ID A0A496PIN7_9MICC Unreviewed; 475 AA.
AC A0A496PIN7;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=DWQ67_07440 {ECO:0000313|EMBL:RKW70327.1};
OS Galactobacter caseinivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Galactobacter.
OX NCBI_TaxID=2676123 {ECO:0000313|EMBL:RKW70327.1, ECO:0000313|Proteomes:UP000273119};
RN [1] {ECO:0000313|EMBL:RKW70327.1, ECO:0000313|Proteomes:UP000273119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JZ R-183 {ECO:0000313|EMBL:RKW70327.1,
RC ECO:0000313|Proteomes:UP000273119};
RA Hahne J., Isele D., Lipski A.;
RT "Arthrobacter sp. nov., isolated from raw cow's milk with high bacterial
RT count.";
RL Submitted (JUL-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:RKW70327.1}.
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DR EMBL; QQXL01000004; RKW70327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A496PIN7; -.
DR Proteomes; UP000273119; 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:UP000273119};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 348..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..237
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 456..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 475 AA; 51480 MW; BA0287DCCFBB5BF5 CRC64;
MALYLDFAAH SDVGKVRKKN DDSGYAGRYF AVVADGMGGH VGGDVASAST VLDLVHLDRS
DVEDPATMLA DEIQSANIIL NELVDQNPKL SGMGTTVTAL LLTRDRFRYA HIGDSRAYRL
KDGVWEQMSR DHTFVEKLLE EGRITAEEAK VHPHRNVIMR VLGDSDASPE LDLFEYPVEP
GERWMLCSDG INAVVPEEET EQIMRDSATV REAADRLVER TLELGSPDNV TAVVVEVLDD
AATPPSLDLS ALPEDPSPDT AQLRVAADGD LEANRAILRH DMANRPHELV GAALLATESG
QLAIVTQRSG ERRAAALLNH KTAQEETQSV ATDSELLTDE PPRKRRGWIL PAILVVCVAM
LASVLWLGYS WTQTRYYVGV NDGKVALFQG VSQDLGPLKL SHVDAQTQIP LDALPAFTQS
GLNSGIPGDT RQEAMETLAQ VLTTAKQNCD VTAPGAAPNG ATTEEPAYCT EEVPQ
//