ID A0A1Y4BR14_9ACTN Unreviewed; 425 AA.
AC A0A1Y4BR14;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=B5F84_08565 {ECO:0000313|EMBL:OUO33491.1};
OS Olsenella sp. An290.
OC Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales; Atopobiaceae;
OC Olsenella.
OX NCBI_TaxID=1965625 {ECO:0000313|EMBL:OUO33491.1, ECO:0000313|Proteomes:UP000196134};
RN [1] {ECO:0000313|Proteomes:UP000196134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An290 {ECO:0000313|Proteomes:UP000196134};
RA Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA Rychlik I.;
RT "Function of individual gut microbiota members based on whole genome
RT sequencing of pure cultures obtained from chicken caecum.";
RL Submitted (APR-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:OUO33491.1}.
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DR EMBL; NFIU01000019; OUO33491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y4BR14; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000196134; 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 NCBIfam; NF033484; Stp1_PP2C_phos; 1.
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:UP000196134};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 290..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 42..270
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 425 AA; 43921 MW; 19485900E4ECD286 CRC64;
MTPEETLPTV APEPTNAPGR SEVPVEVREG ADVIAGSNEF VSWGAYSDVG LVRGHNEDSF
LIQAPLFVVS DGMGGHAAGE VASSIAIETI GQRAPGSADD VLLGAAVEAA NQAVIAGAEA
GVGKPGMGCT ASAVLIEKDR MAVAHVGDSR VYVLHHGTLV RITHDHSYVE ELVDAGQITA
DEARTHPSRS IITRALGSDP DMYADHFSLE VNSGDRVILC SDGLSSMVPD SEIEALAVSS
ATPRQAAGSL VAAALTAGGA DNVTVVVVDV LNDGLADEAR RQLTGLAARI GGALAIVLAV
VAFIAVAFIR SEWYLGTTGD VVGIYRGIKG DFLGVPLSEL VSTSAVEVSD LPTSLQDQLE
QGIRVQNEQA AQETIDSYHT QIDEARSEGA RTADEVRAGT DPDQRDGAAT TVAPDPDPTT
QNGGE
//
