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Database: UniProt
Entry: A0A0T2L0E1_9MICO
LinkDB: A0A0T2L0E1_9MICO
Original site: A0A0T2L0E1_9MICO 
ID   A0A0T2L0E1_9MICO        Unreviewed;       327 AA.
AC   A0A0T2L0E1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Molecular chaperone DnaJ {ECO:0000313|EMBL:KRA25322.1};
GN   ORFNames=ASD65_13495 {ECO:0000313|EMBL:KRA25322.1};
OS   Microbacterium sp. Root61.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA25322.1, ECO:0000313|Proteomes:UP000051216};
RN   [1] {ECO:0000313|EMBL:KRA25322.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA25322.1,
RC   ECO:0000313|Proteomes:UP000051216};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA25322.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA25322.1,
RC   ECO:0000313|Proteomes:UP000051216};
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:KRA25322.1}.
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DR   EMBL; LMGU01000001; KRA25322.1; -; Genomic_DNA.
DR   RefSeq; WP_056223464.1; NZ_LMGU01000001.1.
DR   AlphaFoldDB; A0A0T2L0E1; -.
DR   STRING; 1736570.ASD65_13495; -.
DR   OrthoDB; 9779889at2; -.
DR   Proteomes; UP000051216; 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; DNAJ HOMOLOG 1, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43096:SF52; 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   Reference proteome {ECO:0000313|Proteomes:UP000051216}.
FT   DOMAIN          10..75
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   REGION          307..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   327 AA;  35101 MW;  E48D9E2645C2DD17 CRC64;
     MASQDWFDKD FYKVLGVSKG VSEADLKKTY RKLARKYHPD SNHGDAQAEA TFKEISEAYS
     VLSDPEQRTE YDQIRAMGSG ARFTSGGQGA GFEDVFSRFG QGRGARTQSP EDFDDIFSMF
     NQGGSFGSGG FGQTSGGFRG YGGPTRGADV TARTTIDFIT ATKGETITLQ GEDGKPFKVK
     IPAGVADGQK IRLRGRGRPS PDGGENGDIV VQITVRPHPV FTRDGLNLRV TVPVTFTEAA
     LGATIEVPTL GADPVKLRVA PGTPSGRVLR VKGRGVQTTK GTGDLLAEVQ VAVPSHLDDE
     ARAALERFQE LEPKENPRAE LMTKARG
//
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