P0A6Y5 (HSLO_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
33 kDa chaperonin

Alternative name(s):
Heat shock protein 33
Short name=HSP33

Gene names

Name:	hslO
Synonyms:	yrfI
Ordered Locus Names:	b3401, JW5692

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	292 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. HAMAP MF_00117
Subcellular location	Cytoplasm HAMAP MF_00117.
Induction	By heat shock. HAMAP MF_00117
Post-translational modification	Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive. HAMAP MF_00117
Sequence similarities	Belongs to the HSP33 family.
Sequence caution	The sequence AAA58198.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	Zinc
Molecular function	Chaperone
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: InterPro response to heat Inferred from expression pattern. Source: EcoliWiki
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
tufA	P0CE47	2	EBI-562857,EBI-301077

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 292

292

33 kDa chaperonin HAMAP MF_00117

PRO_0000192174

Amino acid modifications

Disulfide bond

230 ↔ 232

Redox-active Ref.4

Disulfide bond

263 ↔ 266

Redox-active Ref.4

Secondary structure

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292

Helix Strand Turn

Details...

Beta strand

6 – 12

7

Turn

13 – 16

4

Beta strand

17 – 23

7

Helix

25 – 32

8

Helix

39 – 56

18

Beta strand

60 – 75

16

Beta strand

77 – 83

7

Beta strand

87 – 93

7

Helix

104 – 108

5

Beta strand

110 – 122

13

Beta strand

125 – 131

7

Beta strand

133 – 135

3

Helix

136 – 147

12

Beta strand

152 – 161

10

Beta strand

164 – 174

11

Helix

182 – 193

12

Helix

197 – 202

6

Helix

205 – 213

9

Beta strand

218 – 220

3

Helix

234 – 242

9

Helix

246 – 256

11

Beta strand

257 – 262

6

Turn

264 – 266

3

Beta strand

269 – 273

5

Helix

274 – 280

7

Turn

281 – 283

3

Sequences

	Sequence		Length	Mass (Da)
	P0A6Y5 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 18F05BD2F0257552	FASTA	292	32,534
	10 20 30 40 50 60 MPQHDQLHRY LFENFAVRGE LVTVSETLQQ ILENHDYPQP VKNVLAELLV ATSLLTATLK 70 80 90 100 110 120 FDGDITVQLQ GDGPMNLAVI NGNNNQQMRG VARVQGEIPE NADLKTLVGN GYVVITITPS 130 140 150 160 170 180 EGERYQGVVG LEGDTLAACL EDYFMRSEQL PTRLFIRTGD VDGKPAAGGM LLQVMPAQNA 190 200 210 220 230 240 QQDDFDHLAT LTETIKTEEL LTLPANEVLW RLYHEEEVTV YDPQDVEFKC TCSRERCADA 250 260 270 280 290 LKTLPDEEVD SILAEDGEID MHCDYCGNHY LFNAMDIAEI RNNASPADPQ VH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	"Chaperone activity with a redox switch." Jakob U., Muse W., Eser M., Bardwell J.C.A. Cell 96:341-352(1999) [PubMed: 10025400] [Abstract] Cited for: CHARACTERIZATION.
[4]	"Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone." Barbirz S., Jakob U., Glocker M.O. J. Biol. Chem. 275:18759-18766(2000) [PubMed: 10764757] [Abstract] Cited for: DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U18997 Genomic DNA. Translation: AAA58198.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76426.2.
AP009048 Genomic DNA. Translation: BAE77890.1.

PIR

D65135.

RefSeq

NP_417860.2. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HW7	X-ray	2.20	A	1-253	[»]
1I7F	X-ray	2.70	A	1-292	[»]
1XJH	NMR	-	A	225-285	[»]
3M7M	X-ray	2.90	X	1-233	[»]

ProteinModelPortal

P0A6Y5.

SMR

P0A6Y5. Positions 4-285.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48013N.

IntAct

P0A6Y5. 10 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000002752; EBESCP00000002752; EBESCG00000002243.
EBESCT00000015206; EBESCP00000014497; EBESCG00000014266.

GeneID

947178.

GenomeReviews

Gene locus JW5692 in contig AP009048_GR.
Gene locus b3401 in contig U00096_GR.

KEGG

ecj:JW5692.
eco:b3401.

PATRIC

32122236. VBIEscCol129921_3495.

Organism-specific databases

EchoBASE

EB2766.

EcoGene

EG12930. hslO.

Phylogenomic databases

eggNOG

COG1281.

GeneTree

EBGT00050000009037.

HOGENOM

HBG296531.

OMA

AMTIDQG.

PhylomeDB

P0A6Y5.

ProtClustDB

PRK00114.

Enzyme and pathway databases

BioCyc

EcoCyc:G7744-MONOMER.

Gene expression databases

Genevestigator

P0A6Y5.

Family and domain databases

HAMAP

MF_00117. HslO.
[Tree]

InterPro

IPR000397. Heat_shock_Hsp33.
IPR016154. Heat_shock_Hsp33_C.
IPR016153. Heat_shock_Hsp33_N.
IPR023212. Hsp33_helix_hairpin_bin_dom.
[Graphical view]

Gene3D

G3DSA:3.90.1280.10. Heat_shock_Hsp33_C. 1 hit.
G3DSA:3.55.30.10. Heat_shock_Hsp33_N. 1 hit.
G3DSA:1.10.287.480. Hsp33_helix_hairpin_bin_dom. 1 hit.

KO

K04083.

Pfam

PF01430. HSP33. 1 hit.
[Graphical view]

PIRSF

PIRSF005261. Heat_shock_Hsp33. 1 hit.

SUPFAM

SSF64397. Heat_shock_Hsp33_N. 1 hit.
SSF118352. SSF118352. 1 hit.

ProtoNet

Search...

Entry information

Entry name

HSLO_ECOLI

Accession

Primary (citable) accession number: P0A6Y5
Secondary accession number(s): P45803, Q2M766

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	January 25, 2012
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program