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Q8KG79 (CLPB1_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Probable chaperone protein ClpB 1
Gene names
Name:clpB1
Ordered Locus Names:CT0089
OrganismChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) [Reference proteome] [HAMAP]
Taxonomic identifier194439 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length438 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK By similarity.

Subunit structure

Homohexamer. The oligomerization is ATP-dependent By similarity.

Subcellular location

Cytoplasm Probable.

Domain

The N-terminal domain probably functions as a substrate-discriminating domain, recruiting aggregated proteins to the ClpB hexamer and/or stabilizing bound proteins. The NBD2 domain is responsible for oligomerization, whereas the NBD1 domain stabilizes the hexamer probably in an ATP-dependent manner. The movement of the coiled-coil domain is essential for ClpB ability to rescue proteins from an aggregated state, probably by pulling apart large aggregated proteins, which are bound between the coiled-coils motifs of adjacent ClpB subunits in the functional hexamer By similarity.

Sequence similarities

Belongs to the clpA/clpB family.

Caution

This protein is much smaller than the orthologs present in other bacteria; the N-terminal and NBD1 domains are missing. However, there is a paralog in the genome (clpB2) that encodes a protein which contains only the N-terminal and NBD1 domains.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleoside-triphosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 438438Probable chaperone protein ClpB 1
PRO_0000191107

Regions

Nucleotide binding178 – 1858ATP Potential
Region1 – 118118Linker By similarity
Region128 – 345218NBD2 By similarity
Region346 – 43893C-terminal By similarity
Coiled coil1 – 9494 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8KG79 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: C19CC552B2EA29FB

FASTA43849,655
        10         20         30         40         50         60 
MNTADTRQRL LDIEKQIASL REEQATVKAQ WEAEKELIHT SRRLKEELED LRVQAENYER 

        70         80         90        100        110        120 
SGDYGKVAEI RYGKIAEIEK ALEENNRKIE ARQASGDLIM KEEIDAGDIA DIVSRWTGIP 

       130        140        150        160        170        180 
VSKMLQSERQ KLLGIESELH RRVVGQDEAV RAVSDAVKRS RAGMGDEKRP IGSFIFLGPT 

       190        200        210        220        230        240 
GVGKTELART LAEYLFDDED ALIRIDMSEY MEAHTVSRLV GAPPGYVGYE EGGQLTEAVR 

       250        260        270        280        290        300 
RKPFSVVLLD EIEKAHPDVF NILLQILDDG RLTDSKGRTV NFKNTIIIMT SNIGAQLIQS 

       310        320        330        340        350        360 
EMEHLEGRDA DAALAGLKEK LFQLLKQQVR PEFLNRIDEV ILFTPLTREN LREIVTIQFN 

       370        380        390        400        410        420 
RIKETARRQR ITLEISDEAL MWLAKTGFDP AFGARPLKRV MQRQITNRLS EMILAGQVGE 

       430 
DDTVEIGLEN DAIVMKKK 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006470 Genomic DNA. Translation: AAM71337.1.
RefSeqNP_660995.1. NC_002932.3.

3D structure databases

ProteinModelPortalQ8KG79.
ModBaseSearch...

Protein-protein interaction databases

STRING194439.CT0089.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM71337; AAM71337; CT0089.
GeneID1006510.
KEGGcte:CT0089.
PATRIC21398281. VBIChlTep116050_0089.

Phylogenomic databases

eggNOGCOG0542.
HOGENOMHOG000218211.
OMAKRSRAGM.
ProtClustDBCLSK637153.

Enzyme and pathway databases

BioCycCTEP194439:GHN0-90-MONOMER.

Family and domain databases

InterProIPR003593. AAA+_ATPase.
IPR013093. ATPase_AAA-2.
IPR001270. Chaprnin_ClpA/B.
IPR019489. Clp_ATPase_C.
[Graphical view]
PfamPF07724. AAA_2. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
PRINTSPR00300. CLPPROTEASEA.
SMARTSM00382. AAA. 1 hit.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
PROSITEPS00870. CLPAB_1. False negative.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPB1_CHLTE
AccessionPrimary (citable) accession number: Q8KG79
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 1, 2002
Last modified: May 1, 2013
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families