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Database: UniProt
Entry: A0A0R1W8K0_9LACO
LinkDB: A0A0R1W8K0_9LACO
Original site: A0A0R1W8K0_9LACO 
ID   A0A0R1W8K0_9LACO        Unreviewed;       255 AA.
AC   A0A0R1W8K0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   ORFNames=FC15_GL000984 {ECO:0000313|EMBL:KRM13813.1};
OS   Lapidilactobacillus concavus DSM 17758.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lapidilactobacillus.
OX   NCBI_TaxID=1423735 {ECO:0000313|EMBL:KRM13813.1, ECO:0000313|Proteomes:UP000051315};
RN   [1] {ECO:0000313|EMBL:KRM13813.1, ECO:0000313|Proteomes:UP000051315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17758 {ECO:0000313|EMBL:KRM13813.1,
RC   ECO:0000313|Proteomes:UP000051315};
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:KRM13813.1}.
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DR   EMBL; AZFX01000003; KRM13813.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R1W8K0; -.
DR   STRING; 1423735.FC15_GL000984; -.
DR   PATRIC; fig|1423735.3.peg.1023; -.
DR   Proteomes; UP000051315; 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:UP000051315}.
FT   DOMAIN          5..245
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   255 AA;  28230 MW;  59B5365BF36413B1 CRC64;
     MQKMDIVYLT DIGKRRANNQ DFVAAFKNQA DVIFAVVADG MGGHLGGDVA SEMAVSQIGH
     DFTQTDISTV FDLKDWLLKE LTNENNRIIE VSSKFSDLTG MGTTFVALMI SGNRYVITNI
     GDSRGYLLRH GELHQITEDH SLVNELVKYG KISPEEARSH PQKNVITRTL GVSKDVQPDS
     NNDVWHQDDL FLLCSDGLTN MVTDEVIREI LVTENVSLKE RAQRLIVQAN ANGGRDNISV
     LLLQPGAQST EGQDQ
//
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