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Q92JK8 (CLPB_RICCN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:RC0059
OrganismRickettsia conorii (strain ATCC VR-613 / Malish 7) [Complete proteome] [HAMAP]
Taxonomic identifier272944 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

Protein attributes

Sequence length857 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.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

response to heat

Inferred from electronic annotation. Source: InterPro

   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 – 857857Chaperone protein ClpB
PRO_0000191169

Regions

Nucleotide binding207 – 2148ATP 1 By similarity
Nucleotide binding604 – 6118ATP 2 By similarity
Region1 – 144144N-terminal By similarity
Region160 – 341182NBD1 By similarity
Region342 – 544203Linker By similarity
Region554 – 764211NBD2 By similarity
Region765 – 85793C-terminal By similarity
Coiled coil392 – 523132 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q92JK8 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 2D34E3A0BCE47C8A

FASTA85795,972
        10         20         30         40         50         60 
MNIDKFTAHA KSVIASSQLL AAKNDHQQIL PLHLLSSLLS EETGIIQTLI NNTGGNINLL 

        70         80         90        100        110        120 
KDQVQLELNK IPKVQVEGGG QVYSSAEALK VLEKASSIAK DNGDSFVTIE RIFEALTYDN 

       130        140        150        160        170        180 
TIAGKILTNN GINNKKIATA ILQFRKGKKA DTESAENSYD ALKKYGRDVT ELAESGKLDP 

       190        200        210        220        230        240 
IIGRDEEIRR TVQVLSRRMK NNPVLIGEPG VGKTAIIEGL AQRIFSKDVP ESLINCRIIE 

       250        260        270        280        290        300 
LDMGALIAGA KYRGEFEERL KAVLSEIKES SGEIILFIDE LHLLVGTGKT DGAMDASNLL 

       310        320        330        340        350        360 
KPMLARGELH CIGATTLDEY RKYIEKDAAL ARRFQPVYVS EPTVEDTISI LRGIKEKYEL 

       370        380        390        400        410        420 
HHAVRISDSA IVAAATLSNR YITDRYLPDK AIDLIDEACS RMKIELSSKP EELDELDRRI 

       430        440        450        460        470        480 
IQIKIELAAL KKENDEHSKK KIEHLTTALE KLESQSYDMG AKWQAEKSKL QQTQKLKEEL 

       490        500        510        520        530        540 
DRSRNELERA ERDANLAKAS ELKYGIIPEI MKKLQEAESM DNKGLLKEIV SESDIASIIS 

       550        560        570        580        590        600 
RITGIPIDTM LSSERERLLV MEQKLRESVI GQDKAIKGVS DAVRRSRAGI QDINRPLGSF 

       610        620        630        640        650        660 
LFLGPTGVGK TELTKALAGF LFDDRNAILR IDMSEYMEKH AISRLIGAPP GYIGYDQGGV 

       670        680        690        700        710        720 
LTEAVRRRPY QVILFDEVEK AHPDIFNIML QILDEGRLTD SQGITVDFKN TIIVLTSNLG 

       730        740        750        760        770        780 
AEILVNQKED EDTYKVKDEV MEYVKAVFKP EFLNRLDEII LFHRLNRNNI HDIVKIQLES 

       790        800        810        820        830        840 
LKKILLAQNI ILEFDESALN YLAEKGYDPS FGARPLKRLI QREIQNNLAK MILAGEISSG 

       850 
KTVKINSKDK ELKVTMS 

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References

[1]"Mechanisms of evolution in Rickettsia conorii and R. prowazekii."
Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.
Science 293:2093-2098(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-613 / Malish 7.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE006914 Genomic DNA. Translation: AAL02597.1.
PIRC97707.
RefSeqNP_359696.1. NC_003103.1.

3D structure databases

ProteinModelPortalQ92JK8.
SMRQ92JK8. Positions 161-352.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272944.RC0059.

Proteomic databases

PRIDEQ92JK8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL02597; AAL02597; RC0059.
GeneID928600.
KEGGrco:RC0059.
PATRIC17887212. VBIRicCon45613_0070.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0542.
HOGENOMHOG000218211.
KOK03695.
OMAAMETKLV.
OrthoDBEOG65F8SM.

Family and domain databases

Gene3D1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR017730. Chaperonin_ClpB.
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.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
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.
TIGRFAMsTIGR03346. chaperone_ClpB. 1 hit.
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPB_RICCN
AccessionPrimary (citable) accession number: Q92JK8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: December 1, 2001
Last modified: May 14, 2014
This is version 71 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

Rickettsia conorii

(strain Malish 7): entries and gene names