Reviewed, UniProtKB/Swiss-Prot P0A6Z1 (HSCA_ECOLI)

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) [Complete proteome] [HAMAP]

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
Gene Ontology (GO)
Biological process	iron-sulfur cluster assembly Inferred from electronic annotation. Source: InterPro protein folding Inferred from electronic annotation. Source: HAMAP response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity Inferred from electronic annotation. Source: HAMAP 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

1

S → F in hsca1.

Experimental info

Sequence conflict

456 – 465

10

LRGIPALPAG → CVVFRRYRLA in AAA18300. Ref.1

Sequence conflict

516

1

S → T in AAA18300. Ref.1

Sequence conflict

557

1

Missing in AAA18300. Ref.1

Sequence conflict

583

1

Q → K in AAD13473. Ref.2

Secondary structure

1

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616

Helix Strand Turn

Details...

Beta strand

396 – 400

5

Turn

401 – 403

3

Beta strand

404 – 409

6

Beta strand

414 – 424

11

Beta strand

433 – 439

7

Beta strand

441 – 444

4

Helix

445 – 447

3

Beta strand

448 – 456

9

Beta strand

469 – 475

7

Beta strand

481 – 487

7

Turn

488 – 490

3

Beta strand

493 – 498

6

Helix

506 – 518

13

Helix

520 – 550

31

Helix

551 – 553

3

Helix

556 – 572

17

Helix

578 – 609

32

Sequences

	Sequence		Length	Mass (Da)
	P0A6Z1-1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 9C80E6EF1BFDAB48	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

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. , 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: 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

AP_003112.1.
NP_417021.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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

SMR

P0A6Z1. Positions 21-581.

ModBase

Search...

Protein-protein interaction databases

STRING

P0A6Z1.

Genome annotation databases

GeneID

944885.

GenomeReviews

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

KEGG

ecj:JW2510.
eco:b2526.

Organism-specific databases

EchoBASE

EB2051.

EcoGene

EG12130. hscA.

CMR

Search...

Phylogenomic databases

eggNOG

COG0443.

HOGENOM

HBG334976.

OMA

KSTGVQS.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12130-MONOMER.
ECOL168927:B2526-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]

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:	February 9, 2010
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)