ID A0A542XGA0_9MICO Unreviewed; 437 AA.
AC A0A542XGA0;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-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=FB554_3021 {ECO:0000313|EMBL:TQL34840.1};
OS Barrientosiimonas humi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Barrientosiimonas.
OX NCBI_TaxID=999931 {ECO:0000313|EMBL:TQL34840.1, ECO:0000313|Proteomes:UP000318336};
RN [1] {ECO:0000313|EMBL:TQL34840.1, ECO:0000313|Proteomes:UP000318336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24617 {ECO:0000313|EMBL:TQL34840.1,
RC ECO:0000313|Proteomes:UP000318336};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUN-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:TQL34840.1}.
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DR EMBL; VFOK01000001; TQL34840.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A542XGA0; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000318336; 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:UP000318336};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 326..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..239
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 262..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 45635 MW; 0EF78FA081367753 CRC64;
MPIALRYAAR TDLGLGSKSR NEDSAYAGPD LLILADGMGG HAAGDVASST VVGELVALDG
VGLGADDAQE QLRAAVLRAN AHLREAMDAS DDLEGMGTTC IALLRTGTKL VVANIGDSRA
FMLRDGTMTQ ITKDHSFVQA LLDDGRITEE EAEHHPQRNM VTRVLTGRED DEPDLSLREG
KIGDRYLLCS DGLSDYVAAS TIKDILANGG TPDETADKLI AIALRASTRD NVTVVVADVV
DQANASSNQP QVVGAAAALG ATHDPDATQP QPQTPAEKAA ALRREANQPP PPQGPPDAPA
GGATPAPGSG PLLAEEGPGS RSSTRFRWAF LAGLIAVVLA VAAFVGHRWS QQQFYVGQQN
GVVTIFRGVP QDFGPLSLND VDTRTDIAVA DLPPFYRQKV GDTLSASGKT AAIRIVENLR
AEMVKCQTGT GGSGCTS
//
