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Heat shock 70 kDa protein 6, chloroplastic (Chloroplast heat shock protein 70-1) (cpHsc70-1) (Heat shock protein 70-6) (AtHsp70-6)

 HSP7F_ARATH             Reviewed;         718 AA.
Q9STW6;
22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-APR-2018, entry version 132.
RecName: Full=Heat shock 70 kDa protein 6, chloroplastic;
AltName: Full=Chloroplast heat shock protein 70-1;
Short=cpHsc70-1;
AltName: Full=Heat shock protein 70-6;
Short=AtHsp70-6;
Flags: Precursor;
Name=HSP70-6; Synonyms=CPHSC70-1; OrderedLocusNames=At4g24280;
ORFNames=T22A6.110;
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=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
Langham S.-A., McCullagh B., Bilham L., Robben J.,
van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
Chen E., Marra M.A., Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis
thaliana.";
Nature 402:769-777(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11599561; DOI=10.1379/1466-1268(2001)006<0201:GAOTHS>2.0.CO;2;
Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A.,
Delseny M.;
"Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana.";
Cell Stress Chaperones 6:201-208(2001).
[5]
DNAK GENE SUBFAMILY.
PubMed=11402207; DOI=10.1104/pp.126.2.789;
Sung D.Y., Vierling E., Guy C.L.;
"Comprehensive expression profile analysis of the Arabidopsis Hsp70
gene family.";
Plant Physiol. 126:789-800(2001).
[6]
SUBCELLULAR LOCATION.
PubMed=18997426; DOI=10.1271/bbb.80408;
Ratnayake R.M., Inoue H., Nonami H., Akita M.;
"Alternative processing of Arabidopsis Hsp70 precursors during protein
import into chloroplasts.";
Biosci. Biotechnol. Biochem. 72:2926-2935(2008).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18192441; DOI=10.1104/pp.107.114496;
Su P.H., Li H.M.;
"Arabidopsis stromal 70-kD heat shock proteins are essential for plant
development and important for thermotolerance of germinating seeds.";
Plant Physiol. 146:1231-1241(2008).
[8]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
PubMed=20506024; DOI=10.1007/s00425-010-1192-z;
Latijnhouwers M., Xu X.M., Moeller S.G.;
"Arabidopsis stromal 70-kDa heat shock proteins are essential for
chloroplast development.";
Planta 232:567-578(2010).
[9]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20484004; DOI=10.1105/tpc.109.071415;
Su P.H., Li H.M.;
"Stromal Hsp70 is important for protein translocation into pea and
Arabidopsis chloroplasts.";
Plant Cell 22:1516-1531(2010).
[10]
INTERACTION WITH GEMINIVIRUS MP.
PubMed=20193958; DOI=10.1016/j.virol.2010.02.011;
Krenz B., Windeisen V., Wege C., Jeske H., Kleinow T.;
"A plastid-targeted heat shock cognate 70kDa protein interacts with
the Abutilon mosaic virus movement protein.";
Virology 401:6-17(2010).
-!- FUNCTION: Acts redundantly with HSP70-7 in the thermotolerance of
germinating seeds. Plays an important role in the protein
precursor import into chloroplasts. {ECO:0000269|PubMed:18192441,
ECO:0000269|PubMed:20484004, ECO:0000269|PubMed:20506024}.
-!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
preexistent proteins against aggregation and mediate the folding
of newly translated polypeptides in the cytosol as well as within
organelles. These chaperones participate in all these processes
through their ability to recognize nonnative conformations of
other proteins. They bind extended peptide segments with a net
hydrophobic character exposed by polypeptides during translation
and membrane translocation, or following stress-induced damage (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with geminivirus movement protein (MP).
{ECO:0000269|PubMed:20193958}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
{ECO:0000269|PubMed:18997426, ECO:0000269|PubMed:20506024}.
-!- DISRUPTION PHENOTYPE: Variegated cotyledons, malformed leaves,
growth retardation and impaired root growth. Defective in protein
import into chloroplasts during early developmental stages.
{ECO:0000269|PubMed:18192441, ECO:0000269|PubMed:20484004,
ECO:0000269|PubMed:20506024}.
-!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33)
family. DnaK subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL078637; CAB45063.1; -; Genomic_DNA.
EMBL; AL161561; CAB79338.1; -; Genomic_DNA.
EMBL; CP002687; AEE84884.1; -; Genomic_DNA.
EMBL; AY072138; AAL59960.1; -; mRNA.
EMBL; BT001950; AAN71949.1; -; mRNA.
PIR; T09891; T09891.
RefSeq; NP_194159.1; NM_118561.3.
UniGene; At.25311; -.
UniGene; At.67055; -.
ProteinModelPortal; Q9STW6; -.
SMR; Q9STW6; -.
BioGrid; 13820; 8.
STRING; 3702.AT4G24280.1; -.
iPTMnet; Q9STW6; -.
PaxDb; Q9STW6; -.
PRIDE; Q9STW6; -.
EnsemblPlants; AT4G24280.1; AT4G24280.1; AT4G24280.
GeneID; 828531; -.
Gramene; AT4G24280.1; AT4G24280.1; AT4G24280.
KEGG; ath:AT4G24280; -.
Araport; AT4G24280; -.
TAIR; locus:2135897; AT4G24280.
eggNOG; KOG0102; Eukaryota.
eggNOG; COG0443; LUCA.
HOGENOM; HOG000228135; -.
InParanoid; Q9STW6; -.
KO; K03283; -.
OMA; GGTFMPR; -.
OrthoDB; EOG093604GM; -.
PhylomeDB; Q9STW6; -.
PRO; PR:Q9STW6; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q9STW6; baseline and differential.
Genevisible; Q9STW6; AT.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0009941; C:chloroplast envelope; IDA:TAIR.
GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0009579; C:thylakoid; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IDA:TAIR.
GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0045036; P:protein targeting to chloroplast; IMP:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009409; P:response to cold; IEP:TAIR.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
HAMAP; MF_00332; DnaK; 1.
InterPro; IPR012725; Chaperone_DnaK.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
PANTHER; PTHR19375; PTHR19375; 1.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
TIGRFAMs; TIGR02350; prok_dnaK; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
ATP-binding; Chaperone; Chloroplast; Complete proteome;
Host-virus interaction; Nucleotide-binding; Plastid;
Protein transport; Reference proteome; Stress response;
Transit peptide; Transport.
TRANSIT 1 92 Chloroplast. {ECO:0000255}.
CHAIN 93 718 Heat shock 70 kDa protein 6,
chloroplastic.
/FTId=PRO_0000415425.
SEQUENCE 718 AA; 76508 MW; 8723B345C601B8A1 CRC64;
MASSAAQIHV LGGIGFASSS SSKRNLNGKG GTFMPRSAFF GTRTGPFSTP TSAFLRMGTR
NGGGASRYAV GPVRVVNEKV VGIDLGTTNS AVAAMEGGKP TIVTNAEGQR TTPSVVAYTK
SGDRLVGQIA KRQAVVNPEN TFFSVKRFIG RKMNEVDEES KQVSYRVVRD ENNNVKLECP
AINKQFAAEE ISAQVLRKLV DDASRFLNDK VTKAVITVPA YFNDSQRTAT KDAGRIAGLE
VLRIINEPTA ASLAYGFDRK ANETILVFDL GGGTFDVSVL EVGDGVFEVL STSGDTHLGG
DDFDKRVVDW LAAEFKKDEG IDLLKDKQAL QRLTEAAEKA KIELSSLTQT NMSLPFITAT
ADGPKHIETT LTRAKFEELC SDLLDRVRTP VENSLRDAKL SFKDIDEVIL VGGSTRIPAV
QELVRKVTGK EPNVTVNPDE VVALGAAVQA GVLAGDVSDI VLLDVTPLSI GLETLGGVMT
KIIPRNTTLP TSKSEVFSTA ADGQTSVEIN VLQGEREFVR DNKSLGSFRL DGIPPAPRGV
PQIEVKFDID ANGILSVSAV DKGTGKKQDI TITGASTLPK DEVDQMVQEA ERFAKDDKEK
RDAIDTKNQA DSVVYQTEKQ LKELGEKIPG EVKEKVEAKL QELKDKIGSG STQEIKDAMA
ALNQEVMQIG QSLYNQPGAG GPGAGPSPGG EGASSGDSSS SKGGDGDDVI DADFTDSQ


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