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Database: UniProt
Entry: A0A0R2IRB9_9LACO
LinkDB: A0A0R2IRB9_9LACO
Original site: A0A0R2IRB9_9LACO 
ID   A0A0R2IRB9_9LACO        Unreviewed;       247 AA.
AC   A0A0R2IRB9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   ORFNames=IV80_GL000224 {ECO:0000313|EMBL:KRN67681.1};
OS   Pediococcus cellicola.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=319652 {ECO:0000313|EMBL:KRN67681.1, ECO:0000313|Proteomes:UP000051568};
RN   [1] {ECO:0000313|EMBL:KRN67681.1, ECO:0000313|Proteomes:UP000051568}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17757 {ECO:0000313|EMBL:KRN67681.1,
RC   ECO:0000313|Proteomes:UP000051568};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRN67681.1}.
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DR   EMBL; JQBR01000001; KRN67681.1; -; Genomic_DNA.
DR   RefSeq; WP_057748255.1; NZ_JQBR01000001.1.
DR   AlphaFoldDB; A0A0R2IRB9; -.
DR   STRING; 319652.IV80_GL000224; -.
DR   PATRIC; fig|319652.3.peg.226; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000051568; Unassembled WGS sequence.
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:UP000051568}.
FT   DOMAIN          2..241
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   247 AA;  27573 MW;  4915CE629B097D42 CRC64;
     MKYAFQSDIG NHRDENQDYV GVFKNKKDVL FSIVADGIGG RQGGDVASEM AVSHLGYLFQ
     NTDFTDALNA IKWLQTEVTQ ENDEILETSQ KYSDLNGMGT TIVVTIILRN QFIVAHLGDS
     RCYLFKKNEL KQLTSDHSLV NELIKQGQLS PEEARNHPQK NIITKTLGIS TNSDIDVHTY
     VWKKQDQILL CTDGLTNMVS DQTIANVLAS SVSLEEKCLK LIEFANQAGG RDNVTVLIMQ
     ADDEVNE
//
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