HSCB_ECOLI
ID HSCB_ECOLI Reviewed; 171 AA.
AC P0A6L9; P36540;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Co-chaperone protein HscB;
DE AltName: Full=Hsc20;
GN Name=hscB; Synonyms=yfhE; OrderedLocusNames=b2527, JW2511;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8300516; DOI=10.1128/jb.176.3.610-619.1994;
RA Kawula T.H., Lelivelt M.J.;
RT "Mutations in a gene encoding a new Hsp70 suppress rapid DNA inversion and
RT bgl activation, but not proU derepression, in hns-1 mutant Escherichia
RT coli.";
RL J. Bacteriol. 176:610-619(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 119-171.
RC STRAIN=B;
RX PubMed=8134349; DOI=10.1073/pnas.91.6.2066;
RA Seaton B.L., Vickery L.E.;
RT "A gene encoding a DnaK/hsp70 homolog in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:2066-2070(1994).
RN [6]
RP CHARACTERIZATION.
RX PubMed=9144776; DOI=10.1002/pro.5560060511;
RA Vickery L.E., Silberg J.J., Ta D.T.;
RT "Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from
RT Escherichia coli.";
RL Protein Sci. 6:1047-1056(1997).
RN [7]
RP CHARACTERIZATION.
RX PubMed=10869428; DOI=10.1073/pnas.130201997;
RA Hoff K.G., Silberg J.J., Vickery L.E.;
RT "Interaction of the iron-sulfur cluster assembly protein IscU with the
RT Hsc66/Hsc20 molecular chaperone system of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:7790-7795(2000).
RN [8]
RP CRYSTALLIZATION.
RX PubMed=9300502; DOI=10.1002/pro.5560060923;
RA Cupp-Vickery J.R., Vickery L.E.;
RT "Crystallization and preliminary X-ray crystallographic properties of
RT Hsc20, a J-motif co-chaperone protein from Escherichia coli.";
RL Protein Sci. 6:2028-2030(1997).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=11124030; DOI=10.1006/jmbi.2000.4252;
RA Cupp-Vickery J.R., Vickery L.E.;
RT "Crystal structure of Hsc20, a J-type co-chaperone from Escherichia coli.";
RL J. Mol. Biol. 304:835-845(2000).
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.
CC -!- SUBUNIT: Interacts with HscA and stimulates its ATPase activity.
CC Interacts with IscU.
CC -!- SIMILARITY: Belongs to the HscB family. {ECO:0000305}.
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DR EMBL; U01827; AAA18299.1; -; Unassigned_DNA.
DR EMBL; U00096; AAC75580.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16421.1; -; Genomic_DNA.
DR EMBL; U05338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A36958; A36958.
DR RefSeq; NP_417022.1; NC_000913.3.
DR RefSeq; WP_000384413.1; NZ_STEB01000011.1.
DR PDB; 1FPO; X-ray; 1.80 A; A/B/C=1-171.
DR PDBsum; 1FPO; -.
DR AlphaFoldDB; P0A6L9; -.
DR SMR; P0A6L9; -.
DR BioGRID; 4263037; 42.
DR BioGRID; 851334; 3.
DR DIP; DIP-47847N; -.
DR IntAct; P0A6L9; 21.
DR STRING; 511145.b2527; -.
DR jPOST; P0A6L9; -.
DR PaxDb; P0A6L9; -.
DR PRIDE; P0A6L9; -.
DR EnsemblBacteria; AAC75580; AAC75580; b2527.
DR EnsemblBacteria; BAA16421; BAA16421; BAA16421.
DR GeneID; 60903814; -.
DR GeneID; 946995; -.
DR KEGG; ecj:JW2511; -.
DR KEGG; eco:b2527; -.
DR PATRIC; fig|1411691.4.peg.4207; -.
DR EchoBASE; EB2052; -.
DR eggNOG; COG1076; Bacteria.
DR HOGENOM; CLU_068529_2_0_6; -.
DR InParanoid; P0A6L9; -.
DR OMA; KFMAKLQ; -.
DR PhylomeDB; P0A6L9; -.
DR BioCyc; EcoCyc:EG12131-MON; -.
DR BioCyc; MetaCyc:EG12131-MON; -.
DR EvolutionaryTrace; P0A6L9; -.
DR PRO; PR:P0A6L9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1990230; C:iron-sulfur cluster transfer complex; IDA:EcoCyc.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IEA:InterPro.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IBA:GO_Central.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IDA:EcoCyc.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.20.1280.20; -; 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 PANTHER; PTHR14021; PTHR14021; 1.
DR Pfam; PF07743; HSCB_C; 1.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF47144; SSF47144; 1.
DR TIGRFAMs; TIGR00714; hscB; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Reference proteome.
FT CHAIN 1..171
FT /note="Co-chaperone protein HscB"
FT /id="PRO_0000070966"
FT DOMAIN 2..74
FT /note="J"
FT HELIX 2..6
FT /evidence="ECO:0007829|PDB:1FPO"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:1FPO"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:1FPO"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1FPO"
FT HELIX 41..62
FT /evidence="ECO:0007829|PDB:1FPO"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:1FPO"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1FPO"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1FPO"
FT HELIX 89..108
FT /evidence="ECO:0007829|PDB:1FPO"
FT HELIX 111..137
FT /evidence="ECO:0007829|PDB:1FPO"
FT HELIX 141..165
FT /evidence="ECO:0007829|PDB:1FPO"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:1FPO"
SQ SEQUENCE 171 AA; 20138 MW; 095193EE98AA60C9 CRC64;
MDYFTLFGLP ARYQLDTQAL SLRFQDLQRQ YHPDKFASGS QAEQLAAVQQ SATINQAWQT
LRHPLMRAEY LLSLHGFDLA SEQHTVRDTA FLMEQLELRE ELDEIEQAKD EARLESFIKR
VKKMFDTRHQ LMVEQLDNET WDAAADTVRK LRFLDKLRSS AEQLEEKLLD F
