ID   Q9XA19_STRCO            Unreviewed;       515 AA.
AC   Q9XA19;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 116.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=SCO3845 {ECO:0000313|EMBL:CAB45212.1};
GN   ORFNames=SCH69.15 {ECO:0000313|EMBL:CAB45212.1};
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226 {ECO:0000313|EMBL:CAB45212.1, ECO:0000313|Proteomes:UP000001973};
RN   [1] {ECO:0000313|EMBL:CAB45212.1, ECO:0000313|Proteomes:UP000001973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145
RC   {ECO:0000313|Proteomes:UP000001973};
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA   Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939118; CAB45212.1; -; Genomic_DNA.
DR   PIR; T36714; T36714.
DR   RefSeq; NP_628033.1; NC_003888.3.
DR   RefSeq; WP_011029266.1; NZ_VNID01000003.1.
DR   AlphaFoldDB; Q9XA19; -.
DR   STRING; 100226.gene:17761470; -.
DR   PaxDb; 100226-SCO3845; -.
DR   PATRIC; fig|100226.15.peg.3915; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_025431_1_0_11; -.
DR   InParanoid; Q9XA19; -.
DR   OrthoDB; 9801841at2; -.
DR   PhylomeDB; Q9XA19; -.
DR   Proteomes; UP000001973; 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; PF00481; PP2C; 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:UP000001973}.
FT   DOMAIN          6..237
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          278..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   515 AA;  54317 MW;  A28145847FD529FB CRC64;
     MSLSLRFAAG SHKGMIREGN EDSGYAGPRL LAIADGMGGQ AAGEVASSEV ISTIVALDDD
     VPGSDVLTSL GHAVQRANDQ LRQMVEEDPA LEGMGTTLTA LLWTGQRLGM VHVGDSRAYL
     LRDGVLTQIT QDHTWVQRLV DEGRITEEEA GTHPQRSLLM RALGSGDHVE PDLSIREVRA
     GDRYLICSDG LSGVVSHQTM EDTLASYQGP QETVQELIQL ALRGGGPDNI TVIVADVLDL
     DTGDTLAGQL SDTPVVVGAV AENQAQMGDN GIMQTPAGRA AGLGRPGGQR GGGGEFGPPG
     SGDVTGFIPA GDFDDYGPDD FVKPRKSRKW LKRSLYTALA LAVIGGGTYG GWRWTQTQYY
     VGTNDDHLAL YRGISQDLAW VSLSKVQKDH PEIELKYLPP YQQKLVEATI PEGDLNDARA
     KIEELAVQAS ACKKQAARRT AETEKNAKTG EGEAGGTTGT TPASFTSKAS PSPNPSGSPE
     APESSESPST TAPTPGSGPT LSEEEQKVVS LCGKQ
//