ID   A6T201_JANMA            Unreviewed;       273 AA.
AC   A6T201;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=pppL {ECO:0000313|EMBL:ABR89851.1};
GN   OrderedLocusNames=mma_2858 {ECO:0000313|EMBL:ABR89851.1};
OS   Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=375286 {ECO:0000313|EMBL:ABR89851.1, ECO:0000313|Proteomes:UP000006388};
RN   [1] {ECO:0000313|EMBL:ABR89851.1, ECO:0000313|Proteomes:UP000006388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marseille {ECO:0000313|EMBL:ABR89851.1,
RC   ECO:0000313|Proteomes:UP000006388};
RX   PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA   Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA   Drancourt M.;
RT   "Genome analysis of Minibacterium massiliensis highlights the convergent
RT   evolution of water-living bacteria.";
RL   PLoS Genet. 3:1454-1463(2007).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000269; ABR89851.1; -; Genomic_DNA.
DR   RefSeq; WP_012080707.1; NC_009659.1.
DR   AlphaFoldDB; A6T201; -.
DR   STRING; 375286.mma_2858; -.
DR   KEGG; mms:mma_2858; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_4_1_4; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000006388; Chromosome.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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   Hydrolase {ECO:0000313|EMBL:ABR89851.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006388}.
FT   DOMAIN          8..253
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   273 AA;  29585 MW;  F8305C8F282C4CAB CRC64;
     MTYSVELQFA AKTDTGLVRA HNEDAIEVSA DYKAVVLADG MGGYNAGEIA SGIATTVFRA
     ALEQQLQQLQ DKGRIASGKS LQRLMVDAVA AANEQILEVA RIQPQYSGMG TTLVAALFHH
     DRIVVAHIGD SRAYRFRAGR LEQITRDHSQ LQEQIDAGLV SPEWARFAPN KNLITRALGV
     AAQIDVEIND YQTEGGDIYL LCSDGLSDML AGEQMSAMLA DNDTDLELLC GSLVQAANDN
     GGRDNISVIL VKVEASMPVP QSWWQRMTAG FKS
//