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Reviewed, UniProtKB/Swiss-Prot Q83F55 (CLPB_COXBU)

Last modified July 22, 2008. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Chaperone protein clpB
Gene names
Name: clpB
Ordered Locus Names: CBU_0094
OrganismCoxiella burnetii [Complete proteome] [HAMAP]
Taxonomic identifier777 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella

Protein attributes

Sequence length859 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

CytoplasmProbable.

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.

Ontologies

Keywords

   Biological processStress response
   Cellular componentCytoplasm
   DomainCoiled coil
Repeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   Technical termComplete proteome

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Chain1 – 859859Chaperone protein clpB

Regions

Nucleotide binding206 – 2138ATP 1 By similarity
Nucleotide binding607 – 6148ATP 2 By similarity
Region1 – 143143N-terminal By similarity
Region159 – 340182NBD1 By similarity
Region341 – 547207Linker By similarity
Region557 – 766210NBD2 By similarity
Region767 – 85993C-terminal By similarity
Coiled coil391 – 525135 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83F55-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D0D834A1F973197D

FASTA85996,769
        10         20         30         40         50         60 
MRIDKFTTAF QTALADAQSL AVGRDHQFIE PAHVMKVLLE QTQGTVAPLL EQSKVNLSRL 

        70         80         90        100        110        120 
IDGVNKAIDS YPQVEGTGGE VHVSRELSKI LTLMDKFAQQ NKDQYISSEW FIPAALEAKG 

       130        140        150        160        170        180 
QLRDVLIEAG ADKKAIEKNI MNLRKGERVT EQSAEDQRQA LAKYTIDLTE KAETGKLDPV 

       190        200        210        220        230        240 
IGRDEEIRRT VQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIVNGEVPE GLKQKRLLAL 

       250        260        270        280        290        300 
DMGALIAGAK FRGEFEERLK AVLKDIAKEE GRVILFIDEL HTMVGAGKAE GAMDAGNMLK 

       310        320        330        340        350        360 
PALARGELHC VGATTLDEYR KYIEKDAALE RRFQKVLVEE PSTEDAIAIL RGLKERYEVH 

       370        380        390        400        410        420 
HGVEITDPAI IAAATLSQRY ITDRNLPDKA IDLIDEAASQ IRMEMDSKPV ELDRLERRLI 

       430        440        450        460        470        480 
QLKIEREALK KETDEASKKR LSDLETEIKN VEKEYSDLEE VWKSEKASLH GTQQIKEELE 

       490        500        510        520        530        540 
QARIELEAAG RAGDLARMSE LQYGIIPELD KKLKAASQKE EQFHDHKLLR SRVTEEEVAE 

       550        560        570        580        590        600 
VVSKWTHIPV SKMLEGEREK LLHMETELHK RVIGQDEAVN AVANAIRRSR AGLSDPNRPV 

       610        620        630        640        650        660 
GSFLFLGPTG VGKTELCKAL AVFLFDTEDA MVRIDMSEFM EKHSVARLIG APPGYVGYEE 

       670        680        690        700        710        720 
GGYLTEAIRR RPYSVILLDE IEKAHNDVFN VLLQVLDDGR LTDGQGRTVD FRNTVIVMTS 

       730        740        750        760        770        780 
NLGSDLIREF SGENYDKMKD AVMEVVAQHF RPEFINRIDE AVVFHSLKKE QIRNIAIIQI 

       790        800        810        820        830        840 
DRIKKRLKEK DYQLTISDDA LDYLSELGYD PVYGARPLKR VLQQQLENPL SQKILEGKFV 

       850 
PGSLINIEKK GEQLEFKEA 

« Hide

Cross-references

Sequence databases

AE016828 Genomic DNA. Translation: AAO89660.1.
RefSeqNP_819146.1.

3D structure databases

HSSPHSSP built from PDB template 1JBK based on UniProtKB P03815.
ModBaseSearch...

Genome annotation databases

GeneID1207964.
GenomeReviewsGene locus CBU_0094 in contig AE016828_GR.
KEGGcbu:CBU_0094.
NMPDRfig|227377.1.peg.90.
TIGRCBU_0094.

Phylogenomic databases

HOGENOMQ83F55.

Enzyme and pathway databases

BioCycCBUR227377:CBU_0094-MON.

Family and domain databases

InterProIPR003593. AAA+_ATPase_core.
IPR003959. AAA_ATPase_core.
IPR013093. ATPase_AAA-2.
IPR017730. Chaperonin_ClpB.
IPR001270. Chaprnin_clpA/B.
IPR004176. Clp_N.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
[Graphical view]
PRINTSPR00300. CLPPROTEASEA.
SMARTSM00382. AAA. 2 hits.
[Graphical view]
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProDomQ83F55.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

Entry information

Entry nameCLPB_COXBU
AccessionPrimary (citable) accession number: Q83F55
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: June 1, 2003
Last modified: July 22, 2008
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Coxiella burnetii

Coxiella burnetii (strain RSA 493): entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents