ID A0A4Y3UJA9_9MICO Unreviewed; 412 AA.
AC A0A4Y3UJA9;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, 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=FHX68_1838 {ECO:0000313|EMBL:TQM97839.1};
OS Microbacterium lacticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=33885 {ECO:0000313|EMBL:TQM97839.1, ECO:0000313|Proteomes:UP000319804};
RN [1] {ECO:0000313|EMBL:TQM97839.1, ECO:0000313|Proteomes:UP000319804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20427 {ECO:0000313|EMBL:TQM97839.1,
RC ECO:0000313|Proteomes:UP000319804};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (JUN-2019) 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:TQM97839.1}.
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DR EMBL; VFPS01000003; TQM97839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4Y3UJA9; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000319804; 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:UP000319804};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 311..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..239
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 412 AA; 44416 MW; 4BC57D2BCCDA590A CRC64;
MVFEGSSVAI SHTGKVRSNN QDSGYAGSNL FVVADGMGGH AGGDVASSIA VHRLKDLDHP
FATPTEAEVA LQQAISVTAT VLIDTVSERP ELAGMGTTVS ALVMVDDYAV IAHIGDSRIY
LYRDDALTQI TTDHTFVQRL VDSGRITPEE ARYHPRRSVL MRVLGDMDPD PQIDTFIMPT
QPGDRWLLCS DGLCGVVDDA HISKTLGQGL PPGRTADLLL KQALDAGAPD NVTVVIVDVG
GSHPMFSGAG TIVGSASNPR GVEVPAARPG RTSWLHPGRQ AANEPTHFEP AAEFLEELIE
EDRRRARRRR VWWIVGLAVI LAVLAAATLG AYSWTQSRYF VGADDDTVVI FRGIQQDLGP
ISLSSPYEDT GIELVDLPFY QRLAVQQTIS ARSLANAEAI VETMRRTLED AP
//
