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Database: UniProt
Entry: J9ZEJ5_LEPFM
LinkDB: J9ZEJ5_LEPFM
Original site: J9ZEJ5_LEPFM 
ID   J9ZEJ5_LEPFM            Unreviewed;       284 AA.
AC   J9ZEJ5;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=DnaJ-class molecular chaperone {ECO:0000313|EMBL:AFS54596.1};
GN   OrderedLocusNames=LFML04_2407 {ECO:0000313|EMBL:AFS54596.1};
OS   Leptospirillum ferriphilum (strain ML-04).
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1048260 {ECO:0000313|EMBL:AFS54596.1, ECO:0000313|Proteomes:UP000006177};
RN   [1] {ECO:0000313|EMBL:AFS54596.1, ECO:0000313|Proteomes:UP000006177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ML-04 {ECO:0000313|EMBL:AFS54596.1,
RC   ECO:0000313|Proteomes:UP000006177};
RX   PubMed=22203551; DOI=10.1007/s12275-011-1099-9;
RA   Mi S., Song J., Lin J., Che Y., Zheng H., Lin J.;
RT   "Complete genome of Leptospirillum ferriphilum ML-04 provides insight into
RT   its physiology and environmental adaptation.";
RL   J. Microbiol. 49:890-901(2011).
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DR   EMBL; CP002919; AFS54596.1; -; Genomic_DNA.
DR   RefSeq; WP_014962099.1; NC_018649.1.
DR   AlphaFoldDB; J9ZEJ5; -.
DR   STRING; 1048260.LFML04_2407; -.
DR   KEGG; lfi:LFML04_2407; -.
DR   PATRIC; fig|1048260.3.peg.2616; -.
DR   HOGENOM; CLU_017633_0_0_0; -.
DR   Proteomes; UP000006177; Chromosome.
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; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   4: Predicted;
FT   DOMAIN          4..69
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   REGION          57..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   284 AA;  31919 MW;  7FE15E6F9EBD8C29 CRC64;
     MNEDYYSILG VSKSANEDEI KKAYRKLARK FHPDLNPGNK TSEQKFKEIN QAYEILSDPE
     KRKEYDRERE NPGPFRGKAG SDARSHKEGF GDFDGGDASF FWDVFGGGQR GTSRSLTTVR
     LTLSLVEVAR GTKKTVTLQG ESGKVESVTI QIPPGAEEGM GFEVEAPSLG KNRILYVVIE
     HILPDSRFER RGSDIYSDLR LTVPELYFGA SVHIPTLDGE TRLRIPPGSQ GGQTLRLKEK
     GIHSSFDGNR GHHYVRLIAL LPEKRSENLD ALMHQLESYY RISK
//
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