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Database: UniProt
Entry: A0A0R1XES5_9LACO
LinkDB: A0A0R1XES5_9LACO
Original site: A0A0R1XES5_9LACO 
ID   A0A0R1XES5_9LACO        Unreviewed;       250 AA.
AC   A0A0R1XES5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   ORFNames=FC91_GL002778 {ECO:0000313|EMBL:KRM26996.1};
OS   Schleiferilactobacillus harbinensis DSM 16991.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Schleiferilactobacillus.
OX   NCBI_TaxID=1122147 {ECO:0000313|EMBL:KRM26996.1, ECO:0000313|Proteomes:UP000050949};
RN   [1] {ECO:0000313|EMBL:KRM26996.1, ECO:0000313|Proteomes:UP000050949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16991 {ECO:0000313|EMBL:KRM26996.1,
RC   ECO:0000313|Proteomes:UP000050949};
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:KRM26996.1}.
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DR   EMBL; AZFW01000058; KRM26996.1; -; Genomic_DNA.
DR   RefSeq; WP_027828664.1; NZ_AZFW01000058.1.
DR   AlphaFoldDB; A0A0R1XES5; -.
DR   GeneID; 78509299; -.
DR   PATRIC; fig|1122147.4.peg.2864; -.
DR   eggNOG; COG0631; Bacteria.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000050949; 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:UP000050949}.
FT   DOMAIN          2..241
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   250 AA;  27297 MW;  38D2F53497E75A7E CRC64;
     MEYAYQSDVG RRREDNQDFA GVFKNEAGAL FAVVADGMGG HQGGDVASEM AVSHLGHDFS
     QTDMHSVEDA VKWLIYDLQR ENDKILAVSD HYADLRGMGT TFVAVIVVGH QYIVANIGDS
     RCYRYSHGKL EQLTEDHSLV NELLKHGEIS PEEAKHHPQK NVITRTLGVS SDADADVTIF
     DFGPDDYLLL CSDGLTNMVS TDEIKEALAG PGTLDDKCAQ LIGWANDAGG LDNITVLILH
     RQGGVRHDGK
//
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