ID A0A518BA87_9BACT Unreviewed; 451 AA.
AC A0A518BA87;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN Name=stp_4 {ECO:0000313|EMBL:QDU63894.1};
GN ORFNames=Pan216_47750 {ECO:0000313|EMBL:QDU63894.1};
OS Planctomycetes bacterium Pan216.
OC Bacteria; Planctomycetota.
OX NCBI_TaxID=2527975 {ECO:0000313|EMBL:QDU63894.1, ECO:0000313|Proteomes:UP000317093};
RN [1] {ECO:0000313|EMBL:QDU63894.1, ECO:0000313|Proteomes:UP000317093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pan216 {ECO:0000313|EMBL:QDU63894.1,
RC ECO:0000313|Proteomes:UP000317093};
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; CP036279; QDU63894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A518BA87; -.
DR Proteomes; UP000317093; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:QDU63894.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000317093};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 282..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 309..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..263
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 432..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 49979 MW; 70AF03586D10B3CA CRC64;
MSTKQREVAP HAPLRRARSK ISHWCLTDVG VRRSHNQDSF GVTLAPNEES WLSRGHLYVV
ADGMGAHAVG ELASKMAADV LQHAYTKSRI GSPKEALKAS IEEANRSIRE KARQNPDFKG
MGTTITALVL LPEGAIIGHV GDSRCYRVRA GKMEQITQDH SVHWETARKR GVDPDEVKDV
PKNVLSRSLG NEDDIQVDVD GPYEVANGDR FLICSDGLSG HLTDVELGAI NAELPPGEAA
PLMIEMSNMR GGVDNITLIL VEIGEAAVTP PPKRSLIFWR GWGGPALTVL LGIISFPIAY
LLHDLAIGGA LYVGLAGVIL FVAGMSWLLA VSEKKEKKED KEVELPPPIH RVTNSTVDDA
LTSHLHDTVN RISRKVRESQ WPTEWDAFEE HCQRADESYR SGDLHEAFRE YCRSLAVLGR
AVKQHRHKQE VFDPNWETKR RPSPVKQDGH R
//
