ID A0A2U1ZW03_9MICO Unreviewed; 451 AA.
AC A0A2U1ZW03;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=C8046_11340 {ECO:0000313|EMBL:PWD51151.1};
OS Serinibacter arcticus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Beutenbergiaceae;
OC Serinibacter.
OX NCBI_TaxID=1655435 {ECO:0000313|EMBL:PWD51151.1, ECO:0000313|Proteomes:UP000245166};
RN [1] {ECO:0000313|EMBL:PWD51151.1, ECO:0000313|Proteomes:UP000245166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCH200 {ECO:0000313|EMBL:PWD51151.1,
RC ECO:0000313|Proteomes:UP000245166};
RA Thakur V., Kumar V., Singh D.;
RT "Genome assembly of novel Miniimonas species PCH200.";
RL Submitted (MAR-2018) 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:PWD51151.1}.
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DR EMBL; PYHR01000002; PWD51151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1ZW03; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000245166; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 308..329
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..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 46889 MW; 82F86CD4D8EE1DCB CRC64;
MTLAFRYAAR SDVGLIRSSN QDSGYAGPHL LVLADGMGGP AGGDIASSIA IAHLAPLDGE
SHAGDMLTLL RDAVVEAHTE LRTRALDNPD LAGLGTTLIA ALRSGRKLAM IHIGDSRAYL
VRDGQVSRLT TDHTYVQHLV DQGQLDPEEA ENHPHRSVIL RVLGDHDLGV DLDESVRELH
AGERFLLCSD GVSSFVSHDT IVETLTSVTD AGECADRLVD LALRAGGPDN ITAVIADVVE
LDTLPDGAAP DTTPQVVGSA AAHWKKPTRG GSGAAARAAA LTSAAGDGEA EDGDDAAAPK
RKKRRTGAII TVLALLLALV AAGVSGYRWT QTQHYVAASG EFVAIYRGIP QNLGPLHLST
AVETTDLRVD DLPPFAQDRL AQNITPESGS LQDAEELVTS LRAQSTAASD DETDATDPTD
PATPTTSPTD PASTSTTPST TPPATGTTAT P
//
