ID A0A0G3UKM6_9ACTN Unreviewed; 504 AA.
AC A0A0G3UKM6;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=M444_17930 {ECO:0000313|EMBL:AKL66957.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL66957.1, ECO:0000313|Proteomes:UP000035653};
RN [1] {ECO:0000313|EMBL:AKL66957.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL66957.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
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; CP011664; AKL66957.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3UKM6; -.
DR KEGG; strm:M444_17930; -.
DR PATRIC; fig|465541.12.peg.3837; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000035653; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1.
DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR Pfam; PF00481; PP2C; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000035653};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 368..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..252
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 287..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 504 AA; 54078 MW; 749E92B3F355618F CRC64;
MAQDRLYPEP TGEVRMSLSL RFAAGSHKGM IREGNEDSGY AGPRLLAIAD GMGGQAAGEV
ASSEVISTLV QLDDDVPGSD ILTSLATAVQ RANDQLRVMV EEDPQLEGMG TTLTALLWTG
QRLGLVHVGD SRAYLLRDGL LTQITQDHTW VQRLVDEGRI TEEEATTHPQ RSLLMRALGS
GDTVEPDLSI REVRAGDRYL ICSDGLSGVV SHQTLEETLA DYHGPHETVQ ALIQLALRGG
GPDNITCIVA DVLSTDSGDT LAAQLNDTPV VVGAVAENQH QLFDGNAMQT PAGRASGLGR
QASPPAGSFG PPGSGENPGY GFPEQSQGGG YGGGGGYGDP EANSFEGDQR YEDTYDHPRR
RRGKGRKWTT RTLLLLIVAG AIGGGLYGAH RWTQTQYYVG VKGEHVALYR GISQNLGWIH
LNQVETDHPD IELKYLPPFK RKQVEATITE NSLDGARQKI DELGVQVSAC KKDEERRNAE
PQNAQTPSPS LTPAEQALVG LCGK
//