CLPB2_ARATH
ID CLPB2_ARATH Reviewed; 623 AA.
AC F4JVJ1; O23323;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Putative chaperone protein ClpB2, chloroplastic;
DE AltName: Full=ATP-dependent Clp protease ATP-binding subunit ClpB homolog 2;
DE AltName: Full=Casein lytic proteinase B2;
GN Name=CLPB2; Synonyms=CLPB4; OrderedLocusNames=At4g14670;
GN ORFNames=dl3375w, FCAALL.285;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
CC -!- CAUTION: Lacks the C-terminal domain, which is a conserved feature of
CC the family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB46061.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78509.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z97336; CAB46061.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161539; CAB78509.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83473.1; -; Genomic_DNA.
DR PIR; G85160; G85160.
DR RefSeq; NP_567437.1; NM_117549.1.
DR AlphaFoldDB; F4JVJ1; -.
DR SMR; F4JVJ1; -.
DR BioGRID; 12414; 1.
DR STRING; 3702.AT4G14670.1; -.
DR PaxDb; F4JVJ1; -.
DR PRIDE; F4JVJ1; -.
DR EnsemblPlants; AT4G14670.1; AT4G14670.1; AT4G14670.
DR GeneID; 827117; -.
DR Gramene; AT4G14670.1; AT4G14670.1; AT4G14670.
DR KEGG; ath:AT4G14670; -.
DR Araport; AT4G14670; -.
DR TAIR; locus:2130070; AT4G14670.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_2_0_1; -.
DR InParanoid; F4JVJ1; -.
DR OMA; HAMSLSH; -.
DR OrthoDB; 611758at2759; -.
DR PRO; PR:F4JVJ1; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JVJ1; baseline and differential.
DR Genevisible; F4JVJ1; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 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; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
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; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81923; SSF81923; 1.
DR PROSITE; PS51903; CLP_R; 1.
PE 3: Inferred from homology;
KW ATP-binding; Coiled coil; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..623
FT /note="Putative chaperone protein ClpB2, chloroplastic"
FT /id="PRO_0000412572"
FT DOMAIN 1..123
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 77..123
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 129..375
FT /note="I"
FT /evidence="ECO:0000250"
FT COILED 368..462
FT /evidence="ECO:0000255"
FT BINDING 172..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 571..578
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 623 AA; 68898 MW; 95EA1CF869752769 CRC64;
MNDLKFDPNV KLILASARSH AMSLSHGQVT PLHLGVTLIS DLTSVFYRAI TSAGDGDISA
QSVVNVINQS LYKLTKRNLG DTKVGVAVLV ISLLEDSQIS DVLKEAGVVP EKVKSEVEKL
RGEVILRALK TYGTDLVEQA GKLDPVIGRH REIRRVIEVL SRRTKNNPVL IGEPGVGKTA
VVEGLAQRIL KGDVPINLTG VKLISLEFGA MVAGTTLRGQ FEERLKSVLK AVEEAQGKVV
LFIDEIHMAL GACKASGSTD AAKLLKPMLA RGQLRFIGAT TLEEYRTHVE KDAAFERRFQ
QVFVAEPSVP DTISILRGLK EKYEGHHGVR IQDRALVLSA QLSERYITGR RLPDKAIDLV
DESCAHVKAQ LDIQPEEIDS LERKVMQLEI EIHALEKEKD DKASEARLSE VRKELDDLRD
KLEPLTIKYK KEKKIINETR RLKQNRDDLM IALQEAERQH DVPKAAVLKY GAIQEVESAI
AKLEKSAKDN VMLTETVGPE NIAEVVSRWT GIPVTRLDQN EKKRLISLAD KLHERVVGQD
EAVKAVAAAI LRSRVGLGRP QQPSGSFLFL GPTGVGKTEL AKALAEQLFD SENLLVRLDM
SEYNDKFSVN KLIGAPPGYV HWS
