ID   B1I500_DESAP            Unreviewed;       237 AA.
AC   B1I500;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=Daud_1589 {ECO:0000313|EMBL:ACA60091.1};
OS   Desulforudis audaxviator (strain MP104C).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforudis.
OX   NCBI_TaxID=477974 {ECO:0000313|EMBL:ACA60091.1, ECO:0000313|Proteomes:UP000008544};
RN   [1] {ECO:0000313|Proteomes:UP000008544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP104C {ECO:0000313|Proteomes:UP000008544};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA   Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT   "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACA60091.1, ECO:0000313|Proteomes:UP000008544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP104C {ECO:0000313|EMBL:ACA60091.1,
RC   ECO:0000313|Proteomes:UP000008544};
RX   PubMed=18845759; DOI=10.1126/science.1155495;
RA   Chivian D., Brodie E.L., Alm E.J., Culley D.E., Dehal P.S., Desantis T.Z.,
RA   Gihring T.M., Lapidus A., Lin L.H., Lowry S.R., Moser D.P.,
RA   Richardson P.M., Southam G., Wanger G., Pratt L.M., Andersen G.L.,
RA   Hazen T.C., Brockman F.J., Arkin A.P., Onstott T.C.;
RT   "Environmental genomics reveals a single-species ecosystem deep within
RT   Earth.";
RL   Science 322:275-278(2008).
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; CP000860; ACA60091.1; -; Genomic_DNA.
DR   RefSeq; WP_012302672.1; NC_010424.1.
DR   AlphaFoldDB; B1I500; -.
DR   STRING; 477974.Daud_1589; -.
DR   KEGG; dau:Daud_1589; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_4_1_9; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000008544; 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   Reference proteome {ECO:0000313|Proteomes:UP000008544}.
FT   DOMAIN          2..237
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   237 AA;  25546 MW;  C0C29E468685A562 CRC64;
     MRWSAVTDTG LVRPNNEDNH RVNEALGLFA VADGMGGHQA GEVASRLALT VLEEQFQELV
     QQGEETGNAL LYAVEAANRQ VFEESCRSNR CNGMGTTLSA CLIAEEGLIL AHVGDSRVYL
     VRAGEIFQLT EDHSVVQELL NEGRITAEEV PGHPYRNVLS RALGTGEQLE IDLLRVPLQA
     GDRVLLCTDG LTNMVSDAAI QAVVAGYGDP DQAVRELVRL ALEQGGSDNI TLILVVL
//