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Chaperone protein ClpB1 (ATP-dependent Clp protease ATP-binding subunit ClpB homolog 1) (Casein lytic proteinase B1) (Heat shock protein 101) (Protein DEFECTIVE IN LONG-TERM ACQUIRED THERMOTOLERANCE)

 CLPB1_ARATH             Reviewed;         911 AA.
P42730; Q8W4F2; Q9LE57;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
27-MAY-2002, sequence version 2.
07-JUN-2017, entry version 133.
RecName: Full=Chaperone protein ClpB1;
AltName: Full=ATP-dependent Clp protease ATP-binding subunit ClpB homolog 1;
AltName: Full=Casein lytic proteinase B1;
AltName: Full=Heat shock protein 101;
AltName: Full=Protein DEFECTIVE IN LONG-TERM ACQUIRED THERMOTOLERANCE {ECO:0000303|PubMed:23439916};
Name=CLPB1; Synonyms=DLT1 {ECO:0000303|PubMed:23439916}, HOT1, HSP101;
OrderedLocusNames=At1g74310; ORFNames=F1O17.2;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION BY HEAT STRESS.
STRAIN=cv. Columbia; TISSUE=Leaf;
PubMed=7866032; DOI=10.1105/tpc.6.12.1899;
Schirmer E.C., Lindquist S., Vierling E.;
"An Arabidopsis heat shock protein complements a thermotolerance
defect in yeast.";
Plant Cell 6:1899-1909(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION BY HEAT STRESS,
DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-637.
STRAIN=cv. Columbia;
PubMed=10760305; DOI=10.1073/pnas.97.8.4392;
Hong S.-W., Vierling E.;
"Mutants of Arabidopsis thaliana defective in the acquisition of
tolerance to high temperature stress.";
Proc. Natl. Acad. Sci. U.S.A. 97:4392-4397(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-460.
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[6]
FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION BY HEAT STRESS.
PubMed=10760238; DOI=10.1105/tpc.12.4.479;
Queitsch C., Hong S.W., Vierling E., Lindquist S.;
"Heat shock protein 101 plays a crucial role in thermotolerance in
Arabidopsis.";
Plant Cell 12:479-492(2000).
[7]
FUNCTION, DEVELOPMENTAL STAGE, INDUCTION BY HEAT STRESS, AND
DISRUPTION PHENOTYPE.
PubMed=11489180; DOI=10.1046/j.1365-313x.2001.01066.x;
Hong S.W., Vierling E.;
"Hsp101 is necessary for heat tolerance but dispensable for
development and germination in the absence of stress.";
Plant J. 27:25-35(2001).
[8]
FUNCTION, AND MUTAGENESIS OF ALA-499; GLU-509; GLU-637; ARG-706 AND
GLY-815.
PubMed=15659638; DOI=10.1105/tpc.104.027540;
Lee U., Wie C., Escobar M., Williams B., Hong S.W., Vierling E.;
"Genetic analysis reveals domain interactions of Arabidopsis
Hsp100/ClpB and cooperation with the small heat shock protein
chaperone system.";
Plant Cell 17:559-571(2005).
[9]
INDUCTION BY HEAT STRESS.
PubMed=16995899; DOI=10.1111/j.1365-313X.2006.02873.x;
Myouga F., Motohashi R., Kuromori T., Nagata N., Shinozaki K.;
"An Arabidopsis chloroplast-targeted Hsp101 homologue, APG6, has an
essential role in chloroplast development as well as heat-stress
response.";
Plant J. 48:249-260(2006).
[10]
INDUCTION BY OILSEED RAPE MOSAIC VIRUS.
PubMed=16644052; DOI=10.1016/j.virusres.2006.03.013;
Carr T., Wang Y., Huang Z., Yeakley J.M., Fan J.B., Whitham S.A.;
"Tobamovirus infection is independent of HSP101 mRNA induction and
protein expression.";
Virus Res. 121:33-41(2006).
[11]
FUNCTION, AND INDUCTION BY HEAT STRESS.
PubMed=17144892; DOI=10.1111/j.1365-313X.2006.02940.x;
Lee U., Rioflorido I., Hong S.W., Larkindale J., Waters E.R.,
Vierling E.;
"The Arabidopsis ClpB/Hsp100 family of proteins: chaperones for stress
and chloroplast development.";
Plant J. 49:115-127(2007).
[12]
FUNCTION, MUTAGENESIS OF HIS-33 AND THR-599, DISRUPTION PHENOTYPE, AND
INDUCTION BY HSA32.
STRAIN=cv. Columbia;
PubMed=23439916; DOI=10.1104/pp.112.212589;
Wu T.-Y., Juan Y.-T., Hsu Y.-H., Wu S.-H., Liao H.-T., Fung R.W.M.,
Charng Y.-Y.;
"Interplay between heat shock proteins HSP101 and HSA32 prolongs heat
acclimation memory posttranscriptionally in Arabidopsis.";
Plant Physiol. 161:2075-2084(2013).
-!- FUNCTION: Molecular chaperone that plays an important role in
thermotolerance. Together with HSA32, required for long-term
acquired thermotolerance (LAT) in plants and naturally high basal
thermotolerance observed in germinating seedlings.
{ECO:0000269|PubMed:10760238, ECO:0000269|PubMed:10760305,
ECO:0000269|PubMed:11489180, ECO:0000269|PubMed:15659638,
ECO:0000269|PubMed:17144892, ECO:0000269|PubMed:23439916,
ECO:0000269|PubMed:7866032}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus {ECO:0000305}.
-!- DEVELOPMENTAL STAGE: Starts to accumulate in maturing seeds 15
days after pollination and decreases rapidly during seed
germination. {ECO:0000269|PubMed:10760238,
ECO:0000269|PubMed:11489180}.
-!- INDUCTION: By heat stress and oilseed rape mosaic virus
(PubMed:10760238, PubMed:10760305, PubMed:11489180,
PubMed:16644052, PubMed:16995899, PubMed:17144892,
PubMed:7866032). Regulated by HSA32 that retards its decay in a
positive feedback loop (at protein level) during recovery after
heat treatment (PubMed:23439916). {ECO:0000269|PubMed:10760238,
ECO:0000269|PubMed:10760305, ECO:0000269|PubMed:11489180,
ECO:0000269|PubMed:16644052, ECO:0000269|PubMed:16995899,
ECO:0000269|PubMed:17144892, ECO:0000269|PubMed:23439916,
ECO:0000269|PubMed:7866032}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but germinating seeds have greatly reduced basal
thermotolerance and are unable to acquire thermotolerance
(PubMed:10760305, PubMed:11489180). Faster degradation of HSA32
(at protein level) (PubMed:23439916).
{ECO:0000269|PubMed:10760305, ECO:0000269|PubMed:11489180,
ECO:0000269|PubMed:23439916}.
-!- MISCELLANEOUS: Over-expression of HSP101 partially reverse the
sensitivity of 14 day-old seedling to heat stress.
-!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U13949; AAA67927.1; -; mRNA.
EMBL; AF218796; AAF26423.1; -; Genomic_DNA.
EMBL; AC020579; AAG52410.1; -; Genomic_DNA.
EMBL; CP002684; AEE35576.1; -; Genomic_DNA.
EMBL; AY062596; AAL32674.1; -; mRNA.
PIR; F96771; F96771.
RefSeq; NP_565083.1; NM_106091.4.
UniGene; At.48370; -.
UniGene; At.69978; -.
ProteinModelPortal; P42730; -.
SMR; P42730; -.
BioGrid; 28990; 2.
IntAct; P42730; 1.
STRING; 3702.AT1G74310.1; -.
PaxDb; P42730; -.
PRIDE; P42730; -.
EnsemblPlants; AT1G74310.1; AT1G74310.1; AT1G74310.
GeneID; 843771; -.
Gramene; AT1G74310.1; AT1G74310.1; AT1G74310.
KEGG; ath:AT1G74310; -.
Araport; AT1G74310; -.
TAIR; locus:2019667; AT1G74310.
eggNOG; KOG1051; Eukaryota.
eggNOG; COG0542; LUCA.
HOGENOM; HOG000218211; -.
InParanoid; P42730; -.
KO; K03695; -.
OMA; EIRVEMN; -.
OrthoDB; EOG093602DK; -.
PhylomeDB; P42730; -.
PRO; PR:P42730; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; P42730; baseline and differential.
Genevisible; P42730; AT.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045727; P:positive regulation of translation; IMP:TAIR.
GO; GO:0019538; P:protein metabolic process; IEA:InterPro.
GO; GO:0043335; P:protein unfolding; IMP:TAIR.
GO; GO:0009408; P:response to heat; IMP:TAIR.
GO; GO:0009644; P:response to high light intensity; IEP:TAIR.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
Gene3D; 1.10.1780.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR019489; Clp_ATPase_C.
InterPro; IPR004176; Clp_N.
InterPro; IPR001270; ClpA/B.
InterPro; IPR018368; ClpA/B_CS1.
InterPro; IPR028299; ClpA/B_CS2.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF00004; AAA; 1.
Pfam; PF07724; AAA_2; 1.
Pfam; PF02861; Clp_N; 2.
Pfam; PF10431; ClpB_D2-small; 1.
PRINTS; PR00300; CLPPROTEASEA.
SMART; SM00382; AAA; 2.
SMART; SM01086; ClpB_D2-small; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF81923; SSF81923; 1.
PROSITE; PS00870; CLPAB_1; 1.
PROSITE; PS00871; CLPAB_2; 1.
1: Evidence at protein level;
ATP-binding; Chaperone; Coiled coil; Complete proteome; Cytoplasm;
Nucleotide-binding; Nucleus; Reference proteome; Repeat;
Stress response.
CHAIN 1 911 Chaperone protein ClpB1.
/FTId=PRO_0000191220.
NP_BIND 207 214 ATP. {ECO:0000255}.
NP_BIND 606 613 ATP. {ECO:0000255}.
REGION 164 410 I.
REGION 532 723 II.
COILED 403 500 {ECO:0000255}.
MUTAGEN 33 33 H->Y: In dlt1-2; normal growth and
development under nonstress conditions.
Impaired chaperone activity and
thermotolerance function, but normal
positive regulation of HSA32 during
recovery after heat treatment.
{ECO:0000269|PubMed:23439916}.
MUTAGEN 499 499 A->T: In hot1-4; reduced basal
thermotolerance and unable to acquire
thermotolerance.
{ECO:0000269|PubMed:15659638}.
MUTAGEN 509 509 E->K: In hot1-6; reduced ability to
acquire thermotolerance.
{ECO:0000269|PubMed:15659638}.
MUTAGEN 599 599 T->I: In dlt1-1; normal growth and
development under nonstress conditions,
and normal chaperone activity and
thermotolerance function. Compromised
positive regulation of HSA32 during
recovery after heat treatment.
{ECO:0000269|PubMed:23439916}.
MUTAGEN 637 637 E->K: In hot1-1; greatly reduced basal
thermotolerance and unable to acquire
thermotolerance.
{ECO:0000269|PubMed:10760305,
ECO:0000269|PubMed:15659638}.
MUTAGEN 706 706 R->K: In hot1-5; unable to acquire
thermotolerance.
{ECO:0000269|PubMed:15659638}.
MUTAGEN 815 815 G->D: In hot1-7; reduced ability to
acquire thermotolerance.
{ECO:0000269|PubMed:15659638}.
CONFLICT 141 141 V -> F (in Ref. 5; AAL32674).
{ECO:0000305}.
CONFLICT 595 595 P -> A (in Ref. 1; AAA67927).
{ECO:0000305}.
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


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