CLPB3_ARATH
ID CLPB3_ARATH Reviewed; 968 AA.
AC Q9LF37; Q8GRN9;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Chaperone protein ClpB3, chloroplastic;
DE AltName: Full=ATP-dependent Clp protease ATP-binding subunit ClpB homolog 3;
DE AltName: Full=Casein lytic proteinase B3;
DE AltName: Full=Protein ALBINO OR PALE GREEN 6;
DE Flags: Precursor;
GN Name=CLPB3; Synonyms=APG6, CLPB-P; OrderedLocusNames=At5g15450;
GN ORFNames=T20K14.60;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 731-968 AND 796-968.
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY HEAT STRESS, AND DISRUPTION
RP PHENOTYPE.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=17272265; DOI=10.1074/mcp.m600408-mcp200;
RA Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
RT "Multidimensional protein identification technology (MudPIT) analysis of
RT ubiquitinated proteins in plants.";
RL Mol. Cell. Proteomics 6:601-610(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY HEAT STRESS, AND DISRUPTION
RP PHENOTYPE.
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).
CC -!- FUNCTION: Molecular chaperone essential for chloroplast development and
CC seedling viability. Mediates internal thylakoid membrane formation and
CC confers thermotolerance to chloroplasts during heat stress.
CC {ECO:0000269|PubMed:16995899, ECO:0000269|PubMed:17144892}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:16995899, ECO:0000269|PubMed:17144892}.
CC -!- INDUCTION: By heat stress. {ECO:0000269|PubMed:16995899,
CC ECO:0000269|PubMed:17144892}.
CC -!- DISRUPTION PHENOTYPE: Seedling lethal when grown on soil. On agar
CC plates supplied with sucrose, seedlings grow slowly with a chlorotic
CC phenotype. They display irregular and small chloroplasts without starch
CC grains in the stroma and with disorganized grana stacks and undeveloped
CC thylakoid membranes. {ECO:0000269|PubMed:16995899,
CC ECO:0000269|PubMed:17144892}.
CC -!- MISCELLANEOUS: Plants overexpressing CLPB3 show inhibition of
CC chloroplast development and a mild pale-green phenotype.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN17424.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL391143; CAC01744.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92162.1; -; Genomic_DNA.
DR EMBL; BT000447; AAN17424.1; ALT_INIT; mRNA.
DR EMBL; BT002569; AAO00929.1; -; mRNA.
DR PIR; T51523; T51523.
DR RefSeq; NP_568314.1; NM_121549.3.
DR AlphaFoldDB; Q9LF37; -.
DR SMR; Q9LF37; -.
DR BioGRID; 16674; 6.
DR IntAct; Q9LF37; 1.
DR STRING; 3702.AT5G15450.1; -.
DR PaxDb; Q9LF37; -.
DR PRIDE; Q9LF37; -.
DR ProteomicsDB; 246772; -.
DR EnsemblPlants; AT5G15450.1; AT5G15450.1; AT5G15450.
DR GeneID; 831398; -.
DR Gramene; AT5G15450.1; AT5G15450.1; AT5G15450.
DR KEGG; ath:AT5G15450; -.
DR Araport; AT5G15450; -.
DR TAIR; locus:2180922; AT5G15450.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_2_1; -.
DR InParanoid; Q9LF37; -.
DR OMA; SKMMQGE; -.
DR OrthoDB; 611758at2759; -.
DR PhylomeDB; Q9LF37; -.
DR PRO; PR:Q9LF37; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LF37; baseline and differential.
DR Genevisible; Q9LF37; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0009532; C:plastid stroma; IDA:TAIR.
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:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0042026; P:protein refolding; IEA:InterPro.
DR GO; GO:0009408; P:response to heat; IEP: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; 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 ATP-binding; Chaperone; Chloroplast; Coiled coil; Nucleotide-binding;
KW Plastid; Reference proteome; Repeat; Stress response; Transit peptide.
FT TRANSIT 1..67
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 68..968
FT /note="Chaperone protein ClpB3, chloroplastic"
FT /id="PRO_0000412573"
FT DOMAIN 78..222
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 82..147
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 159..222
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 237..485
FT /note="I"
FT /evidence="ECO:0000250"
FT REGION 611..802
FT /note="II"
FT /evidence="ECO:0000250"
FT COILED 488..606
FT /evidence="ECO:0000255"
FT BINDING 282..289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 685..692
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 968 AA; 108943 MW; 33FDAE6A140CAAED CRC64;
MATATTTATA AFSGVVSVGT ETRRIYSFSH LQPSAAFPAK PSSFKSLKLK QSARLTRRLD
HRPFVVRCEA SSSNGRLTQQ EFTEMAWQSI VSSPDVAKEN KQQIVETEHL MKALLEQKNG
LARRIFSKIG VDNTKVLEAT EKFIQRQPKV YGDAAGSMLG RDLEALFQRA RQFKKDLKDS
YVSVEHLVLA FADDKRFGKQ LFKDFQISER SLKSAIESIR GKQSVIDQDP EGKYEALEKY
GKDLTAMARE GKLDPVIGRD DEIRRCIQIL SRRTKNNPVL IGEPGVGKTA ISEGLAQRIV
QGDVPQALMN RKLISLDMGA LIAGAKYRGE FEDRLKAVLK EVTDSEGQII LFIDEIHTVV
GAGATNGAMD AGNLLKPMLG RGELRCIGAT TLDEYRKYIE KDPALERRFQ QVYVDQPTVE
DTISILRGLR ERYELHHGVR ISDSALVEAA ILSDRYISGR FLPDKAIDLV DEAAAKLKME
ITSKPTALDE LDRSVIKLEM ERLSLTNDTD KASRERLNRI ETELVLLKEK QAELTEQWEH
ERSVMSRLQS IKEEIDRVNL EIQQAEREYD LNRAAELKYG SLNSLQRQLN EAEKELNEYL
SSGKSMFREE VLGSDIAEIV SKWTGIPVSK LQQSERDKLL HLEEELHKRV VGQNPAVTAV
AEAIQRSRAG LSDPGRPIAS FMFMGPTGVG KTELAKALAS YMFNTEEALV RIDMSEYMEK
HAVSRLIGAP PGYVGYEEGG QLTETVRRRP YSVILFDEIE KAHGDVFNVF LQILDDGRVT
DSQGRTVSFT NTVIIMTSNV GSQFILNNTD DDANELSYET IKERVMNAAR SIFRPEFMNR
VDEYIVFKPL DREQINRIVR LQLARVQKRI ADRKMKINIT DAAVDLLGSL GYDPNYGARP
VKRVIQQNIE NELAKGILRG DFKEEDGILI DTEVTAFSNG QLPQQKLTFK KIESETADAE
QEEAAFSK
