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O67588 (CLPB_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chaperone protein ClpB
Gene names
Name:clpB
Ordered Locus Names:aq_1672
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length1006 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.

Contains 1 UVR domain.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
   DomainCoiled coil
Repeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein metabolic process

Inferred from electronic annotation. Source: InterPro

response 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 – 10061006Chaperone protein ClpB
PRO_0000191087

Regions

Domain603 – 63836UVR
Nucleotide binding340 – 3478ATP 1 By similarity
Nucleotide binding726 – 7338ATP 2 By similarity
Region1 – 232232N-terminal By similarity
Region251 – 473223NBD1 By similarity
Region474 – 666193Linker By similarity
Region676 – 893218NBD2 By similarity
Region894 – 1006113C-terminal By similarity
Coiled coil524 – 648125 By similarity

Sequences

Sequence LengthMass (Da)Tools
O67588 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: FEBB850E75D1A8EF

FASTA1,006114,537
        10         20         30         40         50         60 
MISENLFSAK SLEYLEKAKE IARENKDTKV DTDHLLIALL LDEKSPLSKY IEKRGIDRKE 

        70         80         90        100        110        120 
FLKRVSEYLE NLNKQLEKAI EAEAQNLINL RTQIMEVKSN IGNVQTELSK IRKAKERILR 

       130        140        150        160        170        180 
ELEYARRYGD WWTAETLELE LRQLEATEQS IRRQLEQVEK SLSTVFAPED VKAFLENKLS 

       190        200        210        220        230        240 
IDGLIRKALE KSPLIEQVKE LGISPDRIID KVAEKVFGKK PTFDYSQYLT QVLEKAQDKA 

       250        260        270        280        290        300 
VSEGEAQVQP SHISAALIEA KDTIGGKLIN QVLGGEKEMK KDVTQELKEE EKSPLERFGV 

       310        320        330        340        350        360 
NLNELARQGK LDPVIGRERE INQVIEILLR RTKNNPVLVG DPGVGKTAIV EGLAQRIVNK 

       370        380        390        400        410        420 
EVPPELQDKE IWSIDMASLL AGSKYRGEFE ERLKALLDEV KEKGNVILFI DEIHTVVGAG 

       430        440        450        460        470        480 
AAEGAVDAAN IMKPALARGE IRVIGATTVD EYRKYIEKDP ALERRFQPVF VDEPTEEQTI 

       490        500        510        520        530        540 
EILKGLRPRL EQFHKVKISD EAIEAAVKLT KRYVTFRRLP DKAIDALDQA AARKKLKVIG 

       550        560        570        580        590        600 
TPPEIQEIER KIKALEEQII EANLKGDYEK EAQLKIEKAK LEKEKQELLG KVGGVEAKIA 

       610        620        630        640        650        660 
ELKKKIEELD EKIKEAAEKG DYEKEAELKI EKAKLEKELK KLEQEKSKEL VVTWDDVAEV 

       670        680        690        700        710        720 
VSEWTGIPVS RLKEEEMQKL LKLEDELHKR VVDQEHAVKA VAEAIRRARA GLKDPKRPIA 

       730        740        750        760        770        780 
SFLFLGPTGV GKTELSKALA ELLFGDEDAL IRLDMSEFKE EHSVAKLIGA PPGYVGYEEG 

       790        800        810        820        830        840 
GKLTEAVRRK PYSVILLDEI EKAHPRVLDL FLQVLDDGRL TDSHGRTVDF RNTVIIMTSN 

       850        860        870        880        890        900 
IGSQYLLNIP VDADEETLNR EFEKAKEKVL EELKLYMRPE FINRIDEIIV FKPLTMRELS 

       910        920        930        940        950        960 
KIIDLLIANV NKRLAERNIK IELTEEAKKE LVRRGYDPAF GARPLKRTIQ KYVETPLADK 

       970        980        990       1000 
IIRGEIKDGM TVVVDYKDGE FVFIPKEEYE KQKAEVSASS EEKKES 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07550.1.
PIRC70445.
RefSeqNP_214154.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67588.
SMRO67588. Positions 295-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_1672.

Proteomic databases

PRIDEO67588.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07550; AAC07550; aq_1672.
GeneID1193304.
KEGGaae:aq_1672.
PATRIC20960368. VBIAquAeo85532_1295.

Phylogenomic databases

eggNOGCOG0542.
HOGENOMHOG000218211.
KOK03695.
OMAKNAFRPE.
OrthoDBEOG65F8SM.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-1199-MONOMER.

Family and domain databases

Gene3D1.10.1780.10. 2 hits.
3.40.50.300. 3 hits.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
IPR001270. ClpA/B.
IPR018368. ClpA/B_CS1.
IPR028299. ClpA/B_CS2.
IPR023150. Dbl_Clp-N.
IPR027417. P-loop_NTPase.
IPR001943. UVR_dom.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 1 hit.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
PRINTSPR00300. CLPPROTEASEA.
SMARTSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
PS50151. UVR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPB_AQUAE
AccessionPrimary (citable) accession number: O67588
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: August 1, 1998
Last modified: May 14, 2014
This is version 82 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