ID A0A257B9Q4_9BACT Unreviewed; 349 AA.
AC A0A257B9Q4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=CFK52_01405 {ECO:0000313|EMBL:OYT73604.1};
OS Chloracidobacterium sp. CP2_5A.
OC Bacteria; Acidobacteriota; Blastocatellia; Chloracidobacterium.
OX NCBI_TaxID=2012633 {ECO:0000313|EMBL:OYT73604.1, ECO:0000313|Proteomes:UP000216393};
RN [1] {ECO:0000313|EMBL:OYT73604.1, ECO:0000313|Proteomes:UP000216393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CP2_5A {ECO:0000313|EMBL:OYT73604.1};
RA Ward L.M., Mcglynn S.E., Fischer W.;
RT "Draft genome of Chloracdibacterium sp. CP2_5A, a phototrophic
RT Acidobacteria from a Japanese hot spring.";
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};
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:OYT73604.1}.
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DR EMBL; NKPT01000002; OYT73604.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257B9Q4; -.
DR Proteomes; UP000216393; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 310..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..249
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 253..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 37668 MW; 6C105840D35D6993 CRC64;
MANEVAAPAA APAIRFACIC DRGLKRASNQ DRALAEVNAR LFVVCDGVGG NTGGEIASQT
AIETVRDAFI APDNHPPLVR LERAIHYANR DIFEMAKHDL DLAGMATTLV ALHLDGETAC
AAHAGDSRLY HFANGALTQV TIDHTPLQDA IRCGKLSVAE AEQLPKANEV SRALGIFPEV
EVETQDFAFA VGARFLLCTD GVTRHIANEE LERLMATFAD NPDGLCDEIH RYCYERGAED
NFTALVVCVD PPSAAAPPPS PPSSPSLQER LTRTRELSVA PSFPADRTTG EHHPLKELVE
ARRARSRREL TLQALAVLLL MALSFGAGWW MGARQALPPA VSPRPLTGR
//
