ID A0A1Y1RDX9_9BACT Unreviewed; 627 AA.
AC A0A1Y1RDX9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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=B6244_14250 {ECO:0000313|EMBL:OQY26134.1};
OS Candidatus Cloacimonetes bacterium 4572_55.
OC Bacteria; Candidatus Cloacimonadota.
OX NCBI_TaxID=1971726 {ECO:0000313|EMBL:OQY26134.1, ECO:0000313|Proteomes:UP000192623};
RN [1] {ECO:0000313|Proteomes:UP000192623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dombrowski N., Seitz K., Teske A., Baker B.;
RT "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT hydrothermal sediment communities.";
RL Submitted (MAR-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:OQY26134.1}.
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DR EMBL; NBMB01000083; OQY26134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1RDX9; -.
DR STRING; 1971726.B6244_14250; -.
DR Proteomes; UP000192623; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 307..329
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..253
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 336..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 627 AA; 69174 MW; D08EDBCAF6F17AB3 CRC64;
MSIQTIKSDL GNAVALSDVG MVRSENQDAF AMWEASARGG LPTRLLCVAV ADGMGGHQGG
STASRETLLV VKENLSSIDE RSVAAHVQAS LENANRHVHK LGHQNPELQG MGTTCTLAVI
TPGELYLGHI GDSRCYEIAE DHISQLSKDH LYVLELLERG ALTKEQAANH PDQNVLSRAL
GTRPSVEVDV SKRIIDPNST LLFCSDGLYN YLSDSEIRSI VIQNDHQTAI QKLIDLAKER
GGADNITVIL LALDKDALRS TAEDQKDRYE TRQVAAPHSA TRKMNIDPEK LNPTNAIDRR
DVLKKRVIVI LAVLALITAL LLGMTFLYYK DKQSSSASNK SVPEDAIAPD KSEHDIDPPT
PEPTLQSIKK ENQGNECPMP DLQRSNKEAN ATAILHFGPD DVNFDQYDVY IDGARIHSKK
IEKFPGSYDI KVKLDDETIC EYKIELAAGD KREIQLPRFS PKKVTQQLTT KLPDVKPDTG
SVADPVKAKK GKLNITINGC ACKILFKGNR IDDTFPRKMD PGTHKFKFIV NDNFGYTFDK
DIEIIAGQTN DVEIKLHKVT IASPGNQNSK NFEIHINERL VEYAPIVGIC LPTGEYNISA
IGTKSYTISK RIIEQDCTIN EWDSGSP
//
