ID A0A160T709_9CHLR Unreviewed; 506 AA.
AC A0A160T709;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=CFX0092_B0198 {ECO:0000313|EMBL:CUS05732.1};
OS Candidatus Promineifilum breve.
OC Bacteria; Chloroflexota; Ardenticatenia; Candidatus Promineifilales;
OC Candidatus Promineifilaceae; Candidatus Promineifilum.
OX NCBI_TaxID=1806508 {ECO:0000313|EMBL:CUS05732.1, ECO:0000313|Proteomes:UP000215027};
RN [1] {ECO:0000313|EMBL:CUS05732.1, ECO:0000313|Proteomes:UP000215027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cfx-K {ECO:0000313|EMBL:CUS05732.1,
RC ECO:0000313|Proteomes:UP000215027};
RA Oliw E.H.;
RL Submitted (JAN-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};
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DR EMBL; LN890656; CUS05732.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A160T709; -.
DR KEGG; pbf:CFX0092_B0198; -.
DR OrthoDB; 152713at2; -.
DR Proteomes; UP000215027; Chromosome ii.
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:UP000215027};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 334..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..253
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 293..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 506 AA; 51419 MW; 59AA5AC21F168ED6 CRC64;
MESINNAAAA FDPRFLGVTT VAGRRPVNED AWGAPPPGAA DAVACFVVAD GVGGQERGDV
ASRTAAAAVI RAFYERRAAG DDPAAALLAA VSAANAEVYR LAQSLGVERM GCTLAAAAVG
GGRLDVVHVG DARAWLWQGG RLYALTRDHT WVQEQVDRGT ITPADAAQHE LRHIVTRVLG
NEATIEATLA RPAAFGPGDR LLLSSDGLHD VVDETRLAQL LGLGAPGVAA QTLVEAALAG
GSEDNVTALV VEGRPAGAAR PHEATPVAQP REVAPAARQA TEVLPPDNKR IAAVPPATQS
PSEVATVQGK RPPPGYIPPQ GRAPAAAPPA QRTALLPVLG AAVLAVFVLI GAFTILLPIL
RSLSGSDATP TAAVPGGAAT STPDPAATSP AAAATSTGAP TGVPDGYPPP TATAAAEATV
AVGGVMCIVP ANGTFRYSNE KAAMTATCLW ADDLLQGPVT ILAGRQMITT QPDCGDYEFQ
QVQSVASPHI VGWVLAANLV ACPEER
//
