CLPB4_ARATH
ID CLPB4_ARATH Reviewed; 964 AA.
AC Q8VYJ7;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Chaperone protein ClpB4, mitochondrial;
DE AltName: Full=ATP-dependent Clp protease ATP-binding subunit ClpB homolog 4;
DE AltName: Full=Casein lytic proteinase B4;
DE Flags: Precursor;
GN Name=CLPB4; Synonyms=CLPB-M, HSP98.7; OrderedLocusNames=At2g25140;
GN ORFNames=F13D4.100;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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 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 [5]
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 that does not seem to be involved in heat
CC stress response or tolerance. {ECO:0000269|PubMed:17144892}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17144892}.
CC -!- INDUCTION: By heat stress. {ECO:0000269|PubMed:16995899,
CC ECO:0000269|PubMed:17144892}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions. {ECO:0000269|PubMed:17144892}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002685; AEC07662.1; -; Genomic_DNA.
DR EMBL; AY070722; AAL50064.1; -; mRNA.
DR EMBL; BT002223; AAN72234.1; -; mRNA.
DR PIR; G84644; G84644.
DR RefSeq; NP_565586.1; NM_128071.3.
DR AlphaFoldDB; Q8VYJ7; -.
DR SMR; Q8VYJ7; -.
DR BioGRID; 2404; 6.
DR IntAct; Q8VYJ7; 1.
DR STRING; 3702.AT2G25140.1; -.
DR iPTMnet; Q8VYJ7; -.
DR SwissPalm; Q8VYJ7; -.
DR PaxDb; Q8VYJ7; -.
DR PRIDE; Q8VYJ7; -.
DR ProteomicsDB; 246654; -.
DR EnsemblPlants; AT2G25140.1; AT2G25140.1; AT2G25140.
DR GeneID; 817052; -.
DR Gramene; AT2G25140.1; AT2G25140.1; AT2G25140.
DR KEGG; ath:AT2G25140; -.
DR Araport; AT2G25140; -.
DR TAIR; locus:2040159; AT2G25140.
DR eggNOG; KOG1051; Eukaryota.
DR HOGENOM; CLU_005070_4_2_1; -.
DR InParanoid; Q8VYJ7; -.
DR OMA; KRYITDH; -.
DR OrthoDB; 611758at2759; -.
DR PhylomeDB; Q8VYJ7; -.
DR PRO; PR:Q8VYJ7; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8VYJ7; baseline and differential.
DR Genevisible; Q8VYJ7; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
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:0005739; C:mitochondrion; 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:0042026; P:protein refolding; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding; Chaperone; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Repeat; Transit peptide.
FT TRANSIT 1..39
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 40..964
FT /note="Chaperone protein ClpB4, mitochondrial"
FT /id="PRO_0000412574"
FT DOMAIN 83..227
FT /note="Clp R"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 88..153
FT /note="Repeat 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 164..227
FT /note="Repeat 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01251"
FT REGION 242..490
FT /note="I"
FT /evidence="ECO:0000250"
FT REGION 616..807
FT /note="II"
FT /evidence="ECO:0000250"
FT BINDING 287..294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 690..697
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 964 AA; 108662 MW; F40F7D8053E58E82 CRC64;
MALRRLSKSV SSAIKAQYTL SRPSPLLRSR SLSSSPHYTS IGRPTNSFIG KINNSSITHA
TTTHGQLFPL SSPRRFCTTT AQVNQNEFTE MAWEGLINAF DAARESKQQI VESEHLMKAL
LEQKDGMARK IFTKAGIDNS SVLQATDLFI SKQPTVSDAS GQRLGSSLSV ILENAKRHKK
DMLDSYVSVE HFLLAYYSDT RFGQEFFRDM KLDIQVLKDA IKDVRGDQRV TDRNPESKYQ
ALEKYGNDLT EMARRGKLDP VIGRDDEIRR CIQILCRRTK NNPVIIGEPG VGKTAIAEGL
AQRIVRGDVP EPLMNRKLIS LDMGSLLAGA KFRGDFEERL KAVMKEVSAS NGQTILFIDE
IHTVVGAGAM DGAMDASNLL KPMLGRGELR CIGATTLTEY RKYIEKDPAL ERRFQQVLCV
QPSVEDTISI LRGLRERYEL HHGVTISDSA LVSAAVLADR YITERFLPDK AIDLVDEAGA
KLKMEITSKP TELDGIDRAV IKLEMEKLSL KNDTDKASKE RLQKIENDLS TLKQKQKELN
VQWEKEKSLM TKIRSFKEEI DRVNLEIESA EREYDLNRAA ELKYGTLLSL QRQLEEAEKN
LTNFRQFGQS LLREVVTDLD IAEIVSKWTG IPLSNLQQSE REKLVMLEEV LHHRVIGQDM
AVKSVADAIR RSRAGLSDPN RPIASFMFMG PTGVGKTELA KALAGYLFNT ENAIVRVDMS
EYMEKHSVSR LVGAPPGYVG YEEGGQLTEV VRRRPYSVVL FDEIEKAHPD VFNILLQLLD
DGRITDSQGR TVSFKNCVVI MTSNIGSHHI LETLRNNEDS KEAVYEIMKR QVVELARQNF
RPEFMNRIDE YIVFQPLDSN EISKIVELQM RRVKNSLEQK KIKLQYTKEA VDLLAQLGFD
PNYGARPVKR VIQQMVENEI AVGILKGDFA EEDTVLVDVD HLASDNKLVI KKLESNASAE
EMAA
