ID A0A1Q2M4F0_9GAMM Unreviewed; 331 AA.
AC A0A1Q2M4F0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=Mag101_07665 {ECO:0000313|EMBL:AQQ67530.1};
OS Microbulbifer agarilyticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=260552 {ECO:0000313|EMBL:AQQ67530.1, ECO:0000313|Proteomes:UP000188219};
RN [1] {ECO:0000313|EMBL:AQQ67530.1, ECO:0000313|Proteomes:UP000188219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP101 {ECO:0000313|EMBL:AQQ67530.1,
RC ECO:0000313|Proteomes:UP000188219};
RA Jung J., Bae S.S., Baek K.;
RT "Genome of Microbulbifer agarilyticus GP101.";
RL Submitted (FEB-2017) 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; CP019650; AQQ67530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2M4F0; -.
DR STRING; 260552.Mag101_07665; -.
DR KEGG; maga:Mag101_07665; -.
DR eggNOG; COG0631; Bacteria.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000188219; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000188219};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 307..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 24..263
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 331 AA; 35737 MW; 80FF9DB41D760F29 CRC64;
MSEAKVRERP SGVSQPAVRA TMRSAGATHT GYRRDQNEDA FWGDESRGVW VVADGLGGHQ
AGEIASQTVV EEIQRSSATD RHYEQALRRA HALLAGDENS NTAMGTTAVV VAEDAPYFHI
YWVGDSRAYL WIPPSEAPDG ADQPFPNGTL KQLTVDHSYV QMLVDSGAIN QEEAANHPNR
HVITRCIGGS ANPTLEIDRA SFSWDRGQKL LLCSDGLSND VSPAEICEVL AKNSDNQRAS
DLLIAAALDA GGRDNITVQV ISAPDDQAGD QASKFDANGD PKSQKQNSRT SRSLLGSHKI
FSTRGKLILN ITTLALILSA GIYVTWQLLN T
//
