ID A0A0E3UXM8_9BACT Unreviewed; 177 AA.
AC A0A0E3UXM8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Co-chaperone Hsc20 {ECO:0000313|EMBL:AKD03716.1};
GN ORFNames=PKOR_12000 {ECO:0000313|EMBL:AKD03716.1};
OS Pontibacter korlensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=400092 {ECO:0000313|EMBL:AKD03716.1, ECO:0000313|Proteomes:UP000033109};
RN [1] {ECO:0000313|EMBL:AKD03716.1, ECO:0000313|Proteomes:UP000033109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X14-1T {ECO:0000313|EMBL:AKD03716.1,
RC ECO:0000313|Proteomes:UP000033109};
RX PubMed=26057562; DOI=10.1038/srep10929;
RA Dai J., Dai W., Qiu C., Yang Z., Zhang Y., Zhou M., Zhang L., Fang C.,
RA Gao Q., Yang Q., Li X., Wang Z., Wang Z., Jia Z., Chen X.;
RT "Unraveling adaptation of Pontibacter korlensis to radiation and
RT infertility in desert through complete genome and comparative
RT transcriptomic analysis.";
RL Sci. Rep. 5:10929-10929(2015).
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; CP009621; AKD03716.1; -; Genomic_DNA.
DR RefSeq; WP_046311008.1; NZ_CP009621.1.
DR AlphaFoldDB; A0A0E3UXM8; -.
DR STRING; 400092.PKOR_12000; -.
DR KEGG; pko:PKOR_12000; -.
DR PATRIC; fig|400092.3.peg.2621; -.
DR HOGENOM; CLU_068529_2_0_10; -.
DR OrthoDB; 287587at2; -.
DR Proteomes; UP000033109; 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 CDD; cd06257; DnaJ; 1.
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; PF00226; DnaJ; 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.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Reference proteome {ECO:0000313|Proteomes:UP000033109}.
FT DOMAIN 2..74
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 177 AA; 20932 MW; 572C43FDF85ADF9A CRC64;
MNYFEFYNIP ESFLLDEKAL KNTYYKLSRE YHPDFFANEP QEKQQDILQL STLNTNAYRT
LSDPDLRMQY ILREHGLLEE GGKNELPSDF LMKMMELNEE LMELEFDFDA AKLHEIGEKS
SGVMSQLDND ILPVLQRYPE LHGVTKDEAL QQVKTYYLKK KYLLRIQESL SKFASHS
//
