ID A0A1R4F8S7_9ACTO Unreviewed; 448 AA.
AC A0A1R4F8S7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=CZ771_05425 {ECO:0000313|EMBL:SJM52305.1};
OS Actinomycetales bacterium JB111.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales.
OX NCBI_TaxID=1434822 {ECO:0000313|EMBL:SJM52305.1, ECO:0000313|Proteomes:UP000196124};
RN [1] {ECO:0000313|EMBL:SJM52305.1, ECO:0000313|Proteomes:UP000196124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JB111 {ECO:0000313|EMBL:SJM52305.1,
RC ECO:0000313|Proteomes:UP000196124};
RA Peterson S.W.;
RL Submitted (FEB-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};
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DR EMBL; FUHX01000025; SJM52305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R4F8S7; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000196124; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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 Hydrolase {ECO:0000313|EMBL:SJM52305.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000196124};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 310..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..238
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 246..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 47006 MW; 8087CA71A166B46F CRC64;
MAIYTRYAAR SDVGLIRSSN QDSGYAGDHL LVLADGMGGP AGGDIASSVA VAHLAPLDDT
HGADELLGLL RNAIADAHAD LVARSTADPD LAGLGTTCIA LLRTGSKLAM VHIGDSRAYL
LRDGDLTQVT TDHTFVQYLV STGRLTEEEA ERHPQRNMIL RALGDTEGEV ELDESMREIQ
PGDRWLLSSD GLFGVVSKET IQTTLAEHDD PGAAADALVA LSLRAGAPDN VTCVVADFLS
DGGAHHPMSE PQVVGSAAER PTGRQASAPS AGSPDGAAGG SAAQRAAALL ATDDDAETVQ
PRRHKRLIRG LIAGAAALAV LLVGGFTAYR WSQEQYYVAP SGDYVAIYRG IPQNVGPFDL
SSLHERTDLR IDDLTALAQE RLDEPITRGS LEGARDVVET LRDAADRRAD RESSSESASE
SASESASQGE SPTDGESDSE SPSTDEAE
//
