ID G5R3P4_SALSE Unreviewed; 171 AA.
AC G5R3P4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=Co-chaperone protein HscB {ECO:0000256|ARBA:ARBA00017570, ECO:0000256|HAMAP-Rule:MF_00682};
DE AltName: Full=Hsc20 {ECO:0000256|ARBA:ARBA00030734, ECO:0000256|HAMAP-Rule:MF_00682};
GN Name=hscB {ECO:0000256|HAMAP-Rule:MF_00682};
GN ORFNames=LTSESEN_4138 {ECO:0000313|EMBL:EHC84462.1};
OS Salmonella enterica subsp. enterica serovar Senftenberg str. A4-543.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913082 {ECO:0000313|EMBL:EHC84462.1, ECO:0000313|Proteomes:UP000005065};
RN [1] {ECO:0000313|EMBL:EHC84462.1, ECO:0000313|Proteomes:UP000005065}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A4-543 {ECO:0000313|EMBL:EHC84462.1,
RC ECO:0000313|Proteomes:UP000005065};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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 Interacts with IscU. {ECO:0000256|ARBA:ARBA00025986, ECO:0000256|HAMAP-
CC Rule:MF_00682}.
CC -!- SIMILARITY: Belongs to the HscB family. {ECO:0000256|ARBA:ARBA00010476,
CC ECO:0000256|HAMAP-Rule:MF_00682}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHC84462.1}.
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DR EMBL; AFCU01001360; EHC84462.1; -; Genomic_DNA.
DR AlphaFoldDB; G5R3P4; -.
DR SMR; G5R3P4; -.
DR PATRIC; fig|913082.3.peg.3195; -.
DR Proteomes; UP000005065; 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 GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
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 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}.
FT DOMAIN 2..74
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 171 AA; 20009 MW; E3716F4B6C2E714C CRC64;
MDYFTLFGLP ARYQIDTQAL SLRFQDLQRQ YHPDKFANGT QAQQLAAVQQ SATINQAWQT
LRHPLTRAEY LLSLHGFDLA SEQHTVRDTA FLMEQLTLRE ELDDIEQSKD DVRLESFIKR
VQKMFDARLQ QMVEQLDNAA WDAAADTVRK LRFLDKLRSS AEQLEEKLLD F
//
