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Reviewed, UniProtKB/Swiss-Prot Q9ZEA9 (CLPB_RICPR)

Last modified November 24, 2009. Version 45. 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

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Names and origin

Protein namesRecommended name:
    Chaperone protein clpB
Gene names
Name: clpB
Ordered Locus Names: RP036
OrganismRickettsia prowazekii [Complete proteome] [HAMAP]
Taxonomic identifier782 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group

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Protein attributes

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

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 858858Chaperone protein clpB
PRO_0000191170

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

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Sequences

Sequence LengthMass (Da)Tools
Q9ZEA9-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: A18F52B6CD5805AE

FASTA85896,291
        10         20         30         40         50         60 
MNIDKFTAHA KSVIANHQSL AIKNDHQQIL PLHLLSSLLS EETGIIQALI NNIGGNINLL 

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

       130        140        150        160        170        180 
TIAGKILTNN GINSKKLATA ILHLRKGKKA DTESAENNYD ALKRYGRDVT ELAENGKLDP 

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

       250        260        270        280        290        300 
LDIGALIAGA QYRGEFEKRL KAVLSEIKES SGEIILFIDE LHLLVGTGKV DGAMDASNLL 

       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 KLESKSYDMN TKWQAEKSKL QQAQKLKEEL 

       490        500        510        520        530        540 
EQARIDLERA ERDANLAKAS ELKYGIIPEI MNKLQEAENM DNKGLLKEIV SESDIASIIS 

       550        560        570        580        590        600 
RITGIPIDTM LSSERERLLV IEQKLCESVI GQDEAIKGVS DAVRRSRSGI QDINRPLGSF 

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

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

       730        740        750        760        770        780 
AEILVNQKEG EDTYKVRDEV MQYVRAVFKP EFLNRLDEII LFHRLNRNNI HDIVKIQLGS 

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

       850 
NTVKIRREKE ELSINIID

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References

[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed: 9823893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.

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Cross-references

Sequence databases

AJ235270 Genomic DNA. Translation: CAA14507.1.
PIRD71711.
RefSeqNP_220430.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID883571.
GenomeReviewsGene locus RP036 in contig AJ235269_GR.
KEGGrpr:RP036.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9ZEA9.
OMAMGGAMDA

Enzyme and pathway databases

BioCycRPRO272947:RP036-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...

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Entry information

Entry nameCLPB_RICPR
AccessionPrimary (citable) accession number: Q9ZEA9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: May 1, 1999
Last modified: November 24, 2009
This is version 45 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)

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Relevant documents

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): 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