ID A0A238V2C2_9PSEU Unreviewed; 435 AA.
AC A0A238V2C2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=SAMN06265360_101174 {ECO:0000313|EMBL:SNR28157.1};
OS Haloechinothrix alba.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Haloechinothrix.
OX NCBI_TaxID=664784 {ECO:0000313|EMBL:SNR28157.1, ECO:0000313|Proteomes:UP000198348};
RN [1] {ECO:0000313|EMBL:SNR28157.1, ECO:0000313|Proteomes:UP000198348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45207 {ECO:0000313|EMBL:SNR28157.1,
RC ECO:0000313|Proteomes:UP000198348};
RA Kim H.J., Triplett B.A.;
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};
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DR EMBL; FZNW01000001; SNR28157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238V2C2; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000198348; 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 Reference proteome {ECO:0000313|Proteomes:UP000198348};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..235
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 247..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 45918 MW; 6E61C661453EEA44 CRC64;
MTLVLRYAAR SDRGLVRSNN QDSVYAGPRL LALADGMGGH AAGEVASKVV IAALAPLDDD
EPGDDLLTQL RDSVLSGNRA IAELVESDPE LEGMGTTLTA ILFSGSRLGL VHIGDSRAYL
YRSGQFSQIT HDDTFVQQLQ DEGRITEEEA ENHPQRALLL KALTGQDAEP NLTVREARAG
DRYLLCSDGL SGMVSHETLT EAITIGDPQD CADRMIELAL KGGGTDNITV IVADVVDVDF
GDDAPIVGGA AGDGSDAGPQ GDSPAARAQA LTAPAPSREP PDATESGGDE PDTGTSRWRK
GITFTALFGL GLVLLAAIAL ATRYFVMQQY YVGVDDNNEV TIYQGVTGSI FGLELSSRSE
GSCAPNNALC DPLFLADLQY GARGDVCRGV QQDDLADARD FIATLRAEFL LEDAPDASTR
GEVSCAHDEA RGGDR
//
