ID A0A4R7IWU6_9ACTN Unreviewed; 607 AA.
AC A0A4R7IWU6;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=CLV29_3232 {ECO:0000313|EMBL:TDT29132.1};
OS Naumannella halotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Naumannella.
OX NCBI_TaxID=993414 {ECO:0000313|EMBL:TDT29132.1, ECO:0000313|Proteomes:UP000295371};
RN [1] {ECO:0000313|EMBL:TDT29132.1, ECO:0000313|Proteomes:UP000295371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24323 {ECO:0000313|EMBL:TDT29132.1,
RC ECO:0000313|Proteomes:UP000295371};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2019) 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:TDT29132.1}.
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DR EMBL; SOAW01000004; TDT29132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R7IWU6; -.
DR Proteomes; UP000295371; 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:UP000295371};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 439..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..237
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 244..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..377
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 607 AA; 62835 MW; 4973A5C04966B3B8 CRC64;
MHLRFTAHSE TGPVRKNNQD SGYASTRLLV VADGMGGAAA GDLASAVAAD LFRRLDASAD
KATGEEMLEL LAGAISRSND KIADLVADDP NLEGMGTTVS AYMFDGRQLG IAHIGDSRGY
LLRDGQLRRT THDHSWVQSL IDEGKISEEE ATSHPHRNLL LKVINGQPQN EPDLDLIEVR
PGDRLLLCSD GLCGLVDDQH IAAALSQDTL LEAMDELIDL AYAGGGIDNI TVLLADVLAD
PGEVVDGPGS TGEGTAAVPG GDHQPELSGT GGDAAGSDAE HTGSEGAHPK SISADSTDTD
SSDTAPEGTE PVKADGSETE GTESAATADA DAGSTTGPVV NPDGTEDTLV RVPTQKDQPP
STPASPDEQP PHPSEDLPTA PVILGAATER AIPAVRDRTP DERAAAVADE QMLVSGSPAD
PADDEEARYA LSAPPKLRWL RIAVTVLLAL LVLFVGGLAG NAWINTQYYV GPSEEKVAIF
RGIPDSVAGL NLSQVYETTD TQVSDLPVYY RQRVNETIPA SDLLAARNTV DELAQAAQAC
IAQRDAEAPL DPQASASAPP RPEETESPDS SASASASASA SAEATAESTT TTTPTTTPTQ
GLGGECG
//
