ID   Q89P80_BRADU            Unreviewed;       258 AA.
AC   Q89P80;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=blr3603 {ECO:0000313|EMBL:BAC48868.1};
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC48868.1, ECO:0000313|Proteomes:UP000002526};
RN   [1] {ECO:0000313|Proteomes:UP000002526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC   {ECO:0000313|Proteomes:UP000002526};
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(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; BA000040; BAC48868.1; -; Genomic_DNA.
DR   RefSeq; NP_770243.1; NC_004463.1.
DR   RefSeq; WP_011086384.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89P80; -.
DR   STRING; 224911.AAV28_15025; -.
DR   EnsemblBacteria; BAC48868; BAC48868; BAC48868.
DR   GeneID; 64023340; -.
DR   KEGG; bja:blr3603; -.
DR   PATRIC; fig|224911.44.peg.3264; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_0_3_5; -.
DR   InParanoid; Q89P80; -.
DR   OrthoDB; 9801841at2; -.
DR   PhylomeDB; Q89P80; -.
DR   Proteomes; UP000002526; 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:UP000002526}.
FT   DOMAIN          9..239
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   258 AA;  27875 MW;  A5A1AD60BB65DDDF CRC64;
     MVHTPSLFDV GSVTHAGRVR ERNEDSCLVR TDVGLWAVAD GMGGHEAGDL ASRIVVQSLD
     AIGTPESAAD LLAECEERLF SANRQILALS HERQGATVGT TAAVLLVRDS YYACIWAGDS
     RVYLISRGAI SQVSHDHSEL EELIAEGALS REDVNDWLSN AITRAVGVAD DPEFEVVTGP
     AEPEDVFVIC SDGLTRHVRD DEILQHAATR RAQAACDDML ALALDRGGLD NVTIVIVRLL
     TPRSQEATRS PLDREPQP
//