VIRE2_RHIRD
ID VIRE2_RHIRD Reviewed; 533 AA.
AC P0A3W8; P07544; Q9JN10;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Single-strand DNA-binding protein;
GN Name=virE2;
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OG Plasmid pTiA6.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3547330; DOI=10.1093/nar/15.2.825;
RA Winans S.C., Allenza P., Stachel S.E., McBride K.E., Nester E.W.;
RT "Characterization of the virE operon of the Agrobacterium Ti plasmid
RT pTiA6.";
RL Nucleic Acids Res. 15:825-837(1987).
RN [2]
RP SEQUENCE REVISION TO 358.
RA Winans S.C., Zhu J., Oger P.M., Schrammeijer B., Hooykaas P.J.,
RA Farrand S.K.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
RX PubMed=2832362; DOI=10.1128/jb.170.4.1430-1437.1988;
RA McBride K.E., Knauf V.C.;
RT "Genetic analysis of the virE operon of the Agrobacterium Ti plasmid
RT pTiA6.";
RL J. Bacteriol. 170:1430-1437(1988).
RN [4]
RP FUNCTION.
RX PubMed=17784072; DOI=10.1126/science.240.4851.501;
RA Citovsky V., de Vos G., Zambryski P.;
RT "Single-stranded DNA binding protein encoded by the virE locus of
RT Agrobacterium tumefaciens.";
RL Science 240:501-504(1988).
RN [5]
RP FUNCTION.
RX PubMed=8637884; DOI=10.1073/pnas.93.6.2392;
RA Zupan J.R., Citovsky V., Zambryski P.;
RT "Agrobacterium VirE2 protein mediates nuclear uptake of single-stranded DNA
RT in plant cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:2392-2397(1996).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=1615325; DOI=10.1126/science.1615325;
RA Citovsky V., Zupan J., Warnick D., Zambryski P.;
RT "Nuclear localization of Agrobacterium VirE2 protein in plant cells.";
RL Science 256:1802-1805(1992).
RN [7]
RP FUNCTION, INTERACTION WITH ARABIDOPSIS VIP1, AND SUBCELLULAR LOCATION.
RX PubMed=11432846; DOI=10.1093/emboj/20.13.3596;
RA Tzfira T., Vaidya M., Citovsky V.;
RT "VIP1, an Arabidopsis protein that interacts with Agrobacterium VirE2, is
RT involved in VirE2 nuclear import and Agrobacterium infectivity.";
RL EMBO J. 20:3596-3607(2001).
RN [8]
RP PROTEASOMAL DEGRADATION MEDIATED BY VIRF.
RX PubMed=15343337; DOI=10.1038/nature02857;
RA Tzfira T., Vaidya M., Citovsky V.;
RT "Involvement of targeted proteolysis in plant genetic transformation by
RT Agrobacterium.";
RL Nature 431:87-92(2004).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=A208, and EHA105;
RX PubMed=15824315; DOI=10.1073/pnas.0404118102;
RA Li J., Krichevsky A., Vaidya M., Tzfira T., Citovsky V.;
RT "Uncoupling of the functions of the Arabidopsis VIP1 protein in transient
RT and stable plant genetic transformation by Agrobacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5733-5738(2005).
RN [10]
RP INTERACTION WITH ARABIDOPSIS AND NICOTIANA VIP2.
RC STRAIN=A348;
RX PubMed=17496122; DOI=10.1105/tpc.106.042903;
RA Anand A., Krichevsky A., Schornack S., Lahaye T., Tzfira T., Tang Y.,
RA Citovsky V., Mysore K.S.;
RT "Arabidopsis VIRE2 INTERACTING PROTEIN2 is required for Agrobacterium T-DNA
RT integration in plants.";
RL Plant Cell 19:1695-1708(2007).
RN [11]
RP PROTEASOMAL DEGRADATION MEDIATED BY VBF, AND INTERACTION WITH ARABIDOPSIS
RP VIP1 AND VBF.
RX PubMed=20227663; DOI=10.1016/j.chom.2010.02.009;
RA Zaltsman A., Krichevsky A., Loyter A., Citovsky V.;
RT "Agrobacterium induces expression of a host F-box protein required for
RT tumorigenicity.";
RL Cell Host Microbe 7:197-209(2010).
CC -!- FUNCTION: Involved in DNA transformation; mediates the nuclear uptake
CC of single-stranded DNA copies of the transferred DNA (T-DNA) element.
CC Binds single-stranded but not double-stranded DNA regardless of
CC nucleotide sequence composition. {ECO:0000269|PubMed:11432846,
CC ECO:0000269|PubMed:15824315, ECO:0000269|PubMed:17784072,
CC ECO:0000269|PubMed:8637884}.
CC -!- SUBUNIT: Forms heterodimers with the chaperone protein virE1 that
CC prevent virE2 anarchic homopolymerization (By similarity). Interacts
CC with A.thaliana VIP1 that mediates its translocation to the host
CC nucleus, and with host (e.g. A.thaliana and N.benthamiana) VIP2 that
CC promotes T-DNA integration into the host genome. Forms a complex made
CC of VirE2, host VIP1 and VIP2, and single-stranded DNA (ssDNA). Forms a
CC complex made of virE2 and host (e.g. A.thaliana) proteins VIP1 and VBF.
CC {ECO:0000250, ECO:0000269|PubMed:11432846, ECO:0000269|PubMed:17496122,
CC ECO:0000269|PubMed:20227663}.
CC -!- SUBCELLULAR LOCATION: Secreted. Host nucleus. Note=In infected cells,
CC it is found in the nucleus.
CC -!- INDUCTION: Targeted to degradation by the host proteasome by VBF and
CC Agrobacterium virF in SCF(VBF) and SCF(COI1) E3 ubiquitin ligase
CC complexes after mediating T-DNA translocation to the nucleus.
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DR EMBL; AF242881; AAF77177.1; -; Genomic_DNA.
DR EMBL; M20143; AAA27400.1; -; Genomic_DNA.
DR PIR; B26446; B26446.
DR RefSeq; NP_059819.1; NC_002377.1.
DR RefSeq; WP_010892507.1; NZ_QSNU01000012.1.
DR AlphaFoldDB; P0A3W8; -.
DR SMR; P0A3W8; -.
DR TCDB; 1.C.55.1.1; the agrobacterial vire2 target host cell membrane anion channel (vire2) family.
DR OrthoDB; 103867at2; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0009294; P:DNA-mediated transformation; IDA:UniProtKB.
DR InterPro; IPR009868; VirE2.
DR Pfam; PF07229; VirE2; 1.
PE 1: Evidence at protein level;
KW Crown gall tumor; DNA-binding; Host nucleus; Plasmid; Secreted; Virulence.
FT CHAIN 1..533
FT /note="Single-strand DNA-binding protein"
FT /id="PRO_0000065868"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 60587 MW; D789196DD7218E1F CRC64;
MDLSGNEKSR PWKKANVSSS TISDIQMTNG ENLESGSPTR TEVLSPRLDD GSVDSSSSLY
SGSEHGNQAE IQKELSALFS NMSLPGNDRR PDEYILVRQT GQDAFTGIAK GNLDHMPTKA
EFNACCRLYR DGAGNYYPPP LAFDKISVPA QLEETWGMME AKERNKLRFQ YKLDVWNHAH
ADMGITGTEI FYQTDKNIKL DRNYKLRPED RYVQTERYGR REIQKRYQHE LQAGSLLPDI
MIKTPKNDIH FVYRFAGDNY ANKQFSEFEH TVKRRYGGET EIKLKSKSGI MHDSKYLESW
ERGSADIRFA EFVGENRAHN RQFPTATVNM GQQPDGQGGL TRDRHVSVEF LMQSAPNSPW
AQALKKGELW DRVQLLARDG NRYLSPHRLE YSDPEHFTEL MNRVGLPASM GRQSHAASIK
FEKFDAQAAV IVINGPELRD IHDLSPENLQ NVSTKDVIVA DRNENGQRTG TYTSVAEYER
LQLRLPADAA GVLGEAADKY SRDFVRPEPA SRPISDSRRI YESRPRSQSV NSF
