ID A0A4V3HFL1_9BACT Unreviewed; 370 AA.
AC A0A4V3HFL1;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 9.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=C8D99_1295 {ECO:0000313|EMBL:TDY53839.1};
OS Aminivibrio pyruvatiphilus.
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Aminivibrio.
OX NCBI_TaxID=1005740 {ECO:0000313|EMBL:TDY53839.1, ECO:0000313|Proteomes:UP000295066};
RN [1] {ECO:0000313|EMBL:TDY53839.1, ECO:0000313|Proteomes:UP000295066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25964 {ECO:0000313|EMBL:TDY53839.1,
RC ECO:0000313|Proteomes:UP000295066};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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:TDY53839.1}.
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DR EMBL; SORI01000029; TDY53839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V3HFL1; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000295066; 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:UP000295066};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 273..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..251
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 370 AA; 39793 MW; CE0E7F7B8EBA7999 CRC64;
MIVFPGNAQH IGTRSEQQDA FGISEIGDSE FLSHGGVLAV VADGMGGLAE GGKASRLAIK
TFLEAYLKKT AGEPIGDALE RSMIETNDAV YSLAVELGEK GNFGTTLIAA VVHESGMYWI
YAGDSRIYLT DGQALTRLTE DHVYGRKLKK AAEKGLIEYD MVLSHPARES LTSYIGDQSV
NEIGKGFHSA PLPENFSLLL CTDGLFKFLP EKRIIECYSD DPREWTQKLV DAVLEEQNPS
QDNITAVCLK IGEPQIRTRE VKVAPSKKRR TKLIGAVLLL GFAMAACLGI YWKVSRSDSP
AVLDQDAASQ TVVSGDVLPD AGHQADGNGN LSGIMTSGDI PASKDIILAV PVKEDGGKKI
EAVPKKGKKK
//
