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Database: UniProt
Entry: A0A0T0PRE2_9SPHN
LinkDB: A0A0T0PRE2_9SPHN
Original site: A0A0T0PRE2_9SPHN 
ID   A0A0T0PRE2_9SPHN        Unreviewed;       313 AA.
AC   A0A0T0PRE2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Molecular chaperone DnaJ {ECO:0000313|EMBL:KQT31284.1};
GN   ORFNames=ASG29_15075 {ECO:0000313|EMBL:KQT31284.1};
OS   Sphingomonas sp. Leaf412.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT31284.1, ECO:0000313|Proteomes:UP000051178};
RN   [1] {ECO:0000313|EMBL:KQT31284.1, ECO:0000313|Proteomes:UP000051178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf412 {ECO:0000313|EMBL:KQT31284.1,
RC   ECO:0000313|Proteomes:UP000051178};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT31284.1, ECO:0000313|Proteomes:UP000051178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf412 {ECO:0000313|EMBL:KQT31284.1,
RC   ECO:0000313|Proteomes:UP000051178};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQT31284.1}.
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DR   EMBL; LMQP01000004; KQT31284.1; -; Genomic_DNA.
DR   RefSeq; WP_055986150.1; NZ_LMQP01000004.1.
DR   AlphaFoldDB; A0A0T0PRE2; -.
DR   STRING; 1736370.ASG29_15075; -.
DR   OrthoDB; 9779889at2; -.
DR   Proteomes; UP000051178; Unassembled WGS sequence.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10747; DnaJ_C; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR43096:SF48; CHAPERONE PROTEIN DNAJ; 1.
DR   PANTHER; PTHR43096; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   4: Predicted;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051178}.
FT   DOMAIN          3..68
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   REGION          28..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   313 AA;  32605 MW;  054EE960FB69DA29 CRC64;
     MADPYQTLGV ARSATEADIK KAYRKLAKEL HPDRNKDNPK ASERFSQVTN AYDLLQDKDK
     RARFDRGEID GDGNPAMPFG YGGGTPRGAG GGFRSQEFDA GGFGGGAGGP DVSDLFEGLF
     GGRGAGGFTG GFGRRSAGPP PKGGNVAYRL RVPLPDAAAL APQRITLADG KTIDLKLPAG
     VEDGTQMRLG GKGDPGPGGA GDAIVTIEVE PHRFFTRDGD DVRLDLPVTL KEAVAGAAVK
     VPTVEKPVML TVPAGSTSGR TLRIKGRGFH RKGGGRGDQL VTLLVDVPAD DAALKAFVED
     WTPEGNPRST LGV
//
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