Chaperone protein hscA - Escherichia coli (strain K12)

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P0A6Z1 (HSCA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 61. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Chaperone protein hscA

Alternative name(s):
Hsc66

Gene names

Name:	hscA
Synonyms:	hsc
Ordered Locus Names:	b2526, JW2510

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	616 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Chaperone involved in the maturation of iron-sulfur cluster-containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by hscB. Involved in the maturation of iscU. HAMAP MF_00679
Induction	By cold shock. Ref.6
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Stress response
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cellular response to cold Inferred from expression pattern Ref.6. Source: EcoCyc iron-sulfur cluster assembly Inferred from mutant phenotype. Source: EcoCyc protein folding Inferred from electronic annotation. Source: InterPro
Molecular function	ADP binding Inferred from direct assay. Source: EcoCyc ATP binding Inferred from direct assay. Source: EcoCyc ATPase activity Inferred from direct assay. Source: EcoCyc unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 616

616

Chaperone protein hscA HAMAP MF_00679

PRO_0000078625

Natural variations

Natural variant

216

S → F in hsca1.

Experimental info

Sequence conflict

456 – 465

LRGIPALPAG → CVVFRRYRLA in AAA18300. Ref.1

Sequence conflict

516

S → T in AAA18300. Ref.1

Sequence conflict

557

Missing in AAA18300. Ref.1

Sequence conflict

583

Q → K in AAD13473. Ref.2

Secondary structure

616

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A6Z1 [UniParc].

Last modified June 7, 2005. Version 1.
Checksum: 9C80E6EF1BFDAB48
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FASTA

616

65,652

        10         20         30         40         50         60 
MALLQISEPG LSAAPHQRRL AAGIDLGTTN SLVATVRSGQ AETLADHEGR HLLPSVVHYQ 

        70         80         90        100        110        120 
QQGHSVGYDA RTNAALDTAN TISSVKRLMG RSLADIQQRY PHLPYQFQAS ENGLPMIETA 

       130        140        150        160        170        180 
AGLLNPVRVS ADILKALAAR ATEALAGELD GVVITVPAYF DDAQRQGTKD AARLAGLHVL 

       190        200        210        220        230        240 
RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDISILRL SRGVFEVLAT GGDSALGGDD 

       250        260        270        280        290        300 
FDHLLADYIR EQAGIPDRSD NRVQRELLDA AIAAKIALSD ADSVTVNVAG WQGEISREQF 

       310        320        330        340        350        360 
NELIAPLVKR TLLACRRALK DAGVEADEVL EVVMVGGSTR VPLVRERVGE FFGRPPLTSI 

       370        380        390        400        410        420 
DPDKVVAIGA AIQADILVGN KPDSEMLLLD VIPLSLGLET MGGLVEKVIP RNTTIPVARA 

       430        440        450        460        470        480 
QDFTTFKDGQ TAMSIHVMQG ERELVQDCRS LARFALRGIP ALPAGGAHIR VTFQVDADGL 

       490        500        510        520        530        540 
LSVTAMEKST GVEASIQVKP SYGLTDSEIA SMIKDSMSYA EQDVKARMLA EQKVEAARVL 

       550        560        570        580        590        600 
ESLHGALAAD AALLSAAERQ VIDDAAAHLS EVAQGDDVDA IEQAIKNVDK QTQDFAARRM 

       610 
DQSVRRALKG HSVDEV

« Hide

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: 8300516] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"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: 8134349] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: B.
[3]	"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. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Hsc66, an Hsp70 homolog in Escherichia coli, is induced by cold shock but not by heat shock." Lelivelt M.J., Kawula T.H. J. Bacteriol. 177:4900-4907(1995) [PubMed: 7665466] [Abstract] Cited for: INDUCTION.
[7]	"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: 9144776] [Abstract] Cited for: CHARACTERIZATION.
[8]	"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: 10869428] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U01827 Unassigned DNA. Translation: AAA18300.1.
U05338 Genomic DNA. Translation: AAD13473.1.
U00096 Genomic DNA. Translation: AAC75579.1.
AP009048 Genomic DNA. Translation: BAA16420.1.

PIR

E65029.

RefSeq

NP_417021.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U00	X-ray	1.95	A	390-615	[»]

ProteinModelPortal

P0A6Z1.

SMR

P0A6Z1. Positions 20-615.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47348N.

IntAct

P0A6Z1. 28 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001032; EBESCP00000001032; EBESCG00000000851.
EBESCT00000001033; EBESCP00000001033; EBESCG00000000851.
EBESCT00000014956; EBESCP00000014247; EBESCG00000014016.

GeneID

944885.

GenomeReviews

Gene locus JW2510 in contig AP009048_GR.
Gene locus b2526 in contig U00096_GR.

KEGG

ecj:JW2510.
eco:b2526.

PATRIC

32120447. VBIEscCol129921_2626.

Organism-specific databases

EchoBASE

EB2051.

EcoGene

EG12130. hscA.

Phylogenomic databases

eggNOG

COG0443.

GeneTree

EBGT00050000009550.

HOGENOM

HBG334976.

OMA

KSTGVQS.

PhylomeDB

P0A6Z1.

ProtClustDB

PRK05183.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12130-MONOMER.
MetaCyc:EG12130-MONOMER.

Gene expression databases

Genevestigator

P0A6Z1.

Family and domain databases

HAMAP

MF_00679. HscA.
[Tree]

InterPro

IPR018181. Heat_shock_70_CS.
IPR001023. Hsp70.
IPR013126. Hsp_70.
IPR010236. ISC_FeS_clus_asmbl_HscA.
[Graphical view]

K04044.

PANTHER

PTHR19375. Hsp70. 1 hit.

Pfam

PF00012. HSP70. 1 hit.
[Graphical view]

PRINTS

PR00301. HEATSHOCK70.

TIGRFAMs

TIGR01991. HscA. 1 hit.

PROSITE

PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

HSCA_ECOLI

Accession

Primary (citable) accession number: P0A6Z1
Secondary accession number(s): P36541, P76990, P77497

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	January 25, 2012
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents