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Chaperone protein ClpB3, chloroplastic (ATP-dependent Clp protease ATP-binding subunit ClpB homolog 3) (Casein lytic proteinase B3) (Protein ALBINO OR PALE GREEN 6)

 CLPB3_ARATH             Reviewed;         968 AA.
Q9LF37; Q8GRN9;
21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 117.
RecName: Full=Chaperone protein ClpB3, chloroplastic;
AltName: Full=ATP-dependent Clp protease ATP-binding subunit ClpB homolog 3;
AltName: Full=Casein lytic proteinase B3;
AltName: Full=Protein ALBINO OR PALE GREEN 6;
Flags: Precursor;
Name=CLPB3; Synonyms=APG6, CLPB-P; OrderedLocusNames=At5g15450;
ORFNames=T20K14.60;
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 [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 731-968 AND 796-968.
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).
[4]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY HEAT STRESS, AND
DISRUPTION PHENOTYPE.
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).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[6]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY HEAT STRESS, AND
DISRUPTION PHENOTYPE.
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).
-!- FUNCTION: Molecular chaperone essential for chloroplast
development and seedling viability. Mediates internal thylakoid
membrane formation and confers thermotolerance to chloroplasts
during heat stress. {ECO:0000269|PubMed:16995899,
ECO:0000269|PubMed:17144892}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast
{ECO:0000269|PubMed:16995899, ECO:0000269|PubMed:17144892}.
-!- INDUCTION: By heat stress. {ECO:0000269|PubMed:16995899,
ECO:0000269|PubMed:17144892}.
-!- DISRUPTION PHENOTYPE: Seedling lethal when grown on soil. On agar
plates supplied with sucrose, seedlings grow slowly with a
chlorotic phenotype. They display irregular and small chloroplasts
without starch grains in the stroma and with disorganized grana
stacks and undeveloped thylakoid membranes.
{ECO:0000269|PubMed:16995899, ECO:0000269|PubMed:17144892}.
-!- MISCELLANEOUS: Plants overexpressing CLPB3 show inhibition of
chloroplast development and a mild pale-green phenotype.
-!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAN17424.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AL391143; CAC01744.1; -; Genomic_DNA.
EMBL; CP002688; AED92162.1; -; Genomic_DNA.
EMBL; BT000447; AAN17424.1; ALT_INIT; mRNA.
EMBL; BT002569; AAO00929.1; -; mRNA.
PIR; T51523; T51523.
RefSeq; NP_568314.1; NM_121549.3.
UniGene; At.49023; -.
UniGene; At.66737; -.
ProteinModelPortal; Q9LF37; -.
SMR; Q9LF37; -.
BioGrid; 16674; 3.
IntAct; Q9LF37; 1.
STRING; 3702.AT5G15450.1; -.
PaxDb; Q9LF37; -.
PRIDE; Q9LF37; -.
EnsemblPlants; AT5G15450.1; AT5G15450.1; AT5G15450.
GeneID; 831398; -.
Gramene; AT5G15450.1; AT5G15450.1; AT5G15450.
KEGG; ath:AT5G15450; -.
Araport; AT5G15450; -.
TAIR; locus:2180922; AT5G15450.
eggNOG; KOG1051; Eukaryota.
eggNOG; COG0542; LUCA.
HOGENOM; HOG000218211; -.
InParanoid; Q9LF37; -.
KO; K03695; -.
OMA; HHKVRIK; -.
OrthoDB; EOG093601OG; -.
PhylomeDB; Q9LF37; -.
PRO; PR:Q9LF37; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; Q9LF37; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0009532; C:plastid stroma; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
GO; GO:0016485; P:protein processing; IEA:InterPro.
GO; GO:0009408; P:response to heat; IEP:TAIR.
Gene3D; 1.10.1780.10; -; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR017730; Chaperonin_ClpB.
InterPro; IPR019489; Clp_ATPase_C.
InterPro; IPR004176; Clp_N.
InterPro; IPR036628; Clp_N_dom_sf.
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.
TIGRFAMs; TIGR03346; chaperone_ClpB; 1.
PROSITE; PS00870; CLPAB_1; 1.
PROSITE; PS00871; CLPAB_2; 1.
1: Evidence at protein level;
ATP-binding; Chaperone; Chloroplast; Coiled coil; Complete proteome;
Nucleotide-binding; Plastid; Reference proteome; Repeat;
Stress response; Transit peptide.
TRANSIT 1 67 Chloroplast. {ECO:0000255}.
CHAIN 68 968 Chaperone protein ClpB3, chloroplastic.
/FTId=PRO_0000412573.
NP_BIND 282 289 ATP. {ECO:0000255}.
NP_BIND 685 692 ATP. {ECO:0000255}.
REGION 237 485 I. {ECO:0000250}.
REGION 611 802 II. {ECO:0000250}.
COILED 488 606 {ECO:0000255}.
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


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