ID K8X899_9GAMM Unreviewed; 173 AA.
AC K8X899;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
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 ECO:0000313|EMBL:EKT64665.1};
GN ORFNames=OOA_02672 {ECO:0000313|EMBL:EKT64665.1};
OS Providencia burhodogranariea DSM 19968.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1141662 {ECO:0000313|EMBL:EKT64665.1, ECO:0000313|Proteomes:UP000009336};
RN [1] {ECO:0000313|EMBL:EKT64665.1, ECO:0000313|Proteomes:UP000009336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19968 {ECO:0000313|EMBL:EKT64665.1,
RC ECO:0000313|Proteomes:UP000009336};
RX PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA Galac M.R., Lazzaro B.P.;
RT "Comparative genomics of bacteria in the genus Providencia isolated from
RT wild Drosophila melanogaster.";
RL BMC Genomics 13:612-612(2012).
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:EKT64665.1}.
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DR EMBL; AKKL01000007; EKT64665.1; -; Genomic_DNA.
DR RefSeq; WP_008910580.1; NZ_KB233222.1.
DR AlphaFoldDB; K8X899; -.
DR STRING; 1141662.OOA_02672; -.
DR PATRIC; fig|1141662.3.peg.540; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_068529_2_0_6; -.
DR OrthoDB; 287587at2; -.
DR Proteomes; UP000009336; 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; 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, ECO:0000256|HAMAP-Rule:MF_00682}.
FT DOMAIN 2..74
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
SQ SEQUENCE 173 AA; 20564 MW; D5E66F92A8E93FC2 CRC64;
MDYFTLFGLT PSYAIDSEQL TQCFQSLQRQ YHPDRFATCT EQEKLQSIQQ AANINAAYQA
LRHPLRRAEY MLLLHGFDIN NEQHTMHDTA FLMEQLELRE ELDHIENSHS ADELLVDFMA
RVKKMQRDRS TLMVSQLDNE LWEQSADTVR KLRFLDKLQQ HAEQLEERLL DDF
//
