ID A0A1S2JYB0_9ACTN Unreviewed; 510 AA.
AC A0A1S2JYB0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-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=BJP40_07635 {ECO:0000313|EMBL:OII60742.1};
OS Streptomyces sp. CC53.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1906740 {ECO:0000313|EMBL:OII60742.1, ECO:0000313|Proteomes:UP000179639};
RN [1] {ECO:0000313|EMBL:OII60742.1, ECO:0000313|Proteomes:UP000179639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC53 {ECO:0000313|EMBL:OII60742.1,
RC ECO:0000313|Proteomes:UP000179639};
RA Cruz-Morales P., Ramos-Aboites H.E., Barona-Gomez F.;
RT "Functional and evolutionary genomics of ferrioxamines biosynthesis and
RT transport.";
RL Submitted (OCT-2016) 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:OII60742.1}.
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DR EMBL; MKXB01000194; OII60742.1; -; Genomic_DNA.
DR RefSeq; WP_071282521.1; NZ_MKXB01000194.1.
DR AlphaFoldDB; A0A1S2JYB0; -.
DR STRING; 1906740.BJP40_07635; -.
DR Proteomes; UP000179639; 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; PF00481; PP2C; 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:UP000179639};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 336..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..237
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 269..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 438..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 510 AA; 53854 MW; 13D2B7F31AD67C78 CRC64;
MSLSLRFAAG SHKGMIREGN EDSGYAGPRL LAIADGMGGQ AAGEVASSEV ISTLVTLDDD
IPGSDILTSL GTAVQRANDQ LRMMVEEDPQ LEGMGTTLTA LLWTGQRLGL VHVGDSRAYL
LRDGVLTQIT QDHTWVQRLV DEGRITEEEA TTHPQRSLLM RALGSGDHVE PDLSIREVRA
GDRYLVCSDG LSGVVSHQTL EETLASYQGP QETVQELIQL ALRGGGPDNI TVIIADVLDV
DGGDTLAGQL HDAPVVVGAV AENQQQLNDG GAMQTPAGRA SGLGRPAPQT PAGGFGPPGS
GQDIDYSGMP PEGGRRAYRD EDLAKPRRKG GWFKRIFLMV LVLGLLGAGG YAGWRWTQTQ
YYVGANNGHV ALYRGISQKL AWISLSEVEK DHPDIELKYL PTYYQQQVEE TIAGGNLARA
EAKIRELGVQ ASACRKSEQA REAAERSAAS APAASASPSP STSASPATGE QPDGTSDAKP
GAATTTTPTP APGPTLTEEE KRAASNCGKQ
//
