ID A0A031FS77_9MICO Unreviewed; 409 AA.
AC A0A031FS77;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=BW34_01654 {ECO:0000313|EMBL:EZP27664.1};
OS Microbacterium oleivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=273677 {ECO:0000313|EMBL:EZP27664.1, ECO:0000313|Proteomes:UP000024001};
RN [1] {ECO:0000313|EMBL:EZP27664.1, ECO:0000313|Proteomes:UP000024001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT293 {ECO:0000313|EMBL:EZP27664.1,
RC ECO:0000313|Proteomes:UP000024001};
RA Gan H.Y., Gan H.M., Savka M.A., Hudson A.O.;
RT "Draft Genome Sequences of 13 Willow Endophytes.";
RL Submitted (MAR-2014) 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:EZP27664.1}.
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DR EMBL; JFYO01000005; EZP27664.1; -; Genomic_DNA.
DR RefSeq; WP_036311198.1; NZ_SLUC01000004.1.
DR AlphaFoldDB; A0A031FS77; -.
DR KEGG; moo:BWL13_00024; -.
DR PATRIC; fig|273677.3.peg.1637; -.
DR eggNOG; COG0631; Bacteria.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000024001; 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:UP000024001};
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"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 409 AA; 44250 MW; 17C241F72F0FF665 CRC64;
MVFEGSSAAI SHTGKVRSNN QDSGFSGSNL FVVADGMGGH AGGDIASSIA VHHLEGLDHS
FPTPAEAERE LREAIVDAAH VLVDTVAERP ELAGMGTTVS AVLMVDDYAV IAHIGDSRVY
LFRDGVFTQI TTDHTFVQRL VDSGRITPEE ARYHPRRSVL MRVLGDMGTD PEVDAFIMQT
QPGDRWLICS DGLCGVVDDA QSAKVLRQDL APGRTADMLL KLALDAGAPD NVTIVLVDVG
GRHPMYSGTA TIVGSAATPK GIEVPVARPA RTGWFQTGRQ AANEPSHFEP AAEYLEELIE
EDRRRARRRR VWWIVGFITI VAVIAAGVFA GYAWTQTRYF VGPDDDSVVI YRGIQQDIGP
ISLSTPFEDT NILLADLPAY QRQAVEQTIS ARSLSDAEAI VDNLRQGTP
//
