ID A0A2A9DML5_9CORY Unreviewed; 453 AA.
AC A0A2A9DML5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=ATK06_0678 {ECO:0000313|EMBL:PFG27606.1};
OS Corynebacterium renale.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1724 {ECO:0000313|EMBL:PFG27606.1, ECO:0000313|Proteomes:UP000221653};
RN [1] {ECO:0000313|EMBL:PFG27606.1, ECO:0000313|Proteomes:UP000221653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20688 {ECO:0000313|EMBL:PFG27606.1,
RC ECO:0000313|Proteomes:UP000221653};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFG27606.1}.
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DR EMBL; PDJF01000001; PFG27606.1; -; Genomic_DNA.
DR RefSeq; WP_048378658.1; NZ_PDJF01000001.1.
DR AlphaFoldDB; A0A2A9DML5; -.
DR STRING; 1724.GCA_001044175_00048; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000221653; Unassembled WGS sequence.
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:UP000221653};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 304..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..235
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 242..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 47995 MW; 22AD36984B490998 CRC64;
MALRFDYTTA SDQGLVRGNN EDSAYAGPNL LALADGMGGH AAGEVASQLM ITHLEVLDAD
PGDNDMLALL GAAADDANAS IAAAVTDHPE REGMGTTLTA IMFNGKHLAI CHVGDSRGYR
LRDGKLEQIT VDDTYVQSLV ESGQLDPQDV STHPKRSLIL KAYTGMPVEP GLWTLDAQPG
DRLLLCSDGL SDPVTHETIE STLAGGTPEE AAQRLIALAL RSGGPDNITV VIADVVEDSA
PHRELPTKPA TSGALLGEQE STHPDTAAGR AAALRRQPQV IPPAPTEEDV PDDSDEEGET
GSKAWKWVGI ISLLVVLIAA IGGGWWAYTA GQDRYYVDVD TQDRIVVERG FDFSAFGRDL
HSTYQYACIG KDGSLRMVES DAESCQYFSV KDVPPAVRGS ITATPAGSYE DATAHLRTLA
DEALPVCVTR EKAGADSGSK DLSDPGVNCR EVK
//
