ID A0A257AZS5_9BACT Unreviewed; 453 AA.
AC A0A257AZS5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=CFK52_11265 {ECO:0000313|EMBL:OYT70386.1};
OS Chloracidobacterium sp. CP2_5A.
OC Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX NCBI_TaxID=2012633 {ECO:0000313|EMBL:OYT70386.1, ECO:0000313|Proteomes:UP000216393};
RN [1] {ECO:0000313|EMBL:OYT70386.1, ECO:0000313|Proteomes:UP000216393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP2_5A {ECO:0000313|EMBL:OYT70386.1};
RA Ward L.M., Mcglynn S.E., Fischer W.;
RT "Draft genome of Chloracdibacterium sp. CP2_5A, a phototrophic
RT Acidobacteria from a Japanese hot spring.";
RL Submitted (JUN-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:OYT70386.1}.
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DR EMBL; NKPT01000038; OYT70386.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257AZS5; -.
DR Proteomes; UP000216393; 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 404..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..280
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 288..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 453 AA; 48396 MW; 72CC783EA4951B99 CRC64;
MTTATTANGV RRIEVYALTD VGVVRPHNED NFLIVNLSDG QSWTAENQLP EHPLLVELRP
PDRGVLLAVS DGMGGALAGE VASHLAVTQV CDSMMRLQKD AEFKRFGFHE HLRFAIERAN
LFINSQSQRS PEYAGMGATF TGAGLDGTML YLAQVGDSRA YLFRQDLVVQ VTTDQSLVEQ
LIQSGHITRE EAETHPYKNV ILQALGATPN VTVTVDGLPV CRGDILLLCS DGLSGKINGE
DMRAILDATN GNLRLACQRM VDLANERGGE DNITVMILRF TGDGFPERGE VDGYDRITPI
DRDDDLPYPT EDKLGLGNEP TQDEADSSPT MELASESGSV QEPTPAELAI TGGLGLTRQF
SVVAASPAPK ADAAASNGAA PAAVVLPPAP APVAENAADD GLRMYRLVAA SALVILSVCA
LVWTLINWGK DGGRPDGSDP PRNQTRQVAP RSS
//
