P0A6L9 (HSCB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Co-chaperone protein HscB

Alternative name(s):
Hsc20

Gene names

Name:	hscB
Synonyms:	yfhE
Ordered Locus Names:	b2527, JW2511

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	171 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Co-chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Seems to help targeting proteins to be folded toward HscA. HAMAP-Rule MF_00682
Subunit structure	Interacts with HscA and stimulates its ATPase activity. Interacts with IscU.
Sequence similarities	Belongs to the HscB family. Contains 1 J domain.

Ontologies

Keywords
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein folding Inferred from electronic annotation. Source: HAMAP protein oligomerization Inferred from electronic annotation. Source: InterPro
Molecular_function	chaperone binding Inferred from direct assay Ref.6. Source: EcoCyc heat shock protein binding Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 171

171

Co-chaperone protein HscB HAMAP-Rule MF_00682

PRO_0000070966

Regions

Domain

2 – 74

73

J

Secondary structure

1

.

.

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.

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.

.

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171

Helix Strand Turn

Details...

Helix

2 – 6

5

Beta strand

11 – 13

3

Helix

17 – 30

14

Helix

33 – 36

4

Helix

41 – 62

22

Helix

64 – 73

10

Turn

74 – 76

3

Beta strand

82 – 84

3

Helix

89 – 108

20

Helix

111 – 137

27

Helix

141 – 165

25

Turn

166 – 169

4

Sequences

	Sequence		Length	Mass (Da)
	P0A6L9 [UniParc]. Last modified May 10, 2005. Version 1. Checksum: 095193EE98AA60C9	FASTA	171	20,138
	10 20 30 40 50 60 MDYFTLFGLP ARYQLDTQAL SLRFQDLQRQ YHPDKFASGS QAEQLAAVQQ SATINQAWQT 70 80 90 100 110 120 LRHPLMRAEY LLSLHGFDLA SEQHTVRDTA FLMEQLELRE ELDEIEQAKD EARLESFIKR 130 140 150 160 170 VKKMFDTRHQ LMVEQLDNET WDAAADTVRK LRFLDKLRSS AEQLEEKLLD F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mutations in a gene encoding a new Hsp70 suppress rapid DNA inversion and bgl activation, but not proU derepression, in hns-1 mutant Escherichia coli." Kawula T.H., Lelivelt M.J. J. Bacteriol. 176:610-619(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"A gene encoding a DnaK/hsp70 homolog in Escherichia coli." Seaton B.L., Vickery L.E. Proc. Natl. Acad. Sci. U.S.A. 91:2066-2070(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 119-171. Strain: B.
[6]	"Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli." Vickery L.E., Silberg J.J., Ta D.T. Protein Sci. 6:1047-1056(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[7]	"Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli." Hoff K.G., Silberg J.J., Vickery L.E. Proc. Natl. Acad. Sci. U.S.A. 97:7790-7795(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[8]	"Crystallization and preliminary X-ray crystallographic properties of Hsc20, a J-motif co-chaperone protein from Escherichia coli." Cupp-Vickery J.R., Vickery L.E. Protein Sci. 6:2028-2030(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION.
[9]	"Crystal structure of Hsc20, a J-type co-chaperone from Escherichia coli." Cupp-Vickery J.R., Vickery L.E. J. Mol. Biol. 304:835-845(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U01827 Unassigned DNA. Translation: AAA18299.1.
U00096 Genomic DNA. Translation: AAC75580.1.
AP009048 Genomic DNA. Translation: BAA16421.1.
U05338 Genomic DNA. No translation available.

PIR

A36958.

RefSeq

NP_417022.1. NC_000913.2.
YP_490755.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FPO	X-ray	1.80	A/B/C	1-171	[»]

ProteinModelPortal

P0A6L9.

SMR

P0A6L9. Positions 1-171.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47847N.

IntAct

P0A6L9. 18 interactions.

STRING

511145.b2527.

Proteomic databases

PaxDb

P0A6L9.

PRIDE

P0A6L9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75580; AAC75580; b2527.
BAA16421; BAA16421; BAA16421.

GeneID

12934043.
946995.

KEGG

ecj:Y75_p2480.
eco:b2527.

PATRIC

32120449. VBIEscCol129921_2627.

Organism-specific databases

EchoBASE

EB2052.

EcoGene

EG12131. hscB.

Phylogenomic databases

eggNOG

COG1076.

HOGENOM

HOG000262077.

KO

K04082.

OMA

LMRRMQF.

ProtClustDB

PRK05014.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12131-MONOMER.
ECOL316407:JW2511-MONOMER.

Gene expression databases

Genevestigator

P0A6L9.

Family and domain databases

Gene3D

1.10.287.110. 1 hit.
1.20.1280.20. 1 hit.

HAMAP

MF_00682. HscB.

InterPro

IPR001623. DnaJ_domain.
IPR004640. HscB.
IPR009073. HscB_oligo_C.
[Graphical view]

PANTHER

PTHR14021. PTHR14021. 1 hit.

Pfam

PF00226. DnaJ. 1 hit.
PF07743. HSCB_C. 1 hit.
[Graphical view]

SMART

SM00271. DnaJ. 1 hit.
[Graphical view]

SUPFAM

SSF46565. DnaJ_N. 1 hit.
SSF47144. HSC20_C. 1 hit.

TIGRFAMs

TIGR00714. hscB. 1 hit.

PROSITE

PS00636. DNAJ_1. False negative.
PS50076. DNAJ_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A6L9.

Entry information

Entry name

HSCB_ECOLI

Accession

Primary (citable) accession number: P0A6L9
Secondary accession number(s): P36540

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program