Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q68XR2 (CLPB_RICTY)

Last modified November 24, 2009. Version 38. 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

Hide | Top

Names and origin

Protein namesRecommended name:
    Chaperone protein clpB
Gene names
Name: clpB
Ordered Locus Names: RT0094
OrganismRickettsia typhi [Complete proteome] [HAMAP]
Taxonomic identifier785 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group

Hide | Top

Protein attributes

Sequence length858 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

Hide | Top

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.

Hide | Top

Ontologies

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

protein binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 858858Chaperone protein clpB
PRO_0000281062

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 – 85894C-terminal By similarity
Coiled coil392 – 523132 By similarity

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q68XR2-1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 5F979124653DDEFB

FASTA85896,288
        10         20         30         40         50         60 
MNIDKFTAHA KSVIANHQSL AIKNDHQQIL PLHLLSSLLS EETGIIQALI NNIGGNIHLL 

        70         80         90        100        110        120 
KDQVQLELNK IPKIQVDGGG QIYYSAEDLK VLEKSRSIAK DSGDSFVTIE RIFEALTYDN 

       130        140        150        160        170        180 
TIAGKILTNN GINSKKLAAA ILHLRKGKKA DTESAENSYD ALKRYGRDVT ELAKNGKLDP 

       190        200        210        220        230        240 
IIGRDEEIRR AVQVLSRRMK NNPVLIGAPG VGKTAIIEGL AQRIFNKDVP ETLINCRIIE 

       250        260        270        280        290        300 
LDIGALIAGA QYRGEFEKRL KSVLSEIKES SGEIILFIDE LHLLVGTGKV EGAMDASNLL 

       310        320        330        340        350        360 
KPMLARGELH CIGATTLDEY RKYIEKDAAL ARRFQPVYVG EPSVEDTISI LRGIKEKYEL 

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

       430        440        450        460        470        480 
IQIKIELAAL KKENDEHSKK KITSLTEELK QLDSKSYDMN TKWQAAKSKL QQAQKLKEEL 

       490        500        510        520        530        540 
EQARIDLDRA ERDANLAKAS ELKYGIIPEI MNKLQAAENM DNKGLLKEIV SESDIASIIS 

       550        560        570        580        590        600 
RITGIPIDTM LSSERERLLV IEQKLSESVI GQDEAIKGIS DAVRRSRSGI QDINRPLGSF 

       610        620        630        640        650        660 
LFLGPTGVGK TELTKALAGF LFDDRNALLR IDMSEYMEKH SISRLIGAPP GYIGYDQGGV 

       670        680        690        700        710        720 
LTESVRRRPY QVILFDEVEK AHLDIFNIML QILDEGRLTN SQGITVDFKN TIIVLTSNLG 

       730        740        750        760        770        780 
AEILVNQQED EDTYKVKDEV MQYVRAVFKP EFLNRLDEII LFHRLNRNNI YDIVKIQLGS 

       790        800        810        820        830        840 
LKKILLQQNI ILEFNESALN YLAEKGYDPS FGARPLKRLI QREIQNNLAK MILAGKISSG 

       850 
NTVKIAREKE ELRIEIID

« Hide

Hide | Top

References

[1]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed: 15317790] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Hide | Top

Cross-references

Sequence databases

AE017197 Genomic DNA. Translation: AAU03580.1.
RefSeqYP_067062.1.

3D structure databases

HSSPHSSP built from PDB template 1JBK based on UniProtKB P63284.
ModBaseSearch...

Genome annotation databases

GeneID2959206.
GenomeReviewsGene locus RT0094 in contig AE017197_GR.
KEGGrty:RT0094.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ68XR2.
OMAPDTIADV

Enzyme and pathway databases

BioCycRTYP257363:RT0094-MON.

Family and domain databases

InterProIPR003593. ATPase_AAA+_core.
IPR013093. ATPase_AAA-2.
IPR003959. ATPase_AAA_core.
IPR018368. Chaperonin_ClpA/B_CS.
IPR017730. Chaperonin_ClpB.
IPR001270. Chaprnin_clpA/B.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
[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.
[Graphical view]
TIGRFAMsTIGR03346. chaperone_ClpB. 1 hit.
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameCLPB_RICTY
AccessionPrimary (citable) accession number: Q68XR2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: October 11, 2004
Last modified: November 24, 2009
This is version 38 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)

Hide | Top

Relevant documents

Rickettsia typhi

Rickettsia typhi (strain Wilmington): 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