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Reviewed, UniProtKB/Swiss-Prot Q4UN57 (CLPB_RICFE)

Last modified December 15, 2009. Version 43. 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: RF_0150/RF_0149
OrganismRickettsia felis (Rickettsia azadi) [Complete proteome] [HAMAP]
Taxonomic identifier42862 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever 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.

Sequence caution

The sequence AAY61001.1 differs from that shown. Reason: Erroneous termination at position 709. Translated as Lys.

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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_0000281061

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
Q4UN57-1 [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: 74CFE1983528CC14

FASTA85896,055
        10         20         30         40         50         60 
MNIDKFTAHA KSVIASSQSI AAKNDHQQIL PLHLLSSLLS EETGIIQTLI NNTGGNINLL 

        70         80         90        100        110        120 
KDQVQLELNK IPKVQVEGGG QVYSSAEALK VLEKASSIAK DSGDSFVTIE RIFEALTYGN 

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

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

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

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

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

       430        440        450        460        470        480 
IQIKIELAAL KKENDEHSKK KITHLTEELE KLESKSYDMK AKWQAEKSKL QQAQKLKEEL 

       490        500        510        520        530        540 
ERARIDLERA ERDANLAKAS ELKYGIIPEI MKKIQEAESM DNKGLLKEIV SESDIASIIS 

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

       610        620        630        640        650        660 
LFLGPTGVGK TELTKALASF 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 LLEFDESALN YLAEKGYDPS FGARPLKRLI QREIQNNLAK MILAGEISSG 

       850 
NTVKIAREKE ELRIKIID

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References

[1]"The genome sequence of Rickettsia felis identifies the first putative conjugative plasmid in an obligate intracellular parasite."
Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E., Parinello H., Claverie J.-M., Raoult D.
PLoS Biol. 3:1-12(2005) [PubMed: 15984913] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-1525 / URRWXCal2.

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Cross-references

Sequence databases

CP000053 Genomic DNA. Translation: AAY61000.1. Different initiation.
CP000053 Genomic DNA. Translation: AAY61001.1. Sequence problems.
RefSeqYP_246165.1.
YP_246166.1.

3D structure databases

HSSPHSSP built from PDB template 1QVR based on UniProtKB Q9RA63.
ModBaseSearch...

Genome annotation databases

GeneID3401043.
3401044.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAKRENDEP.

Enzyme and pathway databases

BioCycRFEL315456:RF_0150-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]
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCLPB_RICFE
AccessionPrimary (citable) accession number: Q4UN57
Secondary accession number(s): Q4UN58
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: December 15, 2009
This is version 43 of the entry and version 2 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 felis (Rickettsia azadi)

Rickettsia felis (strain URRWXCal2): 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