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Protein

33 kDa chaperonin

Gene

hslO

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

  • protein folding Source: InterPro
  • response to heat Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

Zinc

Enzyme and pathway databases

BioCyciEcoCyc:G7744-MONOMER.
ECOL316407:JW5692-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
33 kDa chaperoninUniRule annotation
Alternative name(s):
Heat shock protein 33
Short name:
HSP33UniRule annotation
Gene namesi
Name:hslOUniRule annotation
Synonyms:yrfI
Ordered Locus Names:b3401, JW5692
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12930. hslO.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 29229233 kDa chaperoninPRO_0000192174Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi230 ↔ 232Redox-activeUniRule annotation1 Publication
Disulfide bondi263 ↔ 266Redox-activeUniRule annotation1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP0A6Y5.
PaxDbiP0A6Y5.
PRIDEiP0A6Y5.

Expressioni

Inductioni

By heat shock.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-562857,EBI-562857
tufAP0CE472EBI-562857,EBI-301077

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4262486. 6 interactions.
DIPiDIP-48013N.
IntActiP0A6Y5. 10 interactions.
MINTiMINT-8302273.
STRINGi511145.b3401.

Structurei

Secondary structure

1
292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Turni13 – 164Combined sources
Beta strandi17 – 237Combined sources
Helixi25 – 328Combined sources
Helixi39 – 5618Combined sources
Beta strandi60 – 7516Combined sources
Beta strandi77 – 837Combined sources
Beta strandi88 – 936Combined sources
Helixi104 – 1085Combined sources
Beta strandi110 – 12213Combined sources
Beta strandi125 – 1317Combined sources
Beta strandi133 – 1353Combined sources
Helixi136 – 14712Combined sources
Beta strandi152 – 16110Combined sources
Beta strandi164 – 17411Combined sources
Turni176 – 1794Combined sources
Helixi182 – 19312Combined sources
Helixi197 – 2026Combined sources
Helixi205 – 2139Combined sources
Beta strandi218 – 2203Combined sources
Helixi234 – 2429Combined sources
Helixi246 – 25611Combined sources
Beta strandi257 – 2626Combined sources
Turni264 – 2663Combined sources
Beta strandi269 – 2735Combined sources
Helixi274 – 2807Combined sources
Turni281 – 2833Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HW7X-ray2.20A1-253[»]
1I7FX-ray2.70A1-292[»]
1XJHNMR-A225-285[»]
3M7MX-ray2.90X1-233[»]
ProteinModelPortaliP0A6Y5.
SMRiP0A6Y5. Positions 4-285.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A6Y5.

Family & Domainsi

Sequence similaritiesi

Belongs to the HSP33 family.UniRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105F4C. Bacteria.
COG1281. LUCA.
HOGENOMiHOG000261998.
InParanoidiP0A6Y5.
KOiK04083.
OMAiIVCQFCQ.
OrthoDBiEOG651SSJ.
PhylomeDBiP0A6Y5.

Family and domain databases

Gene3Di1.10.287.480. 1 hit.
3.55.30.10. 1 hit.
3.90.1280.10. 1 hit.
HAMAPiMF_00117. HslO.
InterProiIPR000397. Heat_shock_Hsp33.
IPR016154. Heat_shock_Hsp33_C.
IPR016153. Heat_shock_Hsp33_N.
IPR023212. Hsp33_helix_hairpin_bin_dom.
[Graphical view]
PfamiPF01430. HSP33. 1 hit.
[Graphical view]
PIRSFiPIRSF005261. Heat_shock_Hsp33. 1 hit.
SUPFAMiSSF118352. SSF118352. 1 hit.
SSF64397. SSF64397. 1 hit.

Sequencei

Sequence statusi: Complete.

P0A6Y5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPQHDQLHRY LFENFAVRGE LVTVSETLQQ ILENHDYPQP VKNVLAELLV
60 70 80 90 100
ATSLLTATLK FDGDITVQLQ GDGPMNLAVI NGNNNQQMRG VARVQGEIPE
110 120 130 140 150
NADLKTLVGN GYVVITITPS EGERYQGVVG LEGDTLAACL EDYFMRSEQL
160 170 180 190 200
PTRLFIRTGD VDGKPAAGGM LLQVMPAQNA QQDDFDHLAT LTETIKTEEL
210 220 230 240 250
LTLPANEVLW RLYHEEEVTV YDPQDVEFKC TCSRERCADA LKTLPDEEVD
260 270 280 290
SILAEDGEID MHCDYCGNHY LFNAMDIAEI RNNASPADPQ VH
Length:292
Mass (Da):32,534
Last modified:June 7, 2005 - v1
Checksum:i18F05BD2F0257552
GO

Sequence cautioni

The sequence AAA58198.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA58198.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76426.2.
AP009048 Genomic DNA. Translation: BAE77890.1.
PIRiD65135.
RefSeqiNP_417860.2. NC_000913.3.
WP_001135574.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76426; AAC76426; b3401.
BAE77890; BAE77890; BAE77890.
GeneIDi947178.
KEGGiecj:JW5692.
eco:b3401.
PATRICi32122236. VBIEscCol129921_3495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18997 Genomic DNA. Translation: AAA58198.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76426.2.
AP009048 Genomic DNA. Translation: BAE77890.1.
PIRiD65135.
RefSeqiNP_417860.2. NC_000913.3.
WP_001135574.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HW7X-ray2.20A1-253[»]
1I7FX-ray2.70A1-292[»]
1XJHNMR-A225-285[»]
3M7MX-ray2.90X1-233[»]
ProteinModelPortaliP0A6Y5.
SMRiP0A6Y5. Positions 4-285.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262486. 6 interactions.
DIPiDIP-48013N.
IntActiP0A6Y5. 10 interactions.
MINTiMINT-8302273.
STRINGi511145.b3401.

Proteomic databases

EPDiP0A6Y5.
PaxDbiP0A6Y5.
PRIDEiP0A6Y5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76426; AAC76426; b3401.
BAE77890; BAE77890; BAE77890.
GeneIDi947178.
KEGGiecj:JW5692.
eco:b3401.
PATRICi32122236. VBIEscCol129921_3495.

Organism-specific databases

EchoBASEiEB2766.
EcoGeneiEG12930. hslO.

Phylogenomic databases

eggNOGiENOG4105F4C. Bacteria.
COG1281. LUCA.
HOGENOMiHOG000261998.
InParanoidiP0A6Y5.
KOiK04083.
OMAiIVCQFCQ.
OrthoDBiEOG651SSJ.
PhylomeDBiP0A6Y5.

Enzyme and pathway databases

BioCyciEcoCyc:G7744-MONOMER.
ECOL316407:JW5692-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0A6Y5.
PROiP0A6Y5.

Family and domain databases

Gene3Di1.10.287.480. 1 hit.
3.55.30.10. 1 hit.
3.90.1280.10. 1 hit.
HAMAPiMF_00117. HslO.
InterProiIPR000397. Heat_shock_Hsp33.
IPR016154. Heat_shock_Hsp33_C.
IPR016153. Heat_shock_Hsp33_N.
IPR023212. Hsp33_helix_hairpin_bin_dom.
[Graphical view]
PfamiPF01430. HSP33. 1 hit.
[Graphical view]
PIRSFiPIRSF005261. Heat_shock_Hsp33. 1 hit.
SUPFAMiSSF118352. SSF118352. 1 hit.
SSF64397. SSF64397. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.

Entry informationi

Entry nameiHSLO_ECOLI
AccessioniPrimary (citable) accession number: P0A6Y5
Secondary accession number(s): P45803, Q2M766
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 7, 2005
Last modified: March 16, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.