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O34209 (CLPB2_SYNE7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Chaperone protein ClpB 2
Gene names
Name:clpB2
Ordered Locus Names:Synpcc7942_0637
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechococcus ›

Protein attributes

Sequence length895 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.

Miscellaneous

Not induced by heat shock or other stresses, it is expressed constitutively in the cell.

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 – 895895Chaperone protein ClpB 2
PRO_0000191189

Regions

Nucleotide binding210 – 2178ATP 1 By similarity
Nucleotide binding617 – 6248ATP 2 By similarity
Region1 – 145145N-terminal By similarity
Region163 – 346184NBD1 By similarity
Region347 – 557211Linker By similarity
Region567 – 778212NBD2 By similarity
Region779 – 895117C-terminal By similarity
Coiled coil397 – 533137 By similarity

Sequences

Sequence LengthMass (Da)Tools
O34209 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: EF5B0103EB513302

FASTA89599,821
        10         20         30         40         50         60 
MQPTDPNRFT DQAWDAIVES QTVARQLRQQ QLEVEHVLLA LLDQESGVAA EILAKAGVAV 

        70         80         90        100        110        120 
ANLRQPLEDF ARRQPRNASG TQLYLGRGLD RLLDLAERAR ELWQDEFIGV EHLLMGFVED 

       130        140        150        160        170        180 
DRIGRRLAQG LKLDAKTLET TIQALRSPAA DEAEAEESEP SYPFLSKYGR DLTALAEQEK 

       190        200        210        220        230        240 
LDPVIGRDLE IRRVIQVLSR RSKNNPVLIG EPGVGKTAIA EGLAQRIVAG EVPDSLKQRR 

       250        260        270        280        290        300 
LISLDMGSLI AGAKYRGEFE ERLRAVLHEV THSDGQMVLF IDELHTVVGA GAGQQGSAMD 

       310        320        330        340        350        360 
AGNLLKPMLA RGELRCIGAT TTDEYRRTIE KDPALERRFQ QVYVSQPSVE DTIAILRGLK 

       370        380        390        400        410        420 
ERYEGHHGVK ITDGALMAAA KLSHRYISDR FLPDKAIDLI DEASAQLKME ITSKPSELED 

       430        440        450        460        470        480 
LERRLLQLEM EQLSLSGENG QASVHSDRLQ QIQTELQTLQ EQQARLNQQW QQEKQLLEEL 

       490        500        510        520        530        540 
GRLQEEEETL RQQVNQAERE HDLNKGAELK FGQLEALQQQ RQAIEEQIQA LHANGQTLLR 

       550        560        570        580        590        600 
EQVEEADIAE IVARWTNIPV QRLLESERQK LLQLESFLHQ RVIGQDEAVV AVAAAIRRAR 

       610        620        630        640        650        660 
AGMKDPSRPI GSFLFLGPTG VGKTELARAL ANCLFDAEDA LIRFDMSEYM EKNSISRLIG 

       670        680        690        700        710        720 
APPGYIGYEE GGQLSEAIRR HPYAVVLFDE VEKAHPDVFN LLLQVLDDGR ITDSQGRTID 

       730        740        750        760        770        780 
FCNAVIVMTS NIGSQFILEM GEEEASLDAV ELKVLGALRQ HFRPEFLNRI DDTILFQPLS 

       790        800        810        820        830        840 
RGQLQQIVDI QLQRLKRLLA EQAIALNVTP AAAANLADRG YDPVYGARPL KRAIQRLIEN 

       850        860        870        880        890 
PVASLILEQQ FDAGDALIVD VDAEGQLQFQ VSKPVTATVV EPDDSPAIAV EAIPS

« Hide

References

« Hide 'large scale' references
[1]"Novel form of ClpB/HSP100 protein in the cyanobacterium Synechococcus."
Eriksson M.J., Schelin J., Miskiewicz E., Clarke A.K.
J. Bacteriol. 183:7392-7396(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7942.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U97124 Genomic DNA. Translation: AAB72154.1.
CP000100 Genomic DNA. Translation: ABB56669.1.
RefSeqYP_399656.1. NC_007604.1.

3D structure databases

ProteinModelPortalO34209.
SMRO34209. Positions 165-357.
ModBaseSearch...

Protein-protein interaction databases

STRING1140.Synpcc7942_0637.

Proteomic databases

PRIDEO34209.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB56669; ABB56669; Synpcc7942_0637.
GeneID3775620.
KEGGsyf:Synpcc7942_0637.
PATRIC23786419. VBISynElo51371_0746.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0542.
HOGENOMHOG000218211.
KOK03695.
ProtClustDBCLSK743626.

Enzyme and pathway databases

BioCycSELO1140:GJWQ-652-MONOMER.

Family and domain databases

Gene3D1.10.1780.10. 1 hit.
InterProIPR003593. AAA+_ATPase.
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]
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 nameCLPB2_SYNE7
AccessionPrimary (citable) accession number: O34209
Secondary accession number(s): Q31QK0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 80 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

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