ID A0A1L7F434_9PSEU Unreviewed; 482 AA.
AC A0A1L7F434;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=UA75_07610 {ECO:0000313|EMBL:APU19541.1};
OS Actinoalloteichus sp. GBA129-24.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=1612551 {ECO:0000313|EMBL:APU19541.1, ECO:0000313|Proteomes:UP000185506};
RN [1] {ECO:0000313|EMBL:APU19541.1, ECO:0000313|Proteomes:UP000185506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GBA129-24 {ECO:0000313|EMBL:APU19541.1,
RC ECO:0000313|Proteomes:UP000185506};
RA Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA Kalinowski J., Zotchev S.B.;
RT "Complete genome sequence of Actinoalloteichus fjordicus DSM 46856
RT (=GBA129-24).";
RL Submitted (JUN-2016) 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};
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DR EMBL; CP016077; APU19541.1; -; Genomic_DNA.
DR RefSeq; WP_075739663.1; NZ_CP016077.1.
DR AlphaFoldDB; A0A1L7F434; -.
DR STRING; 1612551.UA75_07610; -.
DR KEGG; acti:UA75_07610; -.
DR Proteomes; UP000185506; Chromosome.
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 459..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..236
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 277..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..455
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 482 AA; 48691 MW; 111D0C7B168C7DA9 CRC64;
MTLALRYTAR SDRGLVRSNN EDSVYAGPRL LAVADGMGGH VGGEIASRVV IASVTPLDDA
DPAEDLLGAL RDAAVDGNSA IAATVEEEPE LAGMGTTLTA LLFADDRVGL LNVGDSRAYL
MRDDELVQIT HDDTFVQSLV DAGRITIAEA EVHPKRSLVL RALTGEEVVE TTTELREVRA
GDRYLLCSDG LTDVLNHAAL SVELRIGDHE VCADRLIEAA LAGGGPDNVT VIVADVTEVS
EGAGDAEAAA VAGGSAGSSE PAAVAATVAP AGAAAADAPD ADSAAPDSTA PDGIGHGAET
PAADPTEPAG LDRATAGQDH AEAPVAPTVS AWFTEADRSS QADEAQAAGS RDVERSGAAG
AQADPGWAET SRPADSATAS DSAVSGHAPV TPTNDADPAV STEQATATTP EDAGADGGAA
VTEQAAAGRD ESSDRREDAS TTDWSAAEHR RQPRSARSLL VGAAVLGVGA VATIAVRRRL
GR
//
