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Q5HQI5 (CLPB_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 63. 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
Gene names
Name:clpB
Ordered Locus Names:SERP0564
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length869 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.

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 – 869869Chaperone protein ClpB
PRO_0000191182

Regions

Nucleotide binding205 – 2128ATP 1 By similarity
Nucleotide binding609 – 6168ATP 2 By similarity
Region1 – 142142N-terminal By similarity
Region158 – 339182NBD1 By similarity
Region340 – 549210Linker By similarity
Region559 – 771213NBD2 By similarity
Region772 – 86998C-terminal By similarity
Coiled coil390 – 524135 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HQI5 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 23E6E8A3BF9C5FD2

FASTA86998,213
        10         20         30         40         50         60 
MDINQMTYAV QGALQKAVAY SKEYELQNIE VEALLKAAMN ENDSLFKSIL ERANIDVDQL 

        70         80         90        100        110        120 
IKAYDNQLSH YPTVQGDNVQ YGQYISAKTN ELLDKAEKYM KSYEDEFISM EHILRAAIDT 

       130        140        150        160        170        180 
DETTQKWVGN KVEVIKEIIT KVRGGNHVTS QNPEVNYEAL EKYGRDLVEE VRQGKMDPVI 

       190        200        210        220        230        240 
GRDEEIRNTI RILSRKTKNN PVLIGEPGVG KTAIVEGLAQ RIVRKDVPES LLDKTIFELD 

       250        260        270        280        290        300 
LSALVAGAKY RGEFEERLKA VLKEVKESEG RIILFIDEIH MLVGAGKTDG AMDAGNMLKP 

       310        320        330        340        350        360 
MLARGELHCI GATTLNEYRE YIEKDSALER RFQKVGVSEP DVEDTISILR GLKERYEVYH 

       370        380        390        400        410        420 
GVRIQDRALV AAAELSDRYI TDRFLPDKAI DLVDQACATI RTEMGSNPTE LDQVNRRVMQ 

       430        440        450        460        470        480 
LEIEESALKN ESDNPSKHRL EELQEELSNE KEKQSSLKSR VEQEKEKIAK VQEKRAELDS 

       490        500        510        520        530        540 
SRQALEDAQT EGNLEKAAEL QYGTIPQLEK ELQKFEEAFQ DETGEDSERM IREVVSDEEI 

       550        560        570        580        590        600 
GDIVSQWTGI PVSKLVETER EKLLSLSDIL HKRVVGQDKA VDLVSDAVVR ARAGIKDPNR 

       610        620        630        640        650        660 
PIGSFLFLGP TGVGKTELAK SLASSLFDSE KHMIRIDMSE YMEKHAVSRL IGAPPGYVGH 

       670        680        690        700        710        720 
DEGGQLTEAV RRNPYSVILL DEVEKAHSDV FNVLLQILDE GRLTDSKGRS VDFKNTIIIM 

       730        740        750        760        770        780 
TSNIGSQVLL ENVKDAGEIS DDTEKAVMDS LHAYFKPEIL NRMDDIVLFK PLSVNDMSMI 

       790        800        810        820        830        840 
VDKILTQLNM RLLDQHISIE VTEEAKKWLG EEAYEPQFGA RPLKRFVQRQ IETPIARMMI 

       850        860 
KESLPEGTII KVDLNDNKEL DFKVVKPTS

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References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000029 Genomic DNA. Translation: AAW53951.1.
RefSeqYP_188155.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HQI5.
SMRQ5HQI5. Positions 158-350.
ModBaseSearch...

Protein-protein interaction databases

STRING176279.SERP0564.

Proteomic databases

PRIDEQ5HQI5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW53951; AAW53951; SERP0564.
GeneID3241482.
KEGGser:SERP0564.
PATRIC19611999. VBIStaEpi130894_0545.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0542.
HOGENOMHOG000218211.
KOK03695.
OMADTEKAVM.
ProtClustDBCLSK885042.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-587-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.
IPR027417. P-loop_NTPase.
[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]
SUPFAMSSF52540. SSF52540. 2 hits.
TIGRFAMsTIGR03346. chaperone_ClpB. 1 hit.
PROSITEPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCLPB_STAEQ
AccessionPrimary (citable) accession number: Q5HQI5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: May 29, 2013
This is version 63 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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