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Database: UniProt
Entry: A0A518BLJ3_9BACT
LinkDB: A0A518BLJ3_9BACT
Original site: A0A518BLJ3_9BACT 
ID   A0A518BLJ3_9BACT        Unreviewed;       280 AA.
AC   A0A518BLJ3;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   Name=stp {ECO:0000313|EMBL:QDU67850.1};
GN   ORFNames=Pla133_29390 {ECO:0000313|EMBL:QDU67850.1};
OS   Planctomycetes bacterium Pla133.
OC   Bacteria; Planctomycetota.
OX   NCBI_TaxID=2528011 {ECO:0000313|EMBL:QDU67850.1, ECO:0000313|Proteomes:UP000316921};
RN   [1] {ECO:0000313|EMBL:QDU67850.1, ECO:0000313|Proteomes:UP000316921}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pla133 {ECO:0000313|EMBL:QDU67850.1,
RC   ECO:0000313|Proteomes:UP000316921};
RA   Wiegand S., Jogler M., Boedeker C., Pinto D., Vollmers J., Rivas-Marin E.,
RA   Kohn T., Peeters S.H., Heuer A., Rast P., Oberbeckmann S., Bunk B.,
RA   Jeske O., Meyerdierks A., Storesund J.E., Kallscheuer N., Luecker S.,
RA   Lage O.M., Pohl T., Merkel B.J., Hornburger P., Mueller R.-W., Bruemmer F.,
RA   Labrenz M., Spormann A.M., Op den Camp H., Overmann J., Amann R.,
RA   Jetten M.S.M., Mascher T., Medema M.H., Devos D.P., Kaster A.-K.,
RA   Ovreas L., Rohde M., Galperin M.Y., Jogler C.;
RT   "Deep-cultivation of Planctomycetes and their phenomic and genomic
RT   characterization uncovers novel biology.";
RL   Submitted (FEB-2019) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; CP036287; QDU67850.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A518BLJ3; -.
DR   Proteomes; UP000316921; 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   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:QDU67850.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000316921}.
FT   DOMAIN          1..245
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   280 AA;  29444 MW;  2722E728762206D9 CRC64;
     MLAWRPRPID DGSPAPEEEN EDAALVHNDG RRTVVAVADG AGGHIGGAQA SRLAIEVLAD
     ALQRSDDSTD LRPFILDAFE RANVGIRTLD VNAGSTLAVA EFDGSRLRTY HAGDSEVLVV
     GQRGRQLYRT VSHGPTAYAV EAGVLHPDDA LHHDERHVIS SALGFDELRI ELGRFERLPD
     RATVVVSSDG LTDNLTTDEI IAIVRRGPLL GAARKLVELA ASRMADAAGE GPSKPDDLSL
     ILYRPRADRE TLAAAIDSAA LTTPPSPGGS AGGARSGSAG
//
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