA PAPAPPAAAS ALAGPDVPAA SDVPGACAWD VPAAPDVPDV PDVPDVRDVS
TADPRSAAAA GEQPAPDTPA GTPGTPGTPG IGTNTDASSG RRLCAACREG TIDQDGYCDS
CGHAQPRERD HMERELAGVA AASDRGLRHH RNEDAFAVSA AALPDGSPAV LAVVCDGVSS
ATRPDDASAA AARAAGQSLL AALPRGAHPQ TAMNEAIVAA AEAVNSLAAE AGPTGRHDEA
HQRQQNAPAC TIVSAVVTSG ILTVGWIGDS RAYWVPDDRS ASPARLTEDD SWAAQMVAAG
LMSEAEAYAD ERAHAITGWL GADAYELEPH TASYKPDQPG VVVVCTDGLW NYAESAQEMA
RALPQDAHAR PMHSARVLVG HALEGGGHDN VTVAVLPFPA EPGGAGSG
//
