CLPB_ECOLI
ID CLPB_ECOLI Reviewed; 857 AA.
AC P63284; P03815;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Chaperone protein ClpB;
DE AltName: Full=Heat shock protein F84.1;
GN Name=clpB; Synonyms=htpM; OrderedLocusNames=b2592, JW2573;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2185473; DOI=10.1073/pnas.87.9.3513;
RA Gottesman S., Squires C., Pichersky E., Carrington M., Hobbs M.,
RA Mattick J.S., Dalrymple B., Kuramitsu H., Shiroza T., Foster T.,
RA Clark W.P., Ross B., Squires C.L., Maurizi M.R.;
RT "Conservation of the regulatory subunit for the Clp ATP-dependent protease
RT in prokaryotes and eukaryotes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3513-3517(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-593.
RC STRAIN=K12;
RX PubMed=1906060; DOI=10.1128/jb.173.14.4247-4253.1991;
RA Kitagawa M., Wada C., Yoshioka S., Yura T.;
RT "Expression of ClpB, an analog of the ATP-dependent protease regulatory
RT subunit in Escherichia coli, is controlled by a heat shock sigma factor
RT (sigma 32).";
RL J. Bacteriol. 173:4247-4253(1991).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 753-857.
RX PubMed=6285294; DOI=10.1093/nar/10.10.3303;
RA Shen W.-F., Squires C., Squires C.L.;
RT "Nucleotide sequence of the rrnG ribosomal RNA promoter region of
RT Escherichia coli.";
RL Nucleic Acids Res. 10:3303-3313(1982).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Ogura T., Tomoyasu T.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 1-14; 150-157; 355-364 AND 452-460.
RX PubMed=1953774; DOI=10.1016/s0006-291x(05)81326-9;
RA Pontis E., Sun X.Y., Joernvall H., Krook M., Reichard P.;
RT "ClpB proteins copurify with the anaerobic Escherichia coli reductase.";
RL Biochem. Biophys. Res. Commun. 180:1222-1226(1991).
RN [9]
RP IDENTIFICATION AS A HEAT SHOCK PROTEIN.
RX PubMed=2066329; DOI=10.1128/jb.173.14.4254-4262.1991;
RA Squires C.L., Pedersen S., Ross B.M., Squires C.;
RT "ClpB is the Escherichia coli heat shock protein F84.1.";
RL J. Bacteriol. 173:4254-4262(1991).
RN [10]
RP ALTERNATIVE INITIATION, ATPASE ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=8376377; DOI=10.1016/s0021-9258(20)80709-1;
RA Park S.K., Kim K.I., Woo K.M., Seol J.H., Tanaka K., Ichihara A., Ha D.B.,
RA Chung C.H.;
RT "Site-directed mutagenesis of the dual translational initiation sites of
RT the clpB gene of Escherichia coli and characterization of its gene
RT products.";
RL J. Biol. Chem. 268:20170-20174(1993).
RN [11]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [12]
RP SUBUNIT, AND MUTAGENESIS OF LYS-212 AND LYS-611.
RX PubMed=11061966; DOI=10.1006/jmbi.2000.4165;
RA Kim K.I., Cheong G.-W., Park S.-C., Ha J.-S., Woo K.M., Choi S.J.,
RA Chung C.H.;
RT "Heptameric ring structure of the heat-shock protein ClpB, a protein-
RT activated ATPase in Escherichia coli.";
RL J. Mol. Biol. 303:655-666(2000).
RN [13]
RP FUNCTION OF DOMAINS.
RX PubMed=10982797; DOI=10.1074/jbc.m005211200;
RA Barnett M.E., Zolkiewska A., Zolkiewski M.;
RT "Structure and activity of ClpB from Escherichia coli. Role of the
RT amino- and -carboxyl-terminal domains.";
RL J. Biol. Chem. 275:37565-37571(2000).
RN [14]
RP FUNCTION OF DOMAINS, AND MUTAGENESIS OF LYS-212; GLU-279; ARG-332; TRP-543;
RP LYS-611; GLU-678; ARG-756 AND 813-GLY--ARG-815.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12624113; DOI=10.1074/jbc.m209686200;
RA Mogk A., Schlieker C., Strub C., Rist W., Weibezahn J., Bukau B.;
RT "Roles of individual domains and conserved motifs of the AAA+ chaperone
RT ClpB in oligomerization, ATP hydrolysis, and chaperone activity.";
RL J. Biol. Chem. 278:17615-17624(2003).
RN [15]
RP BINDING TO PROTEIN AGGREGATES, AND INTERACTION WITH DNAK.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12805357; DOI=10.1074/jbc.m303653200;
RA Weibezahn J., Schlieker C., Bukau B., Mogk A.;
RT "Characterization of a trap mutant of the AAA+ chaperone ClpB.";
RL J. Biol. Chem. 278:32608-32617(2003).
RN [16]
RP FUNCTION OF MIDDLE DOMAIN.
RX PubMed=14640692; DOI=10.1021/bi035573d;
RA Kedzierska S., Akoev V., Barnett M.E., Zolkiewski M.;
RT "Structure and function of the middle domain of ClpB from Escherichia
RT coli.";
RL Biochemistry 42:14242-14248(2003).
RN [17]
RP OLIGOMERIZATION, AND NUCLEOTIDE-BINDING.
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=14978298; DOI=10.1110/ps.03422604;
RA Akoev V., Gogol E.P., Barnett M.E., Zolkiewski M.;
RT "Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB.";
RL Protein Sci. 13:567-574(2004).
RN [18]
RP SUBSTRATE-BINDING, AND MUTAGENESIS OF TYR-251; GLU-254 AND GLU-257.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=15208691; DOI=10.1038/nsmb787;
RA Schlieker C., Weibezahn J., Patzelt H., Tessarz P., Strub C., Zeth K.,
RA Erbse A., Schneider-Mergener J., Chin J.W., Schultz P.G., Bukau B.,
RA Mogk A.;
RT "Substrate recognition by the AAA+ chaperone ClpB.";
RL Nat. Struct. Mol. Biol. 11:607-615(2004).
RN [19]
RP MUTAGENESIS OF THR-7; SER-84; ASP-103 AND GLU-109.
RX PubMed=12139937; DOI=10.1016/s0022-2836(02)00591-0;
RA Liu Z., Tek V., Akoev V., Zolkiewski M.;
RT "Conserved amino acid residues within the amino-terminal domain of ClpB are
RT essential for the chaperone activity.";
RL J. Mol. Biol. 321:111-120(2002).
RN [20]
RP MUTAGENESIS OF LYS-212; LYS-611; ASP-797; ARG-815; ARG-819 AND GLU-826.
RX PubMed=12220194; DOI=10.1021/bi026161s;
RA Barnett M.E., Zolkiewski M.;
RT "Site-directed mutagenesis of conserved charged amino acid residues in ClpB
RT from Escherichia coli.";
RL Biochemistry 41:11277-11283(2002).
RN [21]
RP CRYSTALLIZATION OF N-TERMINAL DOMAIN.
RX PubMed=11717522; DOI=10.1107/s0907444901017322;
RA Li J., Sha B.;
RT "Cloning, expression, purification and preliminary X-ray crystallographic
RT studies of Escherichia coli Hsp100 ClpB N-terminal domain.";
RL Acta Crystallogr. D 57:1933-1935(2001).
RN [22]
RP CRYSTALLIZATION OF NBD2.
RX PubMed=12037306; DOI=10.1107/s0907444902006327;
RA Li J., Sha B.;
RT "Cloning, expression, purification and preliminary X-ray crystallographic
RT studies of Escherichia coli Hsp100 nucleotide-binding domain 2 (NBD2).";
RL Acta Crystallogr. D 58:1030-1031(2002).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-96; LYS-176 AND LYS-640, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 159-351.
RX PubMed=12054807; DOI=10.1016/s0022-2836(02)00188-2;
RA Li J., Sha B.;
RT "Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1
RT (NBD1) and mechanistic studies on ClpB ATPase activity.";
RL J. Mol. Biol. 318:1127-1137(2002).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 4-142, AND MUTAGENESIS OF LEU-93;
RP LEU-97 AND LEU-110.
RX PubMed=12623019; DOI=10.1016/s0969-2126(03)00030-3;
RA Li J., Sha B.;
RT "Crystal structure of the E. coli Hsp100 ClpB N-terminal domain.";
RL Structure 11:323-328(2003).
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the
CC processing of protein aggregates. Protein binding stimulates the ATPase
CC activity; ATP hydrolysis unfolds the denatured protein aggregates,
CC which probably helps expose new hydrophobic binding sites on the
CC surface of ClpB-bound aggregates, contributing to the solubilization
CC and refolding of denatured protein aggregates by DnaK.
CC {ECO:0000269|PubMed:10982797, ECO:0000269|PubMed:12624113,
CC ECO:0000269|PubMed:14640692}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000269|PubMed:11061966}.
CC -!- INTERACTION:
CC P63284; P63284: clpB; NbExp=4; IntAct=EBI-546182, EBI-546182;
CC P63284; P0A6Y8: dnaK; NbExp=8; IntAct=EBI-546182, EBI-542092;
CC P63284; P33014: yeeD; NbExp=3; IntAct=EBI-546182, EBI-9130839;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8376377}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=ClpB;
CC IsoId=P63284-1; Sequence=Displayed;
CC Name=ClpB-3;
CC IsoId=P63284-2; Sequence=VSP_018703, VSP_018987;
CC -!- INDUCTION: By heat shock and other environmental stresses.
CC -!- DOMAIN: The Clp repeat (R) domain probably functions as a substrate-
CC discriminating domain, recruiting aggregated proteins to the ClpB
CC hexamer and/or stabilizing bound proteins. The NBD2 domain is
CC responsible for oligomerization, whereas the NBD1 domain stabilizes the
CC hexamer probably in an ATP-dependent manner. The movement of the
CC coiled-coil domain is essential for ClpB ability to rescue proteins
CC from an aggregated state, probably by pulling apart large aggregated
CC proteins, which are bound between the coiled-coils motifs of adjacent
CC ClpB subunits in the functional hexamer.
CC -!- MISCELLANEOUS: One peptide binds per ClpB hexamer; the binding site is
CC formed only upon ATP-driven oligomerization.
CC -!- MISCELLANEOUS: [Isoform ClpB-3]: ClpB-3 ATPase activity is not
CC activated by proteins, as it is in ClpB. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; M29364; AAA24422.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75641.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16476.1; -; Genomic_DNA.
DR EMBL; X57620; CAA40846.1; -; Genomic_DNA.
DR EMBL; V00350; CAA23639.1; -; Genomic_DNA.
DR EMBL; U50134; AAA92959.1; -; Genomic_DNA.
DR PIR; C65037; D35905.
DR RefSeq; NP_417083.1; NC_000913.3.
DR RefSeq; WP_001235102.1; NZ_STEB01000040.1.
DR PDB; 1JBK; X-ray; 1.80 A; A=159-351.
DR PDB; 1KHY; X-ray; 1.95 A; A/B/C/D=1-148.
DR PDB; 4CIU; X-ray; 3.50 A; A=143-857.
DR PDB; 4D2Q; EM; 18.00 A; A/B/C/D/E/F=1-857.
DR PDB; 4D2U; EM; 17.00 A; A/B/C/D/E/F=1-857.
DR PDB; 4D2X; EM; 20.00 A; A/B/C/D/E/F=1-857.
DR PDB; 5OFO; EM; 4.60 A; A/B/C/D/E/F=1-721, A/B/C/D/E/F=750-857.
DR PDB; 5OG1; EM; 4.50 A; A/B/C/D/E/F=1-721, A/B/C/D/E/F=750-857.
DR PDB; 6OAX; EM; 2.90 A; A/B/C/D/E/F=1-857.
DR PDB; 6OAY; EM; 3.30 A; A/B/C/D/E/F=1-857.
DR PDB; 6OG1; EM; 3.30 A; A/F=1-857.
DR PDB; 6OG2; EM; 4.10 A; A/F=1-857.
DR PDB; 6OG3; EM; 4.10 A; A/C/E=1-857.
DR PDB; 6QS6; EM; 3.90 A; A/B/C/D/E/F=1-857.
DR PDB; 6QS7; EM; 3.80 A; A/B/C/D/E/F=1-857.
DR PDB; 6QS8; EM; 3.90 A; A/B/C/D/E/F=1-857.
DR PDBsum; 1JBK; -.
DR PDBsum; 1KHY; -.
DR PDBsum; 4CIU; -.
DR PDBsum; 4D2Q; -.
DR PDBsum; 4D2U; -.
DR PDBsum; 4D2X; -.
DR PDBsum; 5OFO; -.
DR PDBsum; 5OG1; -.
DR PDBsum; 6OAX; -.
DR PDBsum; 6OAY; -.
DR PDBsum; 6OG1; -.
DR PDBsum; 6OG2; -.
DR PDBsum; 6OG3; -.
DR PDBsum; 6QS6; -.
DR PDBsum; 6QS7; -.
DR PDBsum; 6QS8; -.
DR AlphaFoldDB; P63284; -.
DR SMR; P63284; -.
DR BioGRID; 4260618; 221.
DR BioGRID; 851414; 32.
DR DIP; DIP-35844N; -.
DR IntAct; P63284; 81.
DR MINT; P63284; -.
DR STRING; 511145.b2592; -.
DR MEROPS; X20.002; -.
DR CarbonylDB; P63284; -.
DR iPTMnet; P63284; -.
DR SWISS-2DPAGE; P63284; -.
DR jPOST; P63284; -.
DR PaxDb; P63284; -.
DR PRIDE; P63284; -.
DR EnsemblBacteria; AAC75641; AAC75641; b2592.
DR EnsemblBacteria; BAA16476; BAA16476; BAA16476.
DR GeneID; 66673518; -.
DR GeneID; 947077; -.
DR KEGG; ecj:JW2573; -.
DR KEGG; eco:b2592; -.
DR PATRIC; fig|1411691.4.peg.4145; -.
DR EchoBASE; EB0155; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_0_6; -.
DR InParanoid; P63284; -.
DR OMA; SKMMQGE; -.
DR PhylomeDB; P63284; -.
DR BioCyc; EcoCyc:EG10157-MON; -.
DR BioCyc; MetaCyc:EG10157-MON; -.
DR BRENDA; 3.6.4.10; 2026.
DR SABIO-RK; P63284; -.
DR EvolutionaryTrace; P63284; -.
DR PRO; PR:P63284; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR Gene3D; 1.10.1780.10; -; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017730; Chaperonin_ClpB.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; ATP-binding; Chaperone;
KW Coiled coil; Cytoplasm; Direct protein sequencing; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response.
FT CHAIN 1..857
FT /note="Chaperone protein ClpB"
FT /id="PRO_0000005491"
FT DOMAIN 3..146
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..71
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 83..146
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 159..340
FT /note="NBD1"
FT REGION 341..545
FT /note="Linker"
FT REGION 555..765
FT /note="NBD2"
FT REGION 766..857
FT /note="C-terminal"
FT COILED 391..525
FT /evidence="ECO:0000250"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT BINDING 605..612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT MOD_RES 96
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 176
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MOD_RES 640
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT VAR_SEQ 1..148
FT /note="Missing (in isoform ClpB-3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018703"
FT VAR_SEQ 149
FT /note="V -> M (in isoform ClpB-3)"
FT /evidence="ECO:0000305"
FT /id="VSP_018987"
FT MUTAGEN 7
FT /note="T->A: Loss of chaperone activity."
FT /evidence="ECO:0000269|PubMed:12139937"
FT MUTAGEN 84
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:12139937"
FT MUTAGEN 93
FT /note="L->Q: Loss of chaperone activity. Retains ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:12623019"
FT MUTAGEN 97
FT /note="L->Q: 75% decrease in chaperone activity; retains
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:12623019"
FT MUTAGEN 103
FT /note="D->A: Loss of chaperone activity."
FT /evidence="ECO:0000269|PubMed:12139937"
FT MUTAGEN 109
FT /note="E->A: Loss of chaperone activity."
FT /evidence="ECO:0000269|PubMed:12139937"
FT MUTAGEN 110
FT /note="L->Q: 30% decrease in chaperone activity; retains
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:12623019"
FT MUTAGEN 212
FT /note="K->T: Loss of ability to form oligomers even in the
FT presence of ATP. Loss of chaperone activity."
FT /evidence="ECO:0000269|PubMed:11061966,
FT ECO:0000269|PubMed:12220194, ECO:0000269|PubMed:12624113"
FT MUTAGEN 251
FT /note="Y->A: Decrease in ability to disaggregate proteins
FT due to decreased substrate-binding activity. Retains
FT hexameric quaternary structure and ATPase activity."
FT /evidence="ECO:0000269|PubMed:15208691"
FT MUTAGEN 254
FT /note="E->A: Decrease in ability to disaggregate proteins
FT due to decreased substrate-binding activity. Retains
FT hexameric quaternary structure and ATPase activity; when
FT associated with A-257."
FT /evidence="ECO:0000269|PubMed:15208691"
FT MUTAGEN 257
FT /note="E->A: Decrease in ability to disaggregate proteins
FT due to decreased substrate-binding activity. Retains
FT hexameric quaternary structure and ATPase activity; when
FT associated with A-254."
FT /evidence="ECO:0000269|PubMed:15208691"
FT MUTAGEN 279
FT /note="E->A: No effect on oligomerization."
FT /evidence="ECO:0000269|PubMed:12624113"
FT MUTAGEN 332
FT /note="R->A: Loss of ability to form oligomers."
FT /evidence="ECO:0000269|PubMed:12624113"
FT MUTAGEN 543
FT /note="W->F: No effect on chaperone activity or ability to
FT form oligomers."
FT /evidence="ECO:0000269|PubMed:12624113"
FT MUTAGEN 611
FT /note="K->T: No effect on ability to form oligomers. Loss
FT of chaperone activity."
FT /evidence="ECO:0000269|PubMed:11061966,
FT ECO:0000269|PubMed:12220194, ECO:0000269|PubMed:12624113"
FT MUTAGEN 678
FT /note="E->A: No effect on oligomerization."
FT /evidence="ECO:0000269|PubMed:12624113"
FT MUTAGEN 756
FT /note="R->A: No effect on oligomerization. Loss of ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:12624113"
FT MUTAGEN 797
FT /note="D->A: No effect."
FT /evidence="ECO:0000269|PubMed:12220194"
FT MUTAGEN 813..815
FT /note="GAR->AAA: No effect on oligomerization."
FT /evidence="ECO:0000269|PubMed:12624113"
FT MUTAGEN 815
FT /note="R->A: Loss of ability to form oligomers; loss of
FT chaperone activity."
FT /evidence="ECO:0000269|PubMed:12220194"
FT MUTAGEN 819
FT /note="R->A: Loss of ability to form oligomers; loss of
FT chaperone activity."
FT /evidence="ECO:0000269|PubMed:12220194"
FT MUTAGEN 826
FT /note="E->A: No effect."
FT /evidence="ECO:0000269|PubMed:12220194"
FT CONFLICT 96..97
FT /note="KL -> NV (in Ref. 1; AAA24422)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="L -> V (in Ref. 1; AAA24422)"
FT /evidence="ECO:0000305"
FT HELIX 8..23
FT /evidence="ECO:0007829|PDB:1KHY"
FT STRAND 27..29
FT /evidence="ECO:0007829|PDB:1KHY"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:1KHY"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:1KHY"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:1KHY"
FT HELIX 85..101
FT /evidence="ECO:0007829|PDB:1KHY"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:1KHY"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:1KHY"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:1KHY"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:1KHY"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:1JBK"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:1JBK"
FT HELIX 168..173
FT /evidence="ECO:0007829|PDB:1JBK"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:1JBK"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1JBK"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:1JBK"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:1JBK"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:1JBK"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1JBK"
FT HELIX 242..246
FT /evidence="ECO:0007829|PDB:1JBK"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:1JBK"
FT HELIX 252..268
FT /evidence="ECO:0007829|PDB:1JBK"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:1JBK"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:1JBK"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:1JBK"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 296..304
FT /evidence="ECO:0007829|PDB:1JBK"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:6OAY"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:1JBK"
FT HELIX 316..322
FT /evidence="ECO:0007829|PDB:1JBK"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:1JBK"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:1JBK"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:1JBK"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:1JBK"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:6OG1"
FT HELIX 354..361
FT /evidence="ECO:0007829|PDB:6OAX"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:4CIU"
FT HELIX 367..380
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 387..406
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 410..429
FT /evidence="ECO:0007829|PDB:4CIU"
FT HELIX 444..492
FT /evidence="ECO:0007829|PDB:4CIU"
FT HELIX 496..503
FT /evidence="ECO:0007829|PDB:4CIU"
FT HELIX 505..523
FT /evidence="ECO:0007829|PDB:4CIU"
FT HELIX 533..543
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:6OG1"
FT STRAND 551..553
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 555..560
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 562..566
FT /evidence="ECO:0007829|PDB:6OAX"
FT TURN 567..569
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 574..588
FT /evidence="ECO:0007829|PDB:6OAX"
FT STRAND 598..604
FT /evidence="ECO:0007829|PDB:6OAX"
FT STRAND 607..610
FT /evidence="ECO:0007829|PDB:6OG1"
FT HELIX 611..622
FT /evidence="ECO:0007829|PDB:6OAX"
FT STRAND 629..633
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 634..636
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 640..645
FT /evidence="ECO:0007829|PDB:6OAX"
FT STRAND 651..653
FT /evidence="ECO:0007829|PDB:6OAY"
FT HELIX 656..658
FT /evidence="ECO:0007829|PDB:6OAY"
FT HELIX 661..668
FT /evidence="ECO:0007829|PDB:6OAX"
FT STRAND 673..677
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 679..681
FT /evidence="ECO:0007829|PDB:6OAX"
FT TURN 684..686
FT /evidence="ECO:0007829|PDB:6OAY"
FT TURN 687..690
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 691..695
FT /evidence="ECO:0007829|PDB:6OAX"
FT STRAND 696..700
FT /evidence="ECO:0007829|PDB:6OAX"
FT STRAND 702..705
FT /evidence="ECO:0007829|PDB:6OG1"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:6OAX"
FT STRAND 713..718
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 722..728
FT /evidence="ECO:0007829|PDB:6OAX"
FT TURN 729..731
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 734..737
FT /evidence="ECO:0007829|PDB:6OAX"
FT TURN 742..748
FT /evidence="ECO:0007829|PDB:6OAY"
FT STRAND 751..762
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 768..787
FT /evidence="ECO:0007829|PDB:6OAX"
FT TURN 788..790
FT /evidence="ECO:0007829|PDB:6OAX"
FT STRAND 792..795
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 797..806
FT /evidence="ECO:0007829|PDB:6OAX"
FT TURN 811..814
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 815..824
FT /evidence="ECO:0007829|PDB:6OAX"
FT HELIX 826..834
FT /evidence="ECO:0007829|PDB:6OAX"
FT STRAND 836..838
FT /evidence="ECO:0007829|PDB:6OG1"
FT STRAND 842..856
FT /evidence="ECO:0007829|PDB:6OAX"
SQ SEQUENCE 857 AA; 95585 MW; FD38CD96B2F7C32A CRC64;
MRLDRLTNKF QLALADAQSL ALGHDNQFIE PLHLMSALLN QEGGSVSPLL TSAGINAGQL
RTDINQALNR LPQVEGTGGD VQPSQDLVRV LNLCDKLAQK RGDNFISSEL FVLAALESRG
TLADILKAAG ATTANITQAI EQMRGGESVN DQGAEDQRQA LKKYTIDLTE RAEQGKLDPV
IGRDEEIRRT IQVLQRRTKN NPVLIGEPGV GKTAIVEGLA QRIINGEVPE GLKGRRVLAL
DMGALVAGAK YRGEFEERLK GVLNDLAKQE GNVILFIDEL HTMVGAGKAD GAMDAGNMLK
PALARGELHC VGATTLDEYR QYIEKDAALE RRFQKVFVAE PSVEDTIAIL RGLKERYELH
HHVQITDPAI VAAATLSHRY IADRQLPDKA IDLIDEAASS IRMQIDSKPE ELDRLDRRII
QLKLEQQALM KESDEASKKR LDMLNEELSD KERQYSELEE EWKAEKASLS GTQTIKAELE
QAKIAIEQAR RVGDLARMSE LQYGKIPELE KQLEAATQLE GKTMRLLRNK VTDAEIAEVL
ARWTGIPVSR MMESEREKLL RMEQELHHRV IGQNEAVDAV SNAIRRSRAG LADPNRPIGS
FLFLGPTGVG KTELCKALAN FMFDSDEAMV RIDMSEFMEK HSVSRLVGAP PGYVGYEEGG
YLTEAVRRRP YSVILLDEVE KAHPDVFNIL LQVLDDGRLT DGQGRTVDFR NTVVIMTSNL
GSDLIQERFG ELDYAHMKEL VLGVVSHNFR PEFINRIDEV VVFHPLGEQH IASIAQIQLK
RLYKRLEERG YEIHISDEAL KLLSENGYDP VYGARPLKRA IQQQIENPLA QQILSGELVP
GKVIRLEVNE DRIVAVQ
