ID A0A4R6KQS2_9ACTN Unreviewed; 466 AA.
AC A0A4R6KQS2;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=EV643_101745 {ECO:0000313|EMBL:TDO54952.1};
OS Kribbella sp. VKM Ac-2527.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Kribbellaceae; Kribbella.
OX NCBI_TaxID=2512215 {ECO:0000313|EMBL:TDO54952.1, ECO:0000313|Proteomes:UP000295388};
RN [1] {ECO:0000313|EMBL:TDO54952.1, ECO:0000313|Proteomes:UP000295388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-2527 {ECO:0000313|EMBL:TDO54952.1,
RC ECO:0000313|Proteomes:UP000295388};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (MAR-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};
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:TDO54952.1}.
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DR EMBL; SNWQ01000001; TDO54952.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R6KQS2; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000295388; 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:UP000295388};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..236
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 405..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..440
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 466 AA; 49350 MW; 402E816D3ED700AB CRC64;
MTLSLDYAAL SDIGKRHNNE DSAYAGPHLL LLADGMGGAA AGEVASAAAV QVIRRLDKPG
ISGEDMIEAL AGAVHRANER LSELVEEDPE REGMGSTVTA LMFDGVQLGL AHLGDSRAYR
MRGGQLQQLS HDHTFVQSLV DEGRISAEEA FTHPHRNLIL RVLDGRPDSD PDLEILDVQA
GDRLMLCSDG LPDYVSDRQI AASMSDGTPD SVVVELITHA LEAQSNDNIT CVVADVVETE
PVSGTAPQLV GAAAELAQGG TGRGDPTVVV RRGDGDDRLG GAAGHLDPEE LRYAPRAPKR
FLWLRRLAVL IVALALIGGG GWLAYGWTQK QYYVGTDGDY VAIFKGVDDE IPGLTLSNMY
EKQTLQVDKL PTYSREQVEG NIQADDLAAA REIVSELQRT AAECAAKAAK QTPKPTPAPT
TPTASGKPPV STPPKTPITT PVSTPASTPS STPDGTVNPD DCDGVR
//
