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Database: UniProt
Entry: A0A0R2FMB5_9LACO
LinkDB: A0A0R2FMB5_9LACO
Original site: A0A0R2FMB5_9LACO 
ID   A0A0R2FMB5_9LACO        Unreviewed;       249 AA.
AC   A0A0R2FMB5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   ORFNames=IV38_GL000535 {ECO:0000313|EMBL:KRN29648.1}, IV40_GL000133
GN   {ECO:0000313|EMBL:KRN33823.1};
OS   Lactobacillus selangorensis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=81857 {ECO:0000313|EMBL:KRN29648.1, ECO:0000313|Proteomes:UP000051751};
RN   [1] {ECO:0000313|Proteomes:UP000051645, ECO:0000313|Proteomes:UP000051751}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-66 {ECO:0000313|EMBL:KRN29648.1,
RC   ECO:0000313|Proteomes:UP000051751}, and DSM 13344
RC   {ECO:0000313|EMBL:KRN33823.1, ECO:0000313|Proteomes:UP000051645};
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:KRN29648.1}.
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DR   EMBL; JQAT01000001; KRN29648.1; -; Genomic_DNA.
DR   EMBL; JQAZ01000001; KRN33823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2FMB5; -.
DR   STRING; 81857.IV38_GL000535; -.
DR   PATRIC; fig|81857.3.peg.540; -.
DR   Proteomes; UP000051645; Unassembled WGS sequence.
DR   Proteomes; UP000051751; 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:UP000051645}.
FT   DOMAIN          3..242
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   249 AA;  27427 MW;  ABE1E9E90C7ECE48 CRC64;
     MIEIAYQTDV GQKRESNQDY VGTFLNKGGA RFAIVADGMG GHRGGDVASE MAVSHIGYHF
     EQTTSTDVEE LIKWLVVELQ NENQQIIDAS EEYADLMGMG TTMVAVILVD HKFVVANIGD
     SRAYLYRSDR LKQLTEDHSL VNELVKQGEI SPEDARNHPQ KNIITRSLGI STDVDADVTI
     YELAENDLLL LCTDGLTNMM TDRQIAMILA SPEDITEKCK ALVKVANQAG GLDNITALLI
     HETQQAVND
//
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