ID A0A0L6HUN2_9MICO Unreviewed; 431 AA.
AC A0A0L6HUN2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=AKH00_14780 {ECO:0000313|EMBL:KNY04750.1};
OS Microbacterium sp. GCS4.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1692239 {ECO:0000313|EMBL:KNY04750.1, ECO:0000313|Proteomes:UP000037096};
RN [1] {ECO:0000313|Proteomes:UP000037096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GCS4 {ECO:0000313|Proteomes:UP000037096};
RA Jones K.J., Moore K., Sambles C., Love J., Studholme D.J., Aves S.J.;
RT "Genome sequencing of alga-associated bacteria.";
RL Submitted (JUL-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:KNY04750.1}.
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DR EMBL; LGYE01000004; KNY04750.1; -; Genomic_DNA.
DR RefSeq; WP_050723511.1; NZ_LGYE01000004.1.
DR AlphaFoldDB; A0A0L6HUN2; -.
DR STRING; 1692239.AKH00_14780; -.
DR PATRIC; fig|1692239.3.peg.2987; -.
DR OrthoDB; 9801841at2; -.
DR Proteomes; UP000037096; 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 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 411..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 431 AA; 46220 MW; 243125B3C9AA3E3A CRC64;
MVFEGSSVAI SHTGKVRSNN QDSGYSGANL FVVADGMGGH AGGDVASSIA ISRMQPLDQP
YTSTEDAQAS LQAAATTAAG DLIRAAKDRP ELAGLGTTLS AIIMVDDFAV IGHIGDSRIY
LYRDDALTQI TADHTFVQRL VDSGRITPEE ARYHPRRSVL MRVLSDMDSD PELDMFVMHT
QPGDRWLLCS DGLSGVVDED HILKAMRLGL APGRTADNLL KQALDGGAPD NVTIVLVDVG
GQHAMHSGTA TIVGSASNPA NITVPPVRAP RSSWLHPVRQ AANDPSHFEP SSEYLEELIE
EDRRRAKRRR LGWIAGMLVV LAMLAFAAFA AYSWTQTRYF VGADEDSVVI YQGVQQNIGP
ITLSTPIEDT DILLANLPPY QRDSVERTIT ARSLSDAQAI VARLQAGADR VTGETPLPTP
VPTPTETEGA G
//
