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Protein

Chaperone protein ClpB

Gene

clpB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi206 – 213ATP 18
Nucleotide bindingi605 – 612ATP 28

GO - Molecular functioni

  • ATPase activity, coupled Source: EcoCyc
  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: EcoCyc

GO - Biological processi

  • protein processing Source: InterPro
  • response to heat Source: EcoCyc
  • response to unfolded protein Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG10157-MONOMER.
ECOL316407:JW2573-MONOMER.
SABIO-RKP63284.

Names & Taxonomyi

Protein namesi
Recommended name:
Chaperone protein ClpB
Alternative name(s):
Heat shock protein F84.1
Gene namesi
Name:clpB
Synonyms:htpM
Ordered Locus Names:b2592, JW2573
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10157. clpB.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7T → A: Loss of chaperone activity. 1 Publication1
Mutagenesisi84S → A: No effect. 1 Publication1
Mutagenesisi93L → Q: Loss of chaperone activity. Retains ATPase activity. 1 Publication1
Mutagenesisi97L → Q: 75% decrease in chaperone activity; retains ATPase activity. 1 Publication1
Mutagenesisi103D → A: Loss of chaperone activity. 1 Publication1
Mutagenesisi109E → A: Loss of chaperone activity. 1 Publication1
Mutagenesisi110L → Q: 30% decrease in chaperone activity; retains ATPase activity. 1 Publication1
Mutagenesisi212K → T: Loss of ability to form oligomers even in the presence of ATP. Loss of chaperone activity. 3 Publications1
Mutagenesisi251Y → A: Decrease in ability to disaggregate proteins due to decreased substrate-binding activity. Retains hexameric quaternary structure and ATPase activity. 1 Publication1
Mutagenesisi254E → A: Decrease in ability to disaggregate proteins due to decreased substrate-binding activity. Retains hexameric quaternary structure and ATPase activity; when associated with A-257. 1 Publication1
Mutagenesisi257E → A: Decrease in ability to disaggregate proteins due to decreased substrate-binding activity. Retains hexameric quaternary structure and ATPase activity; when associated with A-254. 1 Publication1
Mutagenesisi279E → A: No effect on oligomerization. 1 Publication1
Mutagenesisi332R → A: Loss of ability to form oligomers. 1 Publication1
Mutagenesisi543W → F: No effect on chaperone activity or ability to form oligomers. 1 Publication1
Mutagenesisi611K → T: No effect on ability to form oligomers. Loss of chaperone activity. 3 Publications1
Mutagenesisi678E → A: No effect on oligomerization. 1 Publication1
Mutagenesisi756R → A: No effect on oligomerization. Loss of ATPase activity. 1 Publication1
Mutagenesisi797D → A: No effect. 1 Publication1
Mutagenesisi813 – 815GAR → AAA: No effect on oligomerization. 1 Publication3
Mutagenesisi815R → A: Loss of ability to form oligomers; loss of chaperone activity. 1 Publication1
Mutagenesisi819R → A: Loss of ability to form oligomers; loss of chaperone activity. 1 Publication1
Mutagenesisi826E → A: No effect. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000054911 – 857Chaperone protein ClpBAdd BLAST857

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei96N6-acetyllysine1 Publication1
Modified residuei176N6-acetyllysine1 Publication1
Modified residuei640N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP63284.
PaxDbiP63284.
PRIDEiP63284.

2D gel databases

SWISS-2DPAGEP63284.

PTM databases

iPTMnetiP63284.

Expressioni

Inductioni

By heat shock and other environmental stresses.

Interactioni

Subunit structurei

Homohexamer. The oligomerization is ATP-dependent.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-546182,EBI-546182
yeeDP330143EBI-546182,EBI-9130839

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4260618. 194 interactors.
851414. 30 interactors.
DIPiDIP-35844N.
IntActiP63284. 77 interactors.
MINTiMINT-1222117.
STRINGi511145.b2592.

Structurei

Secondary structure

1857
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi8 – 23Combined sources16
Beta strandi27 – 29Combined sources3
Helixi31 – 39Combined sources9
Helixi46 – 53Combined sources8
Helixi57 – 68Combined sources12
Helixi85 – 101Combined sources17
Beta strandi104 – 106Combined sources3
Helixi108 – 116Combined sources9
Helixi120 – 128Combined sources9
Helixi133 – 141Combined sources9
Helixi159 – 164Combined sources6
Beta strandi165 – 167Combined sources3
Helixi168 – 173Combined sources6
Helixi184 – 194Combined sources11
Beta strandi196 – 199Combined sources4
Beta strandi201 – 205Combined sources5
Helixi212 – 225Combined sources14
Helixi230 – 232Combined sources3
Beta strandi236 – 240Combined sources5
Helixi242 – 246Combined sources5
Turni247 – 249Combined sources3
Helixi252 – 268Combined sources17
Turni270 – 272Combined sources3
Beta strandi273 – 278Combined sources6
Helixi280 – 283Combined sources4
Helixi296 – 304Combined sources9
Beta strandi310 – 314Combined sources5
Helixi316 – 322Combined sources7
Turni323 – 325Combined sources3
Helixi327 – 330Combined sources4
Beta strandi333 – 337Combined sources5
Helixi343 – 347Combined sources5
Beta strandi363 – 365Combined sources3
Helixi367 – 380Combined sources14
Helixi388 – 406Combined sources19
Helixi410 – 429Combined sources20
Helixi444 – 492Combined sources49
Helixi496 – 503Combined sources8
Helixi505 – 523Combined sources19
Helixi533 – 544Combined sources12
Helixi549 – 552Combined sources4
Helixi555 – 560Combined sources6
Helixi562 – 569Combined sources8
Helixi574 – 589Combined sources16
Beta strandi598 – 605Combined sources8
Beta strandi607 – 610Combined sources4
Helixi611 – 623Combined sources13
Beta strandi624 – 633Combined sources10
Helixi634 – 636Combined sources3
Helixi640 – 645Combined sources6
Helixi661 – 668Combined sources8
Beta strandi673 – 678Combined sources6
Helixi679 – 681Combined sources3
Helixi684 – 696Combined sources13
Beta strandi697 – 700Combined sources4
Beta strandi706 – 708Combined sources3
Beta strandi713 – 719Combined sources7
Helixi722 – 726Combined sources5
Turni734 – 736Combined sources3
Helixi737 – 748Combined sources12
Helixi751 – 756Combined sources6
Beta strandi757 – 762Combined sources6
Helixi768 – 788Combined sources21
Beta strandi792 – 795Combined sources4
Helixi797 – 807Combined sources11
Turni810 – 812Combined sources3
Turni814 – 816Combined sources3
Helixi817 – 824Combined sources8
Helixi826 – 835Combined sources10
Beta strandi836 – 838Combined sources3
Beta strandi842 – 849Combined sources8
Beta strandi852 – 857Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JBKX-ray1.80A159-351[»]
1KHYX-ray1.95A/B/C/D1-148[»]
4CIUX-ray3.50A143-857[»]
4D2Qelectron microscopy18.00A/B/C/D/E/F1-857[»]
4D2Uelectron microscopy17.00A/B/C/D/E/F1-857[»]
4D2Xelectron microscopy20.00A/B/C/D/E/F1-857[»]
ProteinModelPortaliP63284.
SMRiP63284.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63284.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 143N-terminalAdd BLAST143
Regioni159 – 340NBD1Add BLAST182
Regioni341 – 545LinkerAdd BLAST205
Regioni555 – 765NBD2Add BLAST211
Regioni766 – 857C-terminalAdd BLAST92

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili391 – 525By similarityAdd BLAST135

Domaini

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.

Sequence similaritiesi

Belongs to the ClpA/ClpB family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG4105C2Z. Bacteria.
COG0542. LUCA.
HOGENOMiHOG000218211.
InParanoidiP63284.
KOiK03695.
OMAiPVERILM.
PhylomeDBiP63284.

Family and domain databases

Gene3Di1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
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.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
PRINTSiPR00300. CLPPROTEASEA.
SMARTiSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF81923. SSF81923. 1 hit.
TIGRFAMsiTIGR03346. chaperone_ClpB. 1 hit.
PROSITEiPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform ClpB (identifier: P63284-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRLDRLTNKF QLALADAQSL ALGHDNQFIE PLHLMSALLN QEGGSVSPLL
60 70 80 90 100
TSAGINAGQL RTDINQALNR LPQVEGTGGD VQPSQDLVRV LNLCDKLAQK
110 120 130 140 150
RGDNFISSEL FVLAALESRG TLADILKAAG ATTANITQAI EQMRGGESVN
160 170 180 190 200
DQGAEDQRQA LKKYTIDLTE RAEQGKLDPV IGRDEEIRRT IQVLQRRTKN
210 220 230 240 250
NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKGRRVLAL DMGALVAGAK
260 270 280 290 300
YRGEFEERLK GVLNDLAKQE GNVILFIDEL HTMVGAGKAD GAMDAGNMLK
310 320 330 340 350
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVAE PSVEDTIAIL
360 370 380 390 400
RGLKERYELH HHVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS
410 420 430 440 450
IRMQIDSKPE ELDRLDRRII QLKLEQQALM KESDEASKKR LDMLNEELSD
460 470 480 490 500
KERQYSELEE EWKAEKASLS GTQTIKAELE QAKIAIEQAR RVGDLARMSE
510 520 530 540 550
LQYGKIPELE KQLEAATQLE GKTMRLLRNK VTDAEIAEVL ARWTGIPVSR
560 570 580 590 600
MMESEREKLL RMEQELHHRV IGQNEAVDAV SNAIRRSRAG LADPNRPIGS
610 620 630 640 650
FLFLGPTGVG KTELCKALAN FMFDSDEAMV RIDMSEFMEK HSVSRLVGAP
660 670 680 690 700
PGYVGYEEGG YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT
710 720 730 740 750
DGQGRTVDFR NTVVIMTSNL GSDLIQERFG ELDYAHMKEL VLGVVSHNFR
760 770 780 790 800
PEFINRIDEV VVFHPLGEQH IASIAQIQLK RLYKRLEERG YEIHISDEAL
810 820 830 840 850
KLLSENGYDP VYGARPLKRA IQQQIENPLA QQILSGELVP GKVIRLEVNE

DRIVAVQ
Length:857
Mass (Da):95,585
Last modified:October 11, 2004 - v1
Checksum:iFD38CD96B2F7C32A
GO
Isoform ClpB-3 (identifier: P63284-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-148: Missing.
     149-149: V → M

Note: ClpB-3 ATPase activity is not activated by proteins, as it is in ClpB.
Show »
Length:709
Mass (Da):79,870
Checksum:i60270862D6198B55
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti96 – 97KL → NV in AAA24422 (PubMed:2185473).Curated2
Sequence conflicti122L → V in AAA24422 (PubMed:2185473).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0187031 – 148Missing in isoform ClpB-3. CuratedAdd BLAST148
Alternative sequenceiVSP_018987149V → M in isoform ClpB-3. Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29364 Genomic DNA. Translation: AAA24422.1.
U00096 Genomic DNA. Translation: AAC75641.1.
AP009048 Genomic DNA. Translation: BAA16476.1.
X57620 Genomic DNA. Translation: CAA40846.1.
V00350 Genomic DNA. Translation: CAA23639.1.
U50134 Genomic DNA. Translation: AAA92959.1.
PIRiC65037. D35905.
RefSeqiNP_417083.1. NC_000913.3.
WP_001235102.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75641; AAC75641; b2592.
BAA16476; BAA16476; BAA16476.
GeneIDi947077.
KEGGiecj:JW2573.
eco:b2592.
PATRICi32120587. VBIEscCol129921_2692.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29364 Genomic DNA. Translation: AAA24422.1.
U00096 Genomic DNA. Translation: AAC75641.1.
AP009048 Genomic DNA. Translation: BAA16476.1.
X57620 Genomic DNA. Translation: CAA40846.1.
V00350 Genomic DNA. Translation: CAA23639.1.
U50134 Genomic DNA. Translation: AAA92959.1.
PIRiC65037. D35905.
RefSeqiNP_417083.1. NC_000913.3.
WP_001235102.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JBKX-ray1.80A159-351[»]
1KHYX-ray1.95A/B/C/D1-148[»]
4CIUX-ray3.50A143-857[»]
4D2Qelectron microscopy18.00A/B/C/D/E/F1-857[»]
4D2Uelectron microscopy17.00A/B/C/D/E/F1-857[»]
4D2Xelectron microscopy20.00A/B/C/D/E/F1-857[»]
ProteinModelPortaliP63284.
SMRiP63284.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260618. 194 interactors.
851414. 30 interactors.
DIPiDIP-35844N.
IntActiP63284. 77 interactors.
MINTiMINT-1222117.
STRINGi511145.b2592.

PTM databases

iPTMnetiP63284.

2D gel databases

SWISS-2DPAGEP63284.

Proteomic databases

EPDiP63284.
PaxDbiP63284.
PRIDEiP63284.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75641; AAC75641; b2592.
BAA16476; BAA16476; BAA16476.
GeneIDi947077.
KEGGiecj:JW2573.
eco:b2592.
PATRICi32120587. VBIEscCol129921_2692.

Organism-specific databases

EchoBASEiEB0155.
EcoGeneiEG10157. clpB.

Phylogenomic databases

eggNOGiENOG4105C2Z. Bacteria.
COG0542. LUCA.
HOGENOMiHOG000218211.
InParanoidiP63284.
KOiK03695.
OMAiPVERILM.
PhylomeDBiP63284.

Enzyme and pathway databases

BioCyciEcoCyc:EG10157-MONOMER.
ECOL316407:JW2573-MONOMER.
SABIO-RKP63284.

Miscellaneous databases

EvolutionaryTraceiP63284.
PROiP63284.

Family and domain databases

Gene3Di1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
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.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view]
PRINTSiPR00300. CLPPROTEASEA.
SMARTiSM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF81923. SSF81923. 1 hit.
TIGRFAMsiTIGR03346. chaperone_ClpB. 1 hit.
PROSITEiPS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCLPB_ECOLI
AccessioniPrimary (citable) accession number: P63284
Secondary accession number(s): P03815
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 11, 2004
Last modified: November 2, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

One peptide binds per ClpB hexamer; the binding site is formed only upon ATP-driven oligomerization.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.