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P63284

- CLPB_ECOLI

UniProt

P63284 - CLPB_ECOLI

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Protein
Chaperone protein ClpB
Gene
clpB, htpM, b2592, JW2573
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi206 – 2138ATP 1
Nucleotide bindingi605 – 6128ATP 2

GO - Molecular functioni

  1. ATP bindingInferred from electronic annotationi Source: UniProtKB-KW
  2. identical protein bindingInferred from physical interactioni PubMed 16858726 Source: IntAct
  3. nucleoside-triphosphatase activityInferred from electronic annotationi Source: InterPro
  4. protein bindingInferred from physical interactioni PubMed 24561554 Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. protein processingInferred from electronic annotationi Source: InterPro
  2. response to heatInferred from electronic annotationi Source: InterPro
  3. response to unfolded proteinInferred from direct assayi PubMed 1400361 Source: EcoCyc
  1. nucleoside-triphosphatase activityInferred from electronic annotationi Source: InterPro
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-RKiP63284.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10157. clpB.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytosolInferred from direct assayi PubMed 16858726 Source: UniProtKB
  2. membraneInferred from direct assayi PubMed 16858726 Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi7 – 71T → A: Loss of chaperone activity. 1 Publication
Mutagenesisi84 – 841S → A: No effect. 1 Publication
Mutagenesisi93 – 931L → Q: Loss of chaperone activity. Retains ATPase activity. 1 Publication
Mutagenesisi97 – 971L → Q: 75% decrease in chaperone activity; retains ATPase activity. 1 Publication
Mutagenesisi103 – 1031D → A: Loss of chaperone activity. 1 Publication
Mutagenesisi109 – 1091E → A: Loss of chaperone activity. 1 Publication
Mutagenesisi110 – 1101L → Q: 30% decrease in chaperone activity; retains ATPase activity. 1 Publication
Mutagenesisi212 – 2121K → T: Loss of ability to form oligomers even in the presence of ATP. Loss of chaperone activity. 3 Publications
Mutagenesisi251 – 2511Y → A: Decrease in ability to disaggregate proteins due to decreased substrate-binding activity. Retains hexameric quaternary structure and ATPase activity. 1 Publication
Mutagenesisi254 – 2541E → 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 Publication
Mutagenesisi257 – 2571E → 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 Publication
Mutagenesisi279 – 2791E → A: No effect on oligomerization. 1 Publication
Mutagenesisi332 – 3321R → A: Loss of ability to form oligomers. 1 Publication
Mutagenesisi543 – 5431W → F: No effect on chaperone activity or ability to form oligomers. 1 Publication
Mutagenesisi611 – 6111K → T: No effect on ability to form oligomers. Loss of chaperone activity. 3 Publications
Mutagenesisi678 – 6781E → A: No effect on oligomerization. 1 Publication
Mutagenesisi756 – 7561R → A: No effect on oligomerization. Loss of ATPase activity. 1 Publication
Mutagenesisi797 – 7971D → A: No effect. 1 Publication
Mutagenesisi813 – 8153GAR → AAA: No effect on oligomerization. 2 Publications
Mutagenesisi815 – 8151R → A: Loss of ability to form oligomers; loss of chaperone activity. 1 Publication
Mutagenesisi819 – 8191R → A: Loss of ability to form oligomers; loss of chaperone activity. 1 Publication
Mutagenesisi826 – 8261E → A: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 857857Chaperone protein ClpB
PRO_0000005491Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei96 – 961N6-acetyllysine1 Publication
Modified residuei176 – 1761N6-acetyllysine1 Publication
Modified residuei640 – 6401N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP63284.
PRIDEiP63284.

2D gel databases

SWISS-2DPAGEiP63284.

Expressioni

Inductioni

By heat shock and other environmental stresses.

Gene expression databases

GenevestigatoriP63284.

Interactioni

Subunit structurei

Homohexamer. The oligomerization is ATP-dependent.2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi851414. 30 interactions.
DIPiDIP-35844N.
IntActiP63284. 77 interactions.
MINTiMINT-1222117.
STRINGi511145.b2592.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 2316
Beta strandi27 – 293
Helixi31 – 399
Helixi46 – 538
Helixi57 – 6812
Helixi85 – 10117
Beta strandi104 – 1063
Helixi108 – 1169
Helixi120 – 1289
Helixi133 – 1419
Helixi159 – 1646
Beta strandi165 – 1673
Helixi168 – 1736
Helixi184 – 19411
Beta strandi196 – 1994
Beta strandi201 – 2055
Helixi212 – 22514
Helixi230 – 2323
Beta strandi236 – 2405
Helixi242 – 2465
Turni247 – 2493
Helixi252 – 26817
Turni270 – 2723
Beta strandi273 – 2786
Helixi280 – 2834
Helixi296 – 3049
Beta strandi310 – 3145
Helixi316 – 3227
Turni323 – 3253
Helixi327 – 3304
Beta strandi333 – 3375
Helixi343 – 3475

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JBKX-ray1.80A159-351[»]
1KHYX-ray1.95A/B/C/D1-148[»]
4CIUX-ray3.50A143-857[»]
ProteinModelPortaliP63284.

Miscellaneous databases

EvolutionaryTraceiP63284.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 143143N-terminal
Add
BLAST
Regioni159 – 340182NBD1
Add
BLAST
Regioni341 – 545205Linker
Add
BLAST
Regioni555 – 765211NBD2
Add
BLAST
Regioni766 – 85792C-terminal
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili391 – 525135 By similarity
Add
BLAST

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.4 Publications

Sequence similaritiesi

Belongs to the ClpA/ClpB family.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG0542.
HOGENOMiHOG000218211.
KOiK03695.
OMAiGENVNDQ.
OrthoDBiEOG65F8SM.
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.
IPR023150. Dbl_Clp-N.
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.
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. Align

Isoform ClpB (identifier: P63284-1) [UniParc]FASTA

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

MRLDRLTNKF QLALADAQSL ALGHDNQFIE PLHLMSALLN QEGGSVSPLL    50
TSAGINAGQL RTDINQALNR LPQVEGTGGD VQPSQDLVRV LNLCDKLAQK 100
RGDNFISSEL FVLAALESRG TLADILKAAG ATTANITQAI EQMRGGESVN 150
DQGAEDQRQA LKKYTIDLTE RAEQGKLDPV IGRDEEIRRT IQVLQRRTKN 200
NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKGRRVLAL DMGALVAGAK 250
YRGEFEERLK GVLNDLAKQE GNVILFIDEL HTMVGAGKAD GAMDAGNMLK 300
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVAE PSVEDTIAIL 350
RGLKERYELH HHVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS 400
IRMQIDSKPE ELDRLDRRII QLKLEQQALM KESDEASKKR LDMLNEELSD 450
KERQYSELEE EWKAEKASLS GTQTIKAELE QAKIAIEQAR RVGDLARMSE 500
LQYGKIPELE KQLEAATQLE GKTMRLLRNK VTDAEIAEVL ARWTGIPVSR 550
MMESEREKLL RMEQELHHRV IGQNEAVDAV SNAIRRSRAG LADPNRPIGS 600
FLFLGPTGVG KTELCKALAN FMFDSDEAMV RIDMSEFMEK HSVSRLVGAP 650
PGYVGYEEGG YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT 700
DGQGRTVDFR NTVVIMTSNL GSDLIQERFG ELDYAHMKEL VLGVVSHNFR 750
PEFINRIDEV VVFHPLGEQH IASIAQIQLK RLYKRLEERG YEIHISDEAL 800
KLLSENGYDP VYGARPLKRA IQQQIENPLA QQILSGELVP GKVIRLEVNE 850
DRIVAVQ 857
Length:857
Mass (Da):95,585
Last modified:October 11, 2004 - v1
Checksum:iFD38CD96B2F7C32A
GO
Isoform ClpB-3 (identifier: P63284-2) [UniParc]FASTA

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 148148Missing in isoform ClpB-3.
VSP_018703Add
BLAST
Alternative sequencei149 – 1491V → M in isoform ClpB-3.
VSP_018987

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 972KL → NV in AAA24422. 1 Publication
Sequence conflicti122 – 1221L → V in AAA24422. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
PIRiD35905. C65037.
RefSeqiNP_417083.1. NC_000913.3.
YP_490816.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75641; AAC75641; b2592.
BAA16476; BAA16476; BAA16476.
GeneIDi12931624.
947077.
KEGGiecj:Y75_p2541.
eco:b2592.
PATRICi32120587. VBIEscCol129921_2692.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi D35905. C65037.
RefSeqi NP_417083.1. NC_000913.3.
YP_490816.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JBK X-ray 1.80 A 159-351 [» ]
1KHY X-ray 1.95 A/B/C/D 1-148 [» ]
4CIU X-ray 3.50 A 143-857 [» ]
ProteinModelPortali P63284.
ModBasei Search...

Protein-protein interaction databases

BioGridi 851414. 30 interactions.
DIPi DIP-35844N.
IntActi P63284. 77 interactions.
MINTi MINT-1222117.
STRINGi 511145.b2592.

2D gel databases

SWISS-2DPAGEi P63284.

Proteomic databases

PaxDbi P63284.
PRIDEi P63284.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75641 ; AAC75641 ; b2592 .
BAA16476 ; BAA16476 ; BAA16476 .
GeneIDi 12931624.
947077.
KEGGi ecj:Y75_p2541.
eco:b2592.
PATRICi 32120587. VBIEscCol129921_2692.

Organism-specific databases

EchoBASEi EB0155.
EcoGenei EG10157. clpB.

Phylogenomic databases

eggNOGi COG0542.
HOGENOMi HOG000218211.
KOi K03695.
OMAi GENVNDQ.
OrthoDBi EOG65F8SM.
PhylomeDBi P63284.

Enzyme and pathway databases

BioCyci EcoCyc:EG10157-MONOMER.
ECOL316407:JW2573-MONOMER.
SABIO-RKi P63284.

Miscellaneous databases

EvolutionaryTracei P63284.
PROi P63284.

Gene expression databases

Genevestigatori P63284.

Family and domain databases

Gene3Di 1.10.1780.10. 1 hit.
3.40.50.300. 2 hits.
InterProi IPR003593. 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.
IPR023150. Dbl_Clp-N.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00004. AAA. 1 hit.
PF07724. AAA_2. 1 hit.
PF02861. Clp_N. 2 hits.
PF10431. ClpB_D2-small. 1 hit.
[Graphical view ]
PRINTSi PR00300. CLPPROTEASEA.
SMARTi SM00382. AAA. 2 hits.
SM01086. ClpB_D2-small. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
TIGRFAMsi TIGR03346. chaperone_ClpB. 1 hit.
PROSITEi PS00870. CLPAB_1. 1 hit.
PS00871. CLPAB_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Conservation of the regulatory subunit for the Clp ATP-dependent protease in prokaryotes and eukaryotes."
    Gottesman S., Squires C., Pichersky E., Carrington M., Hobbs M., Mattick J.S., Dalrymple B., Kuramitsu H., Shiroza T., Foster T., Clark W.P., Ross B., Squires C.L., Maurizi M.R.
    Proc. Natl. Acad. Sci. U.S.A. 87:3513-3517(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. "The complete genome sequence of Escherichia coli K-12."
    Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
    Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Expression of ClpB, an analog of the ATP-dependent protease regulatory subunit in Escherichia coli, is controlled by a heat shock sigma factor (sigma 32)."
    Kitagawa M., Wada C., Yoshioka S., Yura T.
    J. Bacteriol. 173:4247-4253(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-593.
    Strain: K12.
  6. "Nucleotide sequence of the rrnG ribosomal RNA promoter region of Escherichia coli."
    Shen W.-F., Squires C., Squires C.L.
    Nucleic Acids Res. 10:3303-3313(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 753-857.
  7. Ogura T., Tomoyasu T.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  8. "ClpB proteins copurify with the anaerobic Escherichia coli reductase."
    Pontis E., Sun X.Y., Joernvall H., Krook M., Reichard P.
    Biochem. Biophys. Res. Commun. 180:1222-1226(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-14; 150-157; 355-364 AND 452-460.
  9. "ClpB is the Escherichia coli heat shock protein F84.1."
    Squires C.L., Pedersen S., Ross B.M., Squires C.
    J. Bacteriol. 173:4254-4262(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A HEAT SHOCK PROTEIN.
  10. "Site-directed mutagenesis of the dual translational initiation sites of the clpB gene of Escherichia coli and characterization of its gene products."
    Park S.K., Kim K.I., Woo K.M., Seol J.H., Tanaka K., Ichihara A., Ha D.B., Chung C.H.
    J. Biol. Chem. 268:20170-20174(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE INITIATION, ATPASE ACTIVITY, SUBCELLULAR LOCATION.
  11. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  12. "Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli."
    Kim K.I., Cheong G.-W., Park S.-C., Ha J.-S., Woo K.M., Choi S.J., Chung C.H.
    J. Mol. Biol. 303:655-666(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, MUTAGENESIS OF LYS-212 AND LYS-611.
  13. "Structure and activity of ClpB from Escherichia coli. Role of the amino- and -carboxyl-terminal domains."
    Barnett M.E., Zolkiewska A., Zolkiewski M.
    J. Biol. Chem. 275:37565-37571(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF DOMAINS.
  14. "Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity."
    Mogk A., Schlieker C., Strub C., Rist W., Weibezahn J., Bukau B.
    J. Biol. Chem. 278:17615-17624(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF DOMAINS, MUTAGENESIS OF LYS-212; GLU-279; ARG-332; TRP-543; LYS-611; GLU-678; ARG-756 AND 813-GLY--ARG-815.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  15. "Characterization of a trap mutant of the AAA+ chaperone ClpB."
    Weibezahn J., Schlieker C., Bukau B., Mogk A.
    J. Biol. Chem. 278:32608-32617(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: BINDING TO PROTEIN AGGREGATES, INTERACTION WITH DNAK.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  16. "Structure and function of the middle domain of ClpB from Escherichia coli."
    Kedzierska S., Akoev V., Barnett M.E., Zolkiewski M.
    Biochemistry 42:14242-14248(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF MIDDLE DOMAIN.
  17. "Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB."
    Akoev V., Gogol E.P., Barnett M.E., Zolkiewski M.
    Protein Sci. 13:567-574(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: OLIGOMERIZATION, NUCLEOTIDE-BINDING.
    Strain: K12 / MC1000 / ATCC 39531.
  18. "Substrate recognition by the AAA+ chaperone ClpB."
    Schlieker C., Weibezahn J., Patzelt H., Tessarz P., Strub C., Zeth K., Erbse A., Schneider-Mergener J., Chin J.W., Schultz P.G., Bukau B., Mogk A.
    Nat. Struct. Mol. Biol. 11:607-615(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE-BINDING, MUTAGENESIS OF TYR-251; GLU-254 AND GLU-257.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  19. "Conserved amino acid residues within the amino-terminal domain of ClpB are essential for the chaperone activity."
    Liu Z., Tek V., Akoev V., Zolkiewski M.
    J. Mol. Biol. 321:111-120(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF THR-7; SER-84; ASP-103 AND GLU-109.
  20. "Site-directed mutagenesis of conserved charged amino acid residues in ClpB from Escherichia coli."
    Barnett M.E., Zolkiewski M.
    Biochemistry 41:11277-11283(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-212; LYS-611; ASP-797; ARG-815; ARG-819 AND GLU-826.
  21. "Cloning, expression, purification and preliminary X-ray crystallographic studies of Escherichia coli Hsp100 ClpB N-terminal domain."
    Li J., Sha B.
    Acta Crystallogr. D 57:1933-1935(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION OF N-TERMINAL DOMAIN.
  22. "Cloning, expression, purification and preliminary X-ray crystallographic studies of Escherichia coli Hsp100 nucleotide-binding domain 2 (NBD2)."
    Li J., Sha B.
    Acta Crystallogr. D 58:1030-1031(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION OF NBD2.
  23. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-96; LYS-176 AND LYS-640, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  24. "Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity."
    Li J., Sha B.
    J. Mol. Biol. 318:1127-1137(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 159-351.
  25. "Crystal structure of the E. coli Hsp100 ClpB N-terminal domain."
    Li J., Sha B.
    Structure 11:323-328(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 4-142, MUTAGENESIS OF LEU-93; LEU-97 AND LEU-110.

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: July 9, 2014
This is version 104 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. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene

External Data

Dasty 3

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