MVP1_BYVU
ID MVP1_BYVU Reviewed; 598 AA.
AC P37092;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Movement protein Hsp70h;
DE AltName: Full=Heat shock protein 70 homolog;
DE Short=Hsp70h;
GN ORFNames=ORF3;
OS Beet yellows virus (isolate Ukraine) (BYV) (Sugar beet yellows virus).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Closteroviridae; Closterovirus.
OX NCBI_TaxID=478555;
OH NCBI_TaxID=161934; Beta vulgaris (Sugar beet).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1990061; DOI=10.1099/0022-1317-72-1-15;
RA Agranovsky A.A., Boyko V.P., Karasev A.V., Lunina N.A., Koonin E.V.,
RA Dolja V.V.;
RT "Nucleotide sequence of the 3'-terminal half of beet yellows closterovirus
RT RNA genome: unique arrangement of eight virus genes.";
RL J. Gen. Virol. 72:15-23(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8259666; DOI=10.1006/viro.1994.1034;
RA Agranovsky A.A., Koonin E.V., Boyko V.P., Maiss E., Froetschl R.,
RA Lunina N.A., Atabekov J.G.;
RT "Beet yellows closterovirus: complete genome structure and identification
RT of a leader papain-like thiol protease.";
RL Virology 198:311-324(1994).
RN [3]
RP DISCUSSION OF SEQUENCE.
RX PubMed=2005613; DOI=10.1016/0022-2836(91)90517-a;
RA Agranovsky A.A., Boyko V.P., Karasev A.V., Koonin E.V., Dolja V.V.;
RT "Putative 65 kDa protein of beet yellows closterovirus is a homologue of
RT HSP70 heat shock proteins.";
RL J. Mol. Biol. 217:603-610(1991).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=10405369; DOI=10.1006/viro.1999.9807;
RA Medina V., Peremyslov V.V., Hagiwara Y., Dolja V.V.;
RT "Subcellular localization of the HSP70-homolog encoded by beet yellows
RT closterovirus.";
RL Virology 260:173-181(1999).
RN [5]
RP FUNCTION.
RX PubMed=10936104; DOI=10.1006/viro.2000.0475;
RA Napuli A.J., Falk B.W., Dolja V.V.;
RT "Interaction between HSP70 homolog and filamentous virions of the Beet
RT yellows virus.";
RL Virology 274:232-239(2000).
RN [6]
RP FUNCTION.
RX PubMed=11742977; DOI=10.1093/emboj/20.24.6997;
RA Alzhanova D.V., Napuli A.J., Creamer R., Dolja V.V.;
RT "Cell-to-cell movement and assembly of a plant closterovirus: roles for the
RT capsid proteins and Hsp70 homolog.";
RL EMBO J. 20:6997-7007(2001).
RN [7]
RP SUBUNIT, AND INTERACTION WITH P20.
RX PubMed=12368343; DOI=10.1128/jvi.76.21.11003-11011.2002;
RA Prokhnevsky A.I., Peremyslov V.V., Napuli A.J., Dolja V.V.;
RT "Interaction between long-distance transport factor and Hsp70-related
RT movement protein of Beet yellows virus.";
RL J. Virol. 76:11003-11011(2002).
RN [8]
RP FUNCTION.
RX PubMed=17027895; DOI=10.1016/j.virol.2006.09.007;
RA Alzhanova D.V., Prokhnevsky A.I., Peremyslov V.V., Dolja V.V.;
RT "Virion tails of Beet yellows virus: coordinated assembly by three
RT structural proteins.";
RL Virology 359:220-226(2007).
CC -!- FUNCTION: Transports viral genome to neighboring plant cells directly
CC through plasmosdesmata, without any budding. The movement protein
CC allows efficient cell to cell propagation, by bypassing the host cell
CC wall barrier. Two movement proteins, p6, Hsp70h and three structural
CC proteins, CP, CPm, and P64 are essential for cell-cell movement. Also
CC plays a role in virion formation. Together with CPm and p64,
CC encapsidates the 5'-terminal portion of the viral genome.
CC {ECO:0000269|PubMed:10936104, ECO:0000269|PubMed:11742977,
CC ECO:0000269|PubMed:17027895}.
CC -!- SUBUNIT: Homomultimer. Interacts with p20. This interaction allows the
CC docking of the latter to the virion. {ECO:0000269|PubMed:12368343}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:10405369}. Host cell
CC junction, host plasmodesma {ECO:0000269|PubMed:10405369}. Note=Integral
CC virion tail component.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; X53462; CAA37551.1; -; Genomic_RNA.
DR EMBL; X73476; CAA51865.1; -; Genomic_RNA.
DR PIR; S28712; S28712.
DR RefSeq; NP_041872.1; NC_001598.1.
DR SMR; P37092; -.
DR GeneID; 1724791; -.
DR KEGG; vg:1724791; -.
DR Proteomes; UP000000359; Genome.
DR GO; GO:0044219; C:host cell plasmodesma; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0046740; P:transport of virus in host, cell to cell; IEA:UniProtKB-KW.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chaperone; Host cell junction; Nucleotide-binding;
KW Reference proteome; Transport; Viral movement protein; Virion.
FT CHAIN 1..598
FT /note="Movement protein Hsp70h"
FT /id="PRO_0000078670"
SQ SEQUENCE 598 AA; 65231 MW; 496BB88D937374DC CRC64;
MVVFGLDFGT TFSSVCAYVG EELYLFKQRD SAYIPTYVFL HSDTQEVAFG YDAEVLSNDL
SVRGGFYRDL KRWIGCDEEN YRDYLEKLKP HYKTELLKVA QSSKSTVKLD CYSGTVPQNA
TLPGLIATFV KALISTASEA FKCQCTGVIC SVPANYNCLQ RSFTESCVNL SGYPCVYMVN
EPSAAALSAC SRIKGATSPV LVYDFGGGTF DVSVISALNN TFVVRASGGD MNLGGRDIDK
AFVEHLYNKA QLPVNYKIDI SFLKESLSKK VSFLNFPVVS EQGVRVDVLV NVSELAEVAA
PFVERTIKIV KEVYEKYCSS MRLEPNVKAK LLMVGGSSYL PGLLSRLSSI PFVDECLVLP
DARAAVAGGC ALYSACLRND SPMLLVDCAA HNLSISSKYC ESIVCVPAGS PIPFTGVRTV
NMTGSNASAV YSAALFEGDF VKCRLNKRIF FGDVVLGNVG VTGSATRTVP LTLEINVSSV
GTISFSLVGP TGVKKLIGGN AAYDFSSYQL GERVVADLHK HNSDKVKLIH ALTYQPFQRK
KLTDGDKALF LKRLTADYRR EARKFSSYDD AVLNSSELLL GRIIPKILRG SRVEKLDV
