ID A0A1H9J1E3_9BACT Unreviewed; 172 AA.
AC A0A1H9J1E3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Molecular chaperone HscB {ECO:0000313|EMBL:SEQ80670.1};
GN ORFNames=SAMN05444359_11649 {ECO:0000313|EMBL:SEQ80670.1};
OS Neolewinella agarilytica.
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae;
OC Neolewinella.
OX NCBI_TaxID=478744 {ECO:0000313|EMBL:SEQ80670.1, ECO:0000313|Proteomes:UP000199021};
RN [1] {ECO:0000313|Proteomes:UP000199021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24740 {ECO:0000313|Proteomes:UP000199021};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOFB01000016; SEQ80670.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9J1E3; -.
DR STRING; 478744.SAMN05444359_11649; -.
DR InParanoid; A0A1H9J1E3; -.
DR OrthoDB; 287587at2; -.
DR Proteomes; UP000199021; Unassembled WGS sequence.
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:UP000199021}.
FT DOMAIN 3..77
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 172 AA; 19938 MW; 4B1511BCC7365EB1 CRC64;
MTNYFEFYGL APSPTLDEAA LKKTFYANSK RFHPDFHTLG GDAAREEALE KSTLNNQAYK
VLSDPERRLK HLLDLKGVMG EEGSNKMPQQ FLMEIMDVNE ALMELEFEDD PAARTKIDNM
IAELEDGFER EVSDLLTDYD DASVTESELN RLKDYYLKKR YLLRLKNRNP EV
//
