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Q8YJ91 (CLPB_BRUME) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chaperone protein ClpB
Gene names
Name:clpB
Ordered Locus Names:BMEI0195
OrganismBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]
Taxonomic identifier224914 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella

Protein attributes

Sequence length874 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.

Sequence caution

The sequence AAL51377.1 differs from that shown. Reason: Erroneous initiation.

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 – 874874Chaperone protein ClpB
PRO_0000191099

Regions

Nucleotide binding207 – 2148ATP 1 By similarity
Nucleotide binding605 – 6128ATP 2 By similarity
Region1 – 144144N-terminal By similarity
Region160 – 341182NBD1 By similarity
Region342 – 545204Linker By similarity
Region555 – 765211NBD2 By similarity
Region766 – 874109C-terminal By similarity
Coiled coil392 – 524133 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YJ91 [UniParc].

Last modified October 11, 2004. Version 2.
Checksum: 56BD6A020FBD17E2

FASTA87496,908
        10         20         30         40         50         60 
MNIEKYTERV RGFIQSAQTF ALSSGNQQFT PEHILKVLID DDEGLAASLV ERAGGRVGDV 

        70         80         90        100        110        120 
RMGLQSALEK LPKVSGGNDQ LYLSQPLAKV FSLAEELASK AGDSFVTVER LLTALAMEKS 

       130        140        150        160        170        180 
AKTSEILSAA GVTPTALNRV INDMRKGRTA DSASAESNYD ALKKYARDLT EDARAGKLDP 

       190        200        210        220        230        240 
VIGRDEEIRR TIQVLSRRTK NNPVLIGEPG VGKTAIAEGL ALRIVNGDVP ESLKDKQLMA 

       250        260        270        280        290        300 
LDMGALIAGA KYRGEFEERL KAVLSEVQTA AGQIILFIDE MHTLVGAGKT DGAMDASNLL 

       310        320        330        340        350        360 
KPALARGELH CVGATTLEEY RKYVEKDAAL ARRFQPVFVD EPTVEDTISI LRGLKEKYEQ 

       370        380        390        400        410        420 
HHKVRVSDSA LVAAAMLSNR YITDRFLPDK AIDLVDEAAS RLRMQVDSKP EELDEIDRRI 

       430        440        450        460        470        480 
MQLKIEREAL KVETDAASKD RLQRIEKELS DLEEESAELT AKWQAEKQKL GLAADLKRQL 

       490        500        510        520        530        540 
EEARNALAIA QRNGEFQKAG ELAYGTIPQL EKQLADAESQ ENKGSLLEET VTPDHVAQVI 

       550        560        570        580        590        600 
SRWTGIPVDR MLEGEREKLL RMEDEIGKRV VGQGEAVQAI SKAVRRARAG LQDPNRPIGS 

       610        620        630        640        650        660 
FIFLGPTGVG KTELTKALAS FLFQDDTAMV RIDMSEFMEK HSVSRLIGAP PGYVGYEEGG 

       670        680        690        700        710        720 
VLTEAVRRRP YQVILFDEIE KAHPDVFNVL LQVLDDGRLT DGQGHTVDFR NTVIIMTSNL 

       730        740        750        760        770        780 
GAEYLVNLGE NDDVETVRDD VMGVVRASFR PEFLNRVDEI ILFHRLRRED MGAIVDIQMQ 

       790        800        810        820        830        840 
RLQYLLSDRK ITLQLEDDAR EWLANKGYDP AYGARPLKRV IQKEVQDPLA ERILLGDILD 

       850        860        870 
GSLVKITAGS DRLNFRPISG AFSAAEPERE DEKA

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE008917 Genomic DNA. Translation: AAL51377.1. Different initiation.
PIRAF3276.
RefSeqNP_539113.1. NC_003317.1.

3D structure databases

ProteinModelPortalQ8YJ91.
SMRQ8YJ91. Positions 161-352.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1195907.
GenomeReviewsGene locus BMEI0195 in contig AE008917_GR.
KEGGbme:BMEI0195.
NMPDRfig|224914.1.peg.195.
PATRIC17850349. VBIBruMel92729_0206.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG413133.
OMAENQNINK.
PhylomeDBQ8YJ91.
ProtClustDBCLSK863757.

Enzyme and pathway databases

BioCycBMEL224914:BMEI0195-MONOMER.

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.
IPR023150. Dbl_Clp-N.
[Graphical view]
Gene3DG3DSA:1.10.1780.10. Dbl_Clp-N. 1 hit.
KOK03695.
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]
TIGRFAMsTIGR03346. Chaperone_ClpB. 1 hit.
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPB_BRUME
AccessionPrimary (citable) accession number: Q8YJ91
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella melitensis

Brucella melitensis (strain 16M): entries and gene names

SIMILARITY comments

Index of protein domains and families

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