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Protein

33 kDa chaperonin

Gene

hslO

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 2 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.UniRule annotation

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU00710-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
33 kDa chaperoninUniRule annotation
Alternative name(s):
Heat shock protein 33 homologUniRule annotation
Short name:
HSP33UniRule annotation
Gene namesi
Name:hslOUniRule annotation
Synonyms:yacC
Ordered Locus Names:BSU00710
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001921671 – 29133 kDa chaperoninAdd BLAST291

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi235 ↔ 237Redox-activeUniRule annotation
Disulfide bondi268 ↔ 271Redox-activeUniRule annotation

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.UniRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP37565.
PRIDEiP37565.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100000360.

Structurei

Secondary structure

1291
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Turni10 – 13Combined sources4
Beta strandi14 – 20Combined sources7
Helixi22 – 32Combined sources11
Helixi36 – 53Combined sources18
Beta strandi61 – 67Combined sources7
Beta strandi74 – 80Combined sources7
Beta strandi83 – 90Combined sources8
Helixi106 – 110Combined sources5
Beta strandi112 – 121Combined sources10
Beta strandi126 – 133Combined sources8
Beta strandi135 – 139Combined sources5
Helixi140 – 151Combined sources12
Beta strandi155 – 163Combined sources9
Beta strandi169 – 179Combined sources11
Helixi185 – 195Combined sources11
Helixi201 – 207Combined sources7
Helixi211 – 219Combined sources9
Beta strandi224 – 230Combined sources7
Helixi239 – 247Combined sources9
Helixi251 – 261Combined sources11
Beta strandi262 – 267Combined sources6
Turni269 – 271Combined sources3
Beta strandi274 – 278Combined sources5
Helixi279 – 288Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VZYX-ray1.97A/B1-291[»]
ProteinModelPortaliP37565.
SMRiP37565.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37565.

Family & Domainsi

Sequence similaritiesi

Belongs to the HSP33 family.UniRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105F4C. Bacteria.
COG1281. LUCA.
HOGENOMiHOG000261703.
InParanoidiP37565.
KOiK04083.
OMAiIVCQFCQ.
PhylomeDBiP37565.

Family and domain databases

CDDicd00498. Hsp33. 1 hit.
Gene3Di3.55.30.10. 1 hit.
3.90.1280.10. 1 hit.
HAMAPiMF_00117. HslO. 1 hit.
InterProiIPR000397. Heat_shock_Hsp33.
IPR016154. Heat_shock_Hsp33_C.
IPR016153. Heat_shock_Hsp33_N.
[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.

P37565-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYLVKALAY DGKVRAYAAR TTDMVNEGQR RHGTWPTASA ALGRTMTASL
60 70 80 90 100
MLGAMLKGDD KLTVKIEGGG PIGAIVADAN AKGEVRAYVS NPQVHFDLNE
110 120 130 140 150
QGKLDVRRAV GTNGTLSVVK DLGLREFFTG QVEIVSGELG DDFTYYLVSS
160 170 180 190 200
EQVPSSVGVG VLVNPDNTIL AAGGFIIQLM PGTDDETITK IEQRLSQVEP
210 220 230 240 250
ISKLIQKGLT PEEILEEVLG EKPEILETMP VRFHCPCSKE RFETAILGLG
260 270 280 290
KKEIQDMIEE DGQAEAVCHF CNEKYLFTKE ELEGLRDQTT R
Length:291
Mass (Da):31,811
Last modified:October 1, 1994 - v1
Checksum:i194F742BC0946DD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26185 Genomic DNA. Translation: BAA05306.1.
AL009126 Genomic DNA. Translation: CAB11847.1.
PIRiS66101.
RefSeqiNP_387952.1. NC_000964.3.
WP_003226695.1. NZ_JNCM01000028.1.

Genome annotation databases

EnsemblBacteriaiCAB11847; CAB11847; BSU00710.
GeneIDi936762.
KEGGibsu:BSU00710.
PATRICi18971617. VBIBacSub10457_0072.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26185 Genomic DNA. Translation: BAA05306.1.
AL009126 Genomic DNA. Translation: CAB11847.1.
PIRiS66101.
RefSeqiNP_387952.1. NC_000964.3.
WP_003226695.1. NZ_JNCM01000028.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VZYX-ray1.97A/B1-291[»]
ProteinModelPortaliP37565.
SMRiP37565.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100000360.

Proteomic databases

PaxDbiP37565.
PRIDEiP37565.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB11847; CAB11847; BSU00710.
GeneIDi936762.
KEGGibsu:BSU00710.
PATRICi18971617. VBIBacSub10457_0072.

Phylogenomic databases

eggNOGiENOG4105F4C. Bacteria.
COG1281. LUCA.
HOGENOMiHOG000261703.
InParanoidiP37565.
KOiK04083.
OMAiIVCQFCQ.
PhylomeDBiP37565.

Enzyme and pathway databases

BioCyciBSUB:BSU00710-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP37565.

Family and domain databases

CDDicd00498. Hsp33. 1 hit.
Gene3Di3.55.30.10. 1 hit.
3.90.1280.10. 1 hit.
HAMAPiMF_00117. HslO. 1 hit.
InterProiIPR000397. Heat_shock_Hsp33.
IPR016154. Heat_shock_Hsp33_C.
IPR016153. Heat_shock_Hsp33_N.
[Graphical view]
PfamiPF01430. HSP33. 1 hit.
[Graphical view]
PIRSFiPIRSF005261. Heat_shock_Hsp33. 1 hit.
SUPFAMiSSF118352. SSF118352. 1 hit.
SSF64397. SSF64397. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiHSLO_BACSU
AccessioniPrimary (citable) accession number: P37565
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 2, 2016
This is version 111 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. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  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.