ID A0A328VF90_9CHLR Unreviewed; 763 AA.
AC A0A328VF90;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=A4R35_08485 {ECO:0000313|EMBL:RAQ95569.1};
OS Thermogemmatispora tikiterensis.
OC Bacteria; Chloroflexota; Ktedonobacteria; Thermogemmatisporales;
OC Thermogemmatisporaceae; Thermogemmatispora.
OX NCBI_TaxID=1825093 {ECO:0000313|EMBL:RAQ95569.1, ECO:0000313|Proteomes:UP000248706};
RN [1] {ECO:0000313|EMBL:RAQ95569.1, ECO:0000313|Proteomes:UP000248706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T81 {ECO:0000313|EMBL:RAQ95569.1,
RC ECO:0000313|Proteomes:UP000248706};
RA Tomazini A., Lal S., Stott M., Henrissat B., Polikarpov I., Sparling R.,
RA Levin D.B.;
RT "Analysis of Carbohydrate Active Enzymes in Thermogemmatispora T81 Reveals
RT Carbohydrate Degradation Ability.";
RL Submitted (AUG-2016) 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:RAQ95569.1}.
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DR EMBL; MCIF01000002; RAQ95569.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A328VF90; -.
DR Proteomes; UP000248706; 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 NCBIfam; NF033484; Stp1_PP2C_phos; 1.
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:UP000248706};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 307..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..224
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 763 AA; 80152 MW; C7722893BF6736B2 CRC64;
MAYVIPKDPQ VMATKGSLFI VADGMGGHAA GEVASEIAVD TVSTAYYQDD SDEVPVALVR
AIKRANAAIH QRAAENMLRN GMGTTCVAAV LRGNMAYIAN VGDSRAYLIR GKTVKQISQD
HSWVAEQVRA GLLTEDQART HAQRNVITRS LGTQPDVEID IFTEPLQEGD SLVLCTDGLS
GLITEDELQE IVNRFVPQES VYHLVERANE NGGPDNITAI VIRVNEVGVE PPPRQRRPVA
VGGPEEDTAI LETSLASSAG QAGTRYGNGH SGTFSFSARA VPTLADAAPL AAPALPVSKR
RRRGRIFFLN VALLTVVLLA LVVGAVYYLV LRQGPDPDQV LAQATTLINR ATGELNSDPV
RALQDLASAQ QSLRSLQGVS LSDAQRTQLA SLQRSLTSHA EAALTAYNKR FGITSLPCSS
TGVSPINTGS IATRARSLAI LQQKGKALLY ALGEDSQLYP LMQVNRQYSL QNHLDLDGKV
LGVASANDGS QLYLLLARTS QSQGAASVSY ELAALQAGQT KAKTVPIDTA LTSNGQVPSL
IAAWDGDVYV VFSSKQAPNS AQIVDFDRTK LTAKQAPLPI SANVVSIAAF PNNQLFLLLG
DGSVQSLQYT SGKAQEPVPV PVQVQRPIPS ALPVSDQGFT AATPVPTVTV PAQQGPVPLL
ASNKATLSAG LVNHIPHLYV ADSAAHRLLA FTPLGGGSAG GTSDSNSILV QLTGQYTSPG
LFASLRSAQP DPSSGTLLYA LAQNTASLLN VVAVDTSSSG SCA
//