ID A0A0Q8AIY9_9MICO Unreviewed; 412 AA.
AC A0A0Q8AIY9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=ASD56_04850 {ECO:0000313|EMBL:KQZ85636.1};
OS Microbacterium sp. Root166.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1736478 {ECO:0000313|EMBL:KQZ85636.1, ECO:0000313|Proteomes:UP000051650};
RN [1] {ECO:0000313|Proteomes:UP000051650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root166 {ECO:0000313|Proteomes:UP000051650};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ85636.1, ECO:0000313|Proteomes:UP000051650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root166 {ECO:0000313|EMBL:KQZ85636.1,
RC ECO:0000313|Proteomes:UP000051650};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQZ85636.1}.
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DR EMBL; LMGL01000001; KQZ85636.1; -; Genomic_DNA.
DR RefSeq; WP_055961870.1; NZ_LMGL01000001.1.
DR AlphaFoldDB; A0A0Q8AIY9; -.
DR STRING; 1736478.ASD56_04850; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000051650; 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:UP000051650};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 311..332
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; 44028 MW; C891F6AE5253549A CRC64;
MVFQGSSVAI SHTGKVRSNN QDSGYAGSNL FVVADGMGGH AGGDVASSMV IARLERLDKP
YESTGAAEKA LRDAIGDAAT ELIDTVHDRP ELAGMGTTVS ALIMVDDYAV IAHIGDSRIY
LFRDGALTQI TTDHTFVQRL VDSGRITPEE ARYHPRRSVL MRVLGDMDPD PELDTFIMPT
QPGDRWLLCS DGLSGVVDDP HTGKALGLGV APGRTADILL KQALDGGAPD NVTIVIVDVG
GQHPLFSGTP TVVGSASNPV GVGVPAARAG RPSWLHPNRQ AANEPTHFEP AAEFLEELIE
EDRRRVRRRR IGWIAGAVLV LGILIGVLWV GYQWTQTRYY VGADEDTVVI FRGVQQGIGP
ISLSTPYEDT EIPLDSLSEF ARATVEQTIS AGSLSNARQI VATISDTAEL NG
//
