ID A0A3L8P0U8_9ACTN Unreviewed; 465 AA.
AC A0A3L8P0U8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=D9V37_18440 {ECO:0000313|EMBL:RLV48423.1};
OS Nocardioides mangrovicus.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=2478913 {ECO:0000313|EMBL:RLV48423.1, ECO:0000313|Proteomes:UP000281708};
RN [1] {ECO:0000313|EMBL:RLV48423.1, ECO:0000313|Proteomes:UP000281708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4Q3S-7 {ECO:0000313|EMBL:RLV48423.1,
RC ECO:0000313|Proteomes:UP000281708};
RA Li F.;
RT "Marmoricola sp. 4Q3S-7 whole genome shotgun sequence.";
RL Submitted (OCT-2018) 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:RLV48423.1}.
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DR EMBL; RDBE01000010; RLV48423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8P0U8; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000281708; 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:UP000281708};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 318..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..239
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 417..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 465 AA; 48794 MW; B36F037CAE82CF51 CRC64;
MLRLRYTAVS DVGRVRKDNQ DSGYAGPHLL AVADGVGGSA RGDVASSAAI AELKALDVEP
PQGPDDADLT RTVAATIDAA HRRIGDLTEQ YPELETTSTT VTLAVFDGAR LAIGHVGDSR
GYLLRDGEIT RLTTDHTFVQ SLIDEGRITE EESRVHPHRN LILRAVDGVH ESEPDLFFVD
VRAGDRIMLC SDGASGALDD AALALVLGQG TVEKAAQDLV RESLEAGSTD NVTVVAADVI
DTAAEDPDET QAIAVGPVVV GAAAERRKGL SRRRPRKADT GELEAVPAAA DGGPAPHGIV
TDPETIRYAP RAPHRFAWLG RLVVILIVVA VLYVAATAAY RWSQKQYFIK PAAGYVAIYQ
GVPADLPVVS LHHVLQRSDT LVADLPSYYR GQVRNGMSAD SLADARALLR RLEGQADCSS
AATTTPSATP TPTATPTPGA ATGPSTSPAT SPSVSPTTSP TTPAC
//
