CLPB1_ARATH
ID CLPB1_ARATH Reviewed; 911 AA.
AC P42730; Q8W4F2; Q9LE57;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Chaperone protein ClpB1;
DE AltName: Full=ATP-dependent Clp protease ATP-binding subunit ClpB homolog 1;
DE AltName: Full=Casein lytic proteinase B1;
DE AltName: Full=Heat shock protein 101;
DE AltName: Full=Protein DEFECTIVE IN LONG-TERM ACQUIRED THERMOTOLERANCE {ECO:0000303|PubMed:23439916};
GN Name=CLPB1; Synonyms=DLT1 {ECO:0000303|PubMed:23439916}, HOT1, HSP101;
GN OrderedLocusNames=At1g74310; ORFNames=F1O17.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION BY HEAT STRESS.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7866032; DOI=10.2307/3869916;
RA Schirmer E.C., Lindquist S., Vierling E.;
RT "An Arabidopsis heat shock protein complements a thermotolerance defect in
RT yeast.";
RL Plant Cell 6:1899-1909(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION BY HEAT STRESS,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-637.
RC STRAIN=cv. Columbia;
RX PubMed=10760305; DOI=10.1073/pnas.97.8.4392;
RA Hong S.-W., Vierling E.;
RT "Mutants of Arabidopsis thaliana defective in the acquisition of tolerance
RT to high temperature stress.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4392-4397(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-460.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION BY HEAT STRESS.
RX PubMed=10760238; DOI=10.2307/3871063;
RA Queitsch C., Hong S.W., Vierling E., Lindquist S.;
RT "Heat shock protein 101 plays a crucial role in thermotolerance in
RT Arabidopsis.";
RL Plant Cell 12:479-492(2000).
RN [7]
RP FUNCTION, DEVELOPMENTAL STAGE, INDUCTION BY HEAT STRESS, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=11489180; DOI=10.1046/j.1365-313x.2001.01066.x;
RA Hong S.W., Vierling E.;
RT "Hsp101 is necessary for heat tolerance but dispensable for development and
RT germination in the absence of stress.";
RL Plant J. 27:25-35(2001).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF ALA-499; GLU-509; GLU-637; ARG-706 AND
RP GLY-815.
RX PubMed=15659638; DOI=10.1105/tpc.104.027540;
RA Lee U., Wie C., Escobar M., Williams B., Hong S.W., Vierling E.;
RT "Genetic analysis reveals domain interactions of Arabidopsis Hsp100/ClpB
RT and cooperation with the small heat shock protein chaperone system.";
RL Plant Cell 17:559-571(2005).
RN [9]
RP INDUCTION BY HEAT STRESS.
RX PubMed=16995899; DOI=10.1111/j.1365-313x.2006.02873.x;
RA Myouga F., Motohashi R., Kuromori T., Nagata N., Shinozaki K.;
RT "An Arabidopsis chloroplast-targeted Hsp101 homologue, APG6, has an
RT essential role in chloroplast development as well as heat-stress
RT response.";
RL Plant J. 48:249-260(2006).
RN [10]
RP INDUCTION BY OILSEED RAPE MOSAIC VIRUS.
RX PubMed=16644052; DOI=10.1016/j.virusres.2006.03.013;
RA Carr T., Wang Y., Huang Z., Yeakley J.M., Fan J.B., Whitham S.A.;
RT "Tobamovirus infection is independent of HSP101 mRNA induction and protein
RT expression.";
RL Virus Res. 121:33-41(2006).
RN [11]
RP FUNCTION, AND INDUCTION BY HEAT STRESS.
RX PubMed=17144892; DOI=10.1111/j.1365-313x.2006.02940.x;
RA Lee U., Rioflorido I., Hong S.W., Larkindale J., Waters E.R., Vierling E.;
RT "The Arabidopsis ClpB/Hsp100 family of proteins: chaperones for stress and
RT chloroplast development.";
RL Plant J. 49:115-127(2007).
RN [12]
RP FUNCTION, MUTAGENESIS OF HIS-33 AND THR-599, DISRUPTION PHENOTYPE, AND
RP INDUCTION BY HSA32.
RC STRAIN=cv. Columbia;
RX PubMed=23439916; DOI=10.1104/pp.112.212589;
RA Wu T.-Y., Juan Y.-T., Hsu Y.-H., Wu S.-H., Liao H.-T., Fung R.W.M.,
RA Charng Y.-Y.;
RT "Interplay between heat shock proteins HSP101 and HSA32 prolongs heat
RT acclimation memory posttranscriptionally in Arabidopsis.";
RL Plant Physiol. 161:2075-2084(2013).
CC -!- FUNCTION: Molecular chaperone that plays an important role in
CC thermotolerance. Together with HSA32, required for long-term acquired
CC thermotolerance (LAT) in plants and naturally high basal
CC thermotolerance observed in germinating seedlings.
CC {ECO:0000269|PubMed:10760238, ECO:0000269|PubMed:10760305,
CC ECO:0000269|PubMed:11489180, ECO:0000269|PubMed:15659638,
CC ECO:0000269|PubMed:17144892, ECO:0000269|PubMed:23439916,
CC ECO:0000269|PubMed:7866032}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Starts to accumulate in maturing seeds 15 days
CC after pollination and decreases rapidly during seed germination.
CC {ECO:0000269|PubMed:10760238, ECO:0000269|PubMed:11489180}.
CC -!- INDUCTION: By heat stress and oilseed rape mosaic virus
CC (PubMed:10760238, PubMed:10760305, PubMed:11489180, PubMed:16644052,
CC PubMed:16995899, PubMed:17144892, PubMed:7866032). Regulated by HSA32
CC that retards its decay in a positive feedback loop (at protein level)
CC during recovery after heat treatment (PubMed:23439916).
CC {ECO:0000269|PubMed:10760238, ECO:0000269|PubMed:10760305,
CC ECO:0000269|PubMed:11489180, ECO:0000269|PubMed:16644052,
CC ECO:0000269|PubMed:16995899, ECO:0000269|PubMed:17144892,
CC ECO:0000269|PubMed:23439916, ECO:0000269|PubMed:7866032}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but germinating seeds have greatly reduced basal
CC thermotolerance and are unable to acquire thermotolerance
CC (PubMed:10760305, PubMed:11489180). Faster degradation of HSA32 (at
CC protein level) (PubMed:23439916). {ECO:0000269|PubMed:10760305,
CC ECO:0000269|PubMed:11489180, ECO:0000269|PubMed:23439916}.
CC -!- MISCELLANEOUS: Over-expression of HSP101 partially reverse the
CC sensitivity of 14 day-old seedling to heat stress.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
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DR EMBL; U13949; AAA67927.1; -; mRNA.
DR EMBL; AF218796; AAF26423.1; -; Genomic_DNA.
DR EMBL; AC020579; AAG52410.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35576.1; -; Genomic_DNA.
DR EMBL; AY062596; AAL32674.1; -; mRNA.
DR PIR; F96771; F96771.
DR RefSeq; NP_565083.1; NM_106091.4.
DR AlphaFoldDB; P42730; -.
DR SMR; P42730; -.
DR BioGRID; 28990; 2.
DR IntAct; P42730; 1.
DR STRING; 3702.AT1G74310.1; -.
DR PaxDb; P42730; -.
DR PRIDE; P42730; -.
DR ProteomicsDB; 246581; -.
DR EnsemblPlants; AT1G74310.1; AT1G74310.1; AT1G74310.
DR GeneID; 843771; -.
DR Gramene; AT1G74310.1; AT1G74310.1; AT1G74310.
DR KEGG; ath:AT1G74310; -.
DR Araport; AT1G74310; -.
DR TAIR; locus:2019667; AT1G74310.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_2_1; -.
DR InParanoid; P42730; -.
DR OrthoDB; 611758at2759; -.
DR PhylomeDB; P42730; -.
DR PRO; PR:P42730; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P42730; baseline and differential.
DR Genevisible; P42730; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0045727; P:positive regulation of translation; IMP:TAIR.
DR GO; GO:0043335; P:protein unfolding; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
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; 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 PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Coiled coil; Cytoplasm; Nucleotide-binding;
KW Nucleus; Reference proteome; Repeat; Stress response.
FT CHAIN 1..911
FT /note="Chaperone protein ClpB1"
FT /id="PRO_0000191220"
FT DOMAIN 3..147
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 6..73
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 85..147
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 164..410
FT /note="I"
FT REGION 532..723
FT /note="II"
FT COILED 403..500
FT /evidence="ECO:0000255"
FT BINDING 207..214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 606..613
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 33
FT /note="H->Y: In dlt1-2; normal growth and development under
FT nonstress conditions. Impaired chaperone activity and
FT thermotolerance function, but normal positive regulation of
FT HSA32 during recovery after heat treatment."
FT /evidence="ECO:0000269|PubMed:23439916"
FT MUTAGEN 499
FT /note="A->T: In hot1-4; reduced basal thermotolerance and
FT unable to acquire thermotolerance."
FT /evidence="ECO:0000269|PubMed:15659638"
FT MUTAGEN 509
FT /note="E->K: In hot1-6; reduced ability to acquire
FT thermotolerance."
FT /evidence="ECO:0000269|PubMed:15659638"
FT MUTAGEN 599
FT /note="T->I: In dlt1-1; normal growth and development under
FT nonstress conditions, and normal chaperone activity and
FT thermotolerance function. Compromised positive regulation
FT of HSA32 during recovery after heat treatment."
FT /evidence="ECO:0000269|PubMed:23439916"
FT MUTAGEN 637
FT /note="E->K: In hot1-1; greatly reduced basal
FT thermotolerance and unable to acquire thermotolerance."
FT /evidence="ECO:0000269|PubMed:10760305,
FT ECO:0000269|PubMed:15659638"
FT MUTAGEN 706
FT /note="R->K: In hot1-5; unable to acquire thermotolerance."
FT /evidence="ECO:0000269|PubMed:15659638"
FT MUTAGEN 815
FT /note="G->D: In hot1-7; reduced ability to acquire
FT thermotolerance."
FT /evidence="ECO:0000269|PubMed:15659638"
FT CONFLICT 141
FT /note="V -> F (in Ref. 5; AAL32674)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="P -> A (in Ref. 1; AAA67927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 911 AA; 101295 MW; 191EC1853B0C4CB9 CRC64;
MNPEKFTHKT NETIATAHEL AVNAGHAQFT PLHLAGALIS DPTGIFPQAI SSAGGENAAQ
SAERVINQAL KKLPSQSPPP DDIPASSSLI KVIRRAQAAQ KSRGDTHLAV DQLIMGLLED
SQIRDLLNEV GVATARVKSE VEKLRGKEGK KVESASGDTN FQALKTYGRD LVEQAGKLDP
VIGRDEEIRR VVRILSRRTK NNPVLIGEPG VGKTAVVEGL AQRIVKGDVP NSLTDVRLIS
LDMGALVAGA KYRGEFEERL KSVLKEVEDA EGKVILFIDE IHLVLGAGKT EGSMDAANLF
KPMLARGQLR CIGATTLEEY RKYVEKDAAF ERRFQQVYVA EPSVPDTISI LRGLKEKYEG
HHGVRIQDRA LINAAQLSAR YITGRHLPDK AIDLVDEACA NVRVQLDSQP EEIDNLERKR
MQLEIELHAL EREKDKASKA RLIEVRKELD DLRDKLQPLT MKYRKEKERI DEIRRLKQKR
EELMFSLQEA ERRYDLARAA DLRYGAIQEV ESAIAQLEGT SSEENVMLTE NVGPEHIAEV
VSRWTGIPVT RLGQNEKERL IGLADRLHKR VVGQNQAVNA VSEAILRSRA GLGRPQQPTG
SFLFLGPTGV GKTELAKALA EQLFDDENLL VRIDMSEYME QHSVSRLIGA PPGYVGHEEG
GQLTEAVRRR PYCVILFDEV EKAHVAVFNT LLQVLDDGRL TDGQGRTVDF RNSVIIMTSN
LGAEHLLAGL TGKVTMEVAR DCVMREVRKH FRPELLNRLD EIVVFDPLSH DQLRKVARLQ
MKDVAVRLAE RGVALAVTDA ALDYILAESY DPVYGARPIR RWMEKKVVTE LSKMVVREEI
DENSTVYIDA GAGDLVYRVE SGGLVDASTG KKSDVLIHIA NGPKRSDAAQ AVKKMRIEEI
EDDDNEEMIE D
