ID Q3YS55_EHRCJ Unreviewed; 145 AA.
AC Q3YS55;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Heat shock protein DnaJ, N-terminal {ECO:0000313|EMBL:AAZ68450.1};
GN OrderedLocusNames=Ecaj_0407 {ECO:0000313|EMBL:AAZ68450.1};
OS Ehrlichia canis (strain Jake).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=269484 {ECO:0000313|EMBL:AAZ68450.1, ECO:0000313|Proteomes:UP000000435};
RN [1] {ECO:0000313|Proteomes:UP000000435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Jake {ECO:0000313|Proteomes:UP000000435};
RX PubMed=16707693; DOI=10.1128/JB.01837-05;
RA Mavromatis K., Doyle C.K., Lykidis A., Ivanova N., Francino M.P., Chain P.,
RA Shin M., Malfatti S., Larimer F., Copeland A., Detter J.C., Land M.,
RA Richardson P.M., Yu X.J., Walker D.H., McBride J.W., Kyrpides N.C.;
RT "The genome of the obligately intracellular bacterium Ehrlichia canis
RT reveals themes of complex membrane structure and immune evasion
RT strategies.";
RL J. Bacteriol. 188:4015-4023(2006).
CC -!- FUNCTION: Co-chaperone involved in the maturation of iron-sulfur
CC cluster-containing proteins. Seems to help targeting proteins to be
CC folded toward HscA. {ECO:0000256|ARBA:ARBA00025596}.
CC -!- SIMILARITY: Belongs to the HscB family.
CC {ECO:0000256|ARBA:ARBA00010476}.
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DR EMBL; CP000107; AAZ68450.1; -; Genomic_DNA.
DR RefSeq; WP_011304528.1; NC_007354.1.
DR AlphaFoldDB; Q3YS55; -.
DR STRING; 269484.Ecaj_0407; -.
DR KEGG; ecn:Ecaj_0407; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_068529_2_2_5; -.
DR InParanoid; Q3YS55; -.
DR Proteomes; UP000000435; Chromosome.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.20.1280.20; HscB, C-terminal domain; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR004640; HscB.
DR InterPro; IPR036386; HscB_C_sf.
DR InterPro; IPR009073; HscB_oligo_C.
DR InterPro; IPR036869; J_dom_sf.
DR NCBIfam; TIGR00714; hscB; 1.
DR PANTHER; PTHR14021; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR PANTHER; PTHR14021:SF15; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR Pfam; PF07743; HSCB_C; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF47144; HSC20 (HSCB), C-terminal oligomerisation domain; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Stress response {ECO:0000313|EMBL:AAZ68450.1}.
FT DOMAIN 3..66
FT /note="J"
FT /evidence="ECO:0000259|SMART:SM00271"
SQ SEQUENCE 145 AA; 17029 MW; 2F378209EEC31878 CRC64;
MYKDYFSLFK LKQEFCINIQ VLEQNYIALQ SNYHPDLFFL KSEKKLALDN IAEINKAYQI
LKSSITRAEY LLQIKGITAD KNDINSIIEE IFKIQESNNI DIEYQISSAT KAMEDAFSRE
DFNEAAKQVI KLKYLRKIQE DRGII
//
