ID   Q8G517_BIFLO            Unreviewed;       310 AA.
AC   Q8G517;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=ppp {ECO:0000313|EMBL:AAN25008.1};
GN   OrderedLocusNames=BL1202 {ECO:0000313|EMBL:AAN25008.1};
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN25008.1, ECO:0000313|Proteomes:UP000000439};
RN   [1] {ECO:0000313|EMBL:AAN25008.1, ECO:0000313|Proteomes:UP000000439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(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; AE014295; AAN25008.1; -; Genomic_DNA.
DR   RefSeq; NP_696372.1; NC_004307.2.
DR   RefSeq; WP_007056411.1; NC_004307.2.
DR   AlphaFoldDB; Q8G517; -.
DR   STRING; 206672.BL1202; -.
DR   EnsemblBacteria; AAN25008; AAN25008; BL1202.
DR   GeneID; 69577650; -.
DR   KEGG; blo:BL1202; -.
DR   PATRIC; fig|206672.9.peg.916; -.
DR   HOGENOM; CLU_034545_0_0_11; -.
DR   OrthoDB; 9801841at2; -.
DR   PhylomeDB; Q8G517; -.
DR   Proteomes; UP000000439; Chromosome.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
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   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:UP000000439}.
FT   DOMAIN          7..272
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   310 AA;  32732 MW;  0BBE11CFD4C4D30F CRC64;
     MTTGSIRIAM TSDVGLRRKN NQDTGFAQQG VFMVCDGMGG GKGGEQASQL AAQHFAQLAA
     MPSRTRQDID DTLARAQHDI LDLGDRLGGV AGTTCSGLVL PQDHADSASA RSAALFSDAD
     DQDFSDQTYV VNVGDSRTYH LSPLAHADAP ATDIIPVWDA ASLTRITRDH SQRQEAIDSG
     QMLPEEAEAT IPRNIITQCL GDPDGIMPDV YVADLTGRFI ICSDGLHGEV PDEQIAAIAA
     AHSSPQEAVD ALVAAALDAG GTDNITVIVA DMPLTEPEHH AFSAFRLDEG EDIGAIEDAT
     LQTLRTIRSA
//