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O83110 (CLPB_TREPA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chaperone protein ClpB
Gene names
Name:clpB
Ordered Locus Names:TP_0071
OrganismTreponema pallidum (strain Nichols) [Complete proteome] [HAMAP]
Taxonomic identifier243276 [NCBI]
Taxonomic lineageBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema

Protein attributes

Sequence length878 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 – 878878Chaperone protein ClpB
PRO_0000191197

Regions

Nucleotide binding206 – 2138ATP 1 By similarity
Nucleotide binding609 – 6168ATP 2 By similarity
Region1 – 143143N-terminal By similarity
Region159 – 340182NBD1 By similarity
Region341 – 549209Linker By similarity
Region559 – 783225NBD2 By similarity
Region784 – 87895C-terminal By similarity
Coiled coil391 – 525135 By similarity

Sequences

Sequence LengthMass (Da)Tools
O83110 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 7D9E7419E42A2202

FASTA87898,981
        10         20         30         40         50         60 
MNTDRYTVKA SEALNDAISL AEAENHGQVE EEHLLHALLS QKDGIISPLI EKIGAKPDFL 

        70         80         90        100        110        120 
YDELLQCLRR KPRVTGPAAQ TRCAPTLSKA CARAERLALK NQDEYVSCEH LLLAISETDS 

       130        140        150        160        170        180 
NTARLLHSQG ITSKTISAAL KDIRGSKRVT SQDPESTFQC LEKYCRDLTT LAREEKIDPV 

       190        200        210        220        230        240 
IGRDEEIRRV MQVLSRRTKN NPVLIGEPGV GKTAIVEGLA RRIVSGDVPE SLKGKRLLSL 

       250        260        270        280        290        300 
DLGALVAGAK FRGEFEERLK AVIEAVQKSD GGVILFIDEL HTLVGAGASE GSMDASNLLK 

       310        320        330        340        350        360 
PALARGELRS IGATTLNEYR KYIEKDAALE RRFQQVYCVQ PTVEDTIAIL RGLQEKYEVH 

       370        380        390        400        410        420 
HGVRIKDEAL VAATVLSDRY ITNRFLPDKA IDLVDEAASR LKMEIESQPV ELDQVERKIL 

       430        440        450        460        470        480 
QLNIEKASLL KESDPASKER LEKLEKELAG FLERRAAMQV QWQNEKGRIE ESRRYKEELE 

       490        500        510        520        530        540 
RLRIEETMFS REGDLNKAAE LRYGKIPELE KKIMLLTAEV EKKSGLEGQL LREEVCEEDI 

       550        560        570        580        590        600 
AKIISMWTGI PVSKMMASEQ QKYLQLESVL MQRVVGQDEA VRVISDAIRR NKAGLSDTRR 

       610        620        630        640        650        660 
PLGSFLCVGP TGVGKTELAR TLADFLFNDE RALTRIDMSE YMEKHAISRL IGAPPGYVGY 

       670        680        690        700        710        720 
DEGGQLTEAV RRRPYSVLLF DEVEKAHQDV FNIFLQILDD GRLTDGQGRV VDFRNTIIIM 

       730        740        750        760        770        780 
TSNIGSEHIL SARESRTHTS DLPVPETQST EEQTLPEQIR GLLHTYFRPE FLNRIDEVLI 

       790        800        810        820        830        840 
FKRLTRKHIR LITDIQLQMV VERLESRHIK LRVRDAAKAY LAERGYDDTF GARPLKRAIQ 

       850        860        870 
TELENALARE ILSGRFRGGS TIVVDMCKDA LCFTEQTS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000520 Genomic DNA. Translation: AAC65062.1.
PIRG71371.
RefSeqNP_218511.1. NC_000919.1.
YP_008090945.1. NC_021490.2.

3D structure databases

ProteinModelPortalO83110.
SMRO83110. Positions 159-351.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO83110. 5 interactions.
STRING243276.TP0071.

Proteomic databases

PRIDEO83110.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC65062; AAC65062; TP_0071.
GeneID15851364.
2611222.
KEGGtpa:TP0071.
tpw:TPANIC_0071.
PATRIC20530079. VBITrePal57110_0076.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0542.
KOK03695.
OMATIQDHIE.
OrthoDBEOG65F8SM.
ProtClustDBCLSK218513.

Enzyme and pathway databases

BioCycTPAL243276:GC1H-76-MONOMER.

Family and domain databases

Gene3D1.10.1780.10. 1 hit.
3.40.50.300. 3 hits.
InterProIPR003593. AAA+_ATPase.
IPR013093. ATPase_AAA-2.
IPR003959. ATPase_AAA_core.
IPR017730. Chaperonin_ClpB.
IPR019489. Clp_ATPase_C.
IPR004176. Clp_N.
IPR001270. ClpA/B.
IPR018368. ClpA/B_CS1.
IPR028299. ClpA/B_CS2.
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_TREPA
AccessionPrimary (citable) accession number: O83110
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 88 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