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Database: UniProt
Entry: A0A0C5WDC3_9GAMM
LinkDB: A0A0C5WDC3_9GAMM
Original site: A0A0C5WDC3_9GAMM 
ID   A0A0C5WDC3_9GAMM        Unreviewed;       171 AA.
AC   A0A0C5WDC3;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Co-chaperone protein HscB homolog {ECO:0000256|HAMAP-Rule:MF_00682};
GN   Name=hscB {ECO:0000256|HAMAP-Rule:MF_00682};
GN   ORFNames=H744_2c3070 {ECO:0000313|EMBL:AJR09721.1};
OS   Photobacterium gaetbulicola Gung47.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR09721.1, ECO:0000313|Proteomes:UP000032303};
RN   [1] {ECO:0000313|EMBL:AJR09721.1, ECO:0000313|Proteomes:UP000032303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gung47 {ECO:0000313|EMBL:AJR09721.1,
RC   ECO:0000313|Proteomes:UP000032303};
RA   Kim Y.-O.;
RT   "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT   gaetbulicola Gung47.";
RL   Submitted (MAY-2013) 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, ECO:0000256|HAMAP-
CC       Rule:MF_00682}.
CC   -!- SUBUNIT: Interacts with HscA and stimulates its ATPase activity.
CC       {ECO:0000256|HAMAP-Rule:MF_00682}.
CC   -!- SIMILARITY: Belongs to the HscB family. {ECO:0000256|ARBA:ARBA00010476,
CC       ECO:0000256|HAMAP-Rule:MF_00682}.
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DR   EMBL; CP005974; AJR09721.1; -; Genomic_DNA.
DR   RefSeq; WP_044624097.1; NZ_CP005974.1.
DR   AlphaFoldDB; A0A0C5WDC3; -.
DR   STRING; 658445.H744_2c3070; -.
DR   KEGG; pgb:H744_2c3070; -.
DR   PATRIC; fig|658445.3.peg.5132; -.
DR   HOGENOM; CLU_068529_2_0_6; -.
DR   OrthoDB; 287587at2; -.
DR   Proteomes; UP000032303; Chromosome 2.
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   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 1.20.1280.20; HscB, C-terminal domain; 1.
DR   HAMAP; MF_00682; HscB; 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.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   3: Inferred from homology;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00682};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032303}.
FT   DOMAIN          2..74
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
SQ   SEQUENCE   171 AA;  19901 MW;  A67C158DCBC493E3 CRC64;
     MNHFELFGLP FQFQLDGSLL ATQFRELQRH FHPDNFATAS ERDRLLAVQK AAQINDAFQT
     LKNPISRAEY MLSVYGVDIR GEQKTLQDPE FLMQQMELRE ELEAIPESSD PQSALFDFEQ
     HASTLYKAQL VELEQLLVDE NWEVAADAVR KLKFIVKLRE EVERLEDSLL D
//
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