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P63284

- CLPB_ECOLI

UniProt

P63284 - CLPB_ECOLI

Protein

Chaperone protein ClpB

Gene

clpB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    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 binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. nucleoside-triphosphatase activity Source: InterPro
    4. protein binding Source: IntAct

    GO - Biological processi

    1. protein processing Source: InterPro
    2. response to heat Source: InterPro
    3. response to unfolded protein Source: EcoCyc

    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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10157. clpB.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. membrane Source: UniProtKB

    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.
    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 ClpBPRO_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-2DPAGEP63284.

    Expressioni

    Inductioni

    By heat shock and other environmental stresses.

    Gene expression databases

    GenevestigatoriP63284.

    Interactioni

    Subunit structurei

    Homohexamer. The oligomerization is ATP-dependent.1 Publication

    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

    1
    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
    Beta strandi363 – 3653
    Helixi367 – 38014
    Helixi388 – 40619
    Helixi410 – 42920
    Helixi444 – 49249
    Helixi496 – 5038
    Helixi505 – 52319
    Helixi533 – 54412
    Helixi549 – 5524
    Helixi555 – 5606
    Helixi562 – 5698
    Helixi574 – 58916
    Beta strandi598 – 6058
    Beta strandi607 – 6104
    Helixi611 – 62313
    Beta strandi624 – 63310
    Helixi634 – 6363
    Helixi640 – 6456
    Helixi661 – 6688
    Beta strandi673 – 6786
    Helixi679 – 6813
    Helixi684 – 69613
    Beta strandi697 – 7004
    Beta strandi706 – 7083
    Beta strandi713 – 7197
    Helixi722 – 7265
    Turni734 – 7363
    Helixi737 – 74812
    Helixi751 – 7566
    Beta strandi757 – 7626
    Helixi768 – 78821
    Beta strandi792 – 7954
    Helixi797 – 80711
    Turni810 – 8123
    Turni814 – 8163
    Helixi817 – 8248
    Helixi826 – 83510
    Beta strandi836 – 8383
    Beta strandi842 – 8498
    Beta strandi852 – 8576

    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[»]
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP63284.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 143143N-terminalAdd
    BLAST
    Regioni159 – 340182NBD1Add
    BLAST
    Regioni341 – 545205LinkerAdd
    BLAST
    Regioni555 – 765211NBD2Add
    BLAST
    Regioni766 – 85792C-terminalAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili391 – 525135By similarityAdd
    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.

    Sequence similaritiesi

    Belongs to the ClpA/ClpB family.Curated

    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]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

    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]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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 972KL → NV in AAA24422. (PubMed:2185473)Curated
    Sequence conflicti122 – 1221L → V in AAA24422. (PubMed:2185473)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 148148Missing in isoform ClpB-3. CuratedVSP_018703Add
    BLAST
    Alternative sequencei149 – 1491V → M in isoform ClpB-3. CuratedVSP_018987

    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.
    PIRiC65037. D35905.
    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 C65037. D35905.
    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 [» ]
    4D2Q electron microscopy 18.00 A/B/C/D/E/F 1-857 [» ]
    4D2U electron microscopy 17.00 A/B/C/D/E/F 1-857 [» ]
    4D2X electron microscopy 20.00 A/B/C/D/E/F 1-857 [» ]
    ProteinModelPortali P63284.
    ModBasei Search...
    MobiDBi 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-2DPAGE 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-RK 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

    1. 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. 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. 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 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: October 1, 2014
    This is version 106 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

    External Data

    Dasty 3