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Avirulence protein AvrBs3 (TAL effector protein AvrBs3)

 AVRB3_XANEU             Reviewed;        1164 AA.
P14727;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
23-MAY-2018, entry version 62.
RecName: Full=Avirulence protein AvrBs3 {ECO:0000305};
AltName: Full=TAL effector protein AvrBs3 {ECO:0000305};
Name=avrBs3;
Xanthomonas euvesicatoria.
Plasmid pXV11.
Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
Xanthomonadaceae; Xanthomonas.
NCBI_TaxID=456327;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND REPEAT.
STRAIN=Isolate 71-21;
PubMed=2550761; DOI=10.1007/BF00330575;
Bonas U., Stall R.E., Staskawicz B.;
"Genetic and structural characterization of the avirulence gene avrBs3
from Xanthomonas campestris pv. vesicatoria.";
Mol. Gen. Genet. 218:127-136(1989).
[2]
SEQUENCE REVISION.
Bonas U.;
Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION, AND DOMAIN.
DOI=10.1038/356172a0;
Herbers K., Conrads-Strauch J., Bonas U.;
"Race-specificity of plant resistance to bacterial spot disease
determined by repetitive motifs in a bacterial virulence protein.";
Nature 356:172-174(1992).
[4]
FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF LYS-1021;
LYS-1067; 1067-ARG--PRO-1106; SER-1069; LYS-1104 AND PRO-1106.
PubMed=8980236; DOI=10.1016/S0092-8674(00)81825-5;
Van den Ackerveken G., Marois E., Bonas U.;
"Recognition of the bacterial avirulence protein AvrBs3 occurs inside
the host plant cell.";
Cell 87:1307-1316(1996).
[5]
SUBCELLULAR LOCATION.
STRAIN=82-8;
PubMed=10430949; DOI=10.1073/pnas.96.16.9368;
Rossier O., Wengelnik K., Hahn K., Bonas U.;
"The Xanthomonas Hrp type III system secretes proteins from plant and
mammalian bacterial pathogens.";
Proc. Natl. Acad. Sci. U.S.A. 96:9368-9373(1999).
[6]
ACTIVATION DOMAIN.
PubMed=9675896; DOI=10.1094/MPMI.1998.11.8.824;
Zhu W.G., Yang B., Chittoor J.M., Johnson L.B., White F.F.;
"AvrXa10 contains an acidic transcriptional activation domain in the
functionally conserved C terminus.";
Mol. Plant Microbe Interact. 11:824-832(1998).
[7]
INTERACTION WITH CAIMP ALPHA-1 AND CAIMP ALPHA-2, SUBUNIT, DOMAIN,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 1117-PRO--GLU-1153.
PubMed=11439138; DOI=10.1046/j.0960-7412.2001.01046.x;
Szurek B., Marois E., Bonas U., Van den Ackerveken G.;
"Eukaryotic features of the Xanthomonas type III effector AvrBs3:
protein domains involved in transcriptional activation and the
interaction with nuclear import receptors from pepper.";
Plant J. 26:523-534(2001).
[8]
SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 3-PRO--THR-27.
PubMed=12366827; DOI=10.1046/j.1365-2958.2002.03139.x;
Szurek B., Rossier O., Hause G., Bonas U.;
"Type III-dependent translocation of the Xanthomonas AvrBs3 protein
into the plant cell.";
Mol. Microbiol. 46:13-23(2002).
[9]
FUNCTION.
PubMed=12118879; DOI=10.1094/MPMI.2002.15.7.637;
Marois E., Van den Ackerveken G., Bonas U.;
"The xanthomonas type III effector protein AvrBs3 modulates plant gene
expression and induces cell hypertrophy in the susceptible host.";
Mol. Plant Microbe Interact. 15:637-646(2002).
[10]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=15807781; DOI=10.1111/j.1365-313X.2005.02370.x;
Guerlebeck D., Szurek B., Bonas U.;
"Dimerization of the bacterial effector protein AvrBs3 in the plant
cell cytoplasm prior to nuclear import.";
Plant J. 42:175-187(2005).
[11]
FUNCTION, AND DNA-BINDING.
PubMed=17962564; DOI=10.1126/science.1144958;
Romer P., Hahn S., Jordan T., Strauss T., Bonas U., Lahaye T.;
"Plant pathogen recognition mediated by promoter activation of the
pepper Bs3 resistance gene.";
Science 318:645-648(2007).
[12]
FUNCTION, AND DNA-BINDING.
PubMed=17962565; DOI=10.1126/science.1144956;
Kay S., Hahn S., Marois E., Hause G., Bonas U.;
"A bacterial effector acts as a plant transcription factor and induces
a cell size regulator.";
Science 318:648-651(2007).
[13]
FUNCTION IN DNA RECOGNITION, DOMAIN, BIOTECHNOLOGY, AND DNA-BINDING.
PubMed=19933107; DOI=10.1126/science.1178811;
Boch J., Scholze H., Schornack S., Landgraf A., Hahn S., Kay S.,
Lahaye T., Nickstadt A., Bonas U.;
"Breaking the code of DNA binding specificity of TAL-type III
effectors.";
Science 326:1509-1512(2009).
[14]
FUNCTION IN DNA RECOGNITION.
PubMed=19933106; DOI=10.1126/science.1178817;
Moscou M.J., Bogdanove A.J.;
"A simple cipher governs DNA recognition by TAL effectors.";
Science 326:1501-1501(2009).
[15]
BIOTECHNOLOGY.
PubMed=20660643; DOI=10.1534/genetics.110.120717;
Christian M., Cermak T., Doyle E.L., Schmidt C., Zhang F., Hummel A.,
Bogdanove A.J., Voytas D.F.;
"Targeting DNA double-strand breaks with TAL effector nucleases.";
Genetics 186:757-761(2010).
[16]
BIOTECHNOLOGY USES REVIEW.
PubMed=25057889; DOI=10.1042/BJ20140295;
Wright D.A., Li T., Yang B., Spalding M.H.;
"TALEN-mediated genome editing: prospects and perspectives.";
Biochem. J. 462:15-24(2014).
[17]
BIOTECHNOLOGY USES REVIEW.
PubMed=24602153; DOI=10.1111/tpj.12431;
de Lange O., Binder A., Lahaye T.;
"From dead leaf, to new life: TAL effectors as tools for synthetic
biology.";
Plant J. 78:753-771(2014).
[18]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 153-897 IN COMPLEX WITH DNA,
DOMAIN, AND DNA-BINDING.
PubMed=23999294; DOI=10.1107/S0907444913016429;
Stella S., Molina R., Yefimenko I., Prieto J., Silva G., Bertonati C.,
Juillerat A., Duchateau P., Montoya G.;
"Structure of the AvrBs3-DNA complex provides new insights into the
initial thymine-recognition mechanism.";
Acta Crystallogr. D 69:1707-1716(2013).
-!- FUNCTION: Avirulence protein. Acts as a transcription factor in
C.annuum plants. In susceptible plants lacking the Bs3 resistance
gene induces expression of a number of genes, including genes
homologous to a family of auxin-induced genes, alpha-expansin
genes, pectate lyase, anthocyanidin glucoside rhamnosyl
transferase and at least one transcription factor, UPA20. Their
expression leads to plant hypertrophy in mesophyll cells, probably
mainly mediated by UPA20 (PubMed:17962565). In resistant plants
induces the hypersensitive response (HR), by inducing
transcription of plant Bs3 which induces HR; a mutated AvrBs3
missing repeats 11-14 does not induce expression of Bs3 but does
induce Bs3-E, a Bs3 allele with a modified promoter
(PubMed:17962564). Binds DNA corresponding to the upa-box in
sequence-specific manner. {ECO:0000269|PubMed:12118879,
ECO:0000269|PubMed:17962564, ECO:0000269|PubMed:17962565,
ECO:0000269|PubMed:19933106, ECO:0000269|PubMed:19933107,
ECO:0000269|PubMed:8980236, ECO:0000269|Ref.3}.
-!- SUBUNIT: Forms a homodimer in the plant cell cytoplasm, prior to
nuclear import. Interacts with the plant cell importin alpha-1
(Caimp alpha-1) and importin alpha-2 (Caimp alpha-2) via the
nuclear localization signal NLS2, but not via NLS3.
{ECO:0000269|PubMed:11439138, ECO:0000269|PubMed:15807781}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10430949,
ECO:0000269|PubMed:11439138, ECO:0000269|PubMed:12366827,
ECO:0000269|PubMed:15807781, ECO:0000269|PubMed:8980236}. Host
nucleus {ECO:0000269|PubMed:12366827}. Note=Secreted via type III
secretion system (TTSS) (PubMed:10430949, PubMed:12366827).
Localizes to the plant cell nucleus in both susceptible (bs3) and
resistant (Bs3) plants (PubMed:12366827).
{ECO:0000269|PubMed:10430949, ECO:0000269|PubMed:12366827,
ECO:0000269|PubMed:8980236}.
-!- DOMAIN: The N-terminus is responsible for protein export from the
bacteria. {ECO:0000269|PubMed:12366827}.
-!- DOMAIN: The central DNA-binding region is composed of 17.5 tandem
core repeats with 1 base-specifying residue (BSR residue 13, also
called repeat variable diresidue, RVD, residues 12 and 13) which
recognizes 1 base in the target DNA; 10.5 or more repeats are
required for strong gene expression (tested using an artifical
TALE, PubMed:19933107). The BSR is the only residue which contacts
DNA in a sequence-specific manner (PubMed:23999294). The number
and order of core repeats determines its specificity for different
resistance alleles in plants. Deleting and/or swapping core
repeats alters the interplay between bacterial avirulence and
plant resistance genes. Replacement with repeat domains from other
proteins (AvrXa7 or AvrXa10 of X.oryzae pv. oryzae (AC Q56830))
does not elicit the HR in susceptible plants (PubMed:9675896).
{ECO:0000269|PubMed:19933107, ECO:0000269|PubMed:23999294,
ECO:0000269|PubMed:9675896, ECO:0000269|Ref.3,
ECO:0000303|PubMed:19933106, ECO:0000303|PubMed:24602153}.
-!- DOMAIN: An intact NLS2 or NLS3 is required for the plant HR
response, whereas NLS1 plays a minor role. Replacement of NLS1-
NLS3 or NLS2-NLS3 (residues 1021-1106 or 1067-1106) with the large
T-antigen NLS from the SV40 virus fully restores HR activity.
{ECO:0000269|PubMed:8980236}.
-!- DOMAIN: The activation domain is necessary for activity in planta.
{ECO:0000269|PubMed:11439138, ECO:0000303|PubMed:9675896}.
-!- BIOTECHNOLOGY: By varying the BSR in each core repeat, DNA-binding
domains can be generated that target specific DNA sequences and
thus act as transcription factors (PubMed:19933107). By combining
the central DNA-binding domain with the catalytic domain of the
restriction endonuclease FokI, TALE-nuclease (TALEN) enzymes able
to target specific dsDNA sequences can be created that enable
eukaryotic genome modification (PubMed:20660643). Other potential
uses as transcriptional repressors, for transposon targeting, DNA
methylation or histone tail modifictions are also possible.
{ECO:0000269|PubMed:19933107, ECO:0000269|PubMed:20660643,
ECO:0000303|PubMed:24602153, ECO:0000303|PubMed:25057889}.
-!- SIMILARITY: Belongs to the transcription activator-like effector
(TALE) family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X16130; CAA34257.1; -; Genomic_DNA.
PIR; JQ0316; JQ0316.
PDB; 2YPF; X-ray; 2.55 A; A=153-897.
PDBsum; 2YPF; -.
SMR; P14727; -.
PRIDE; P14727; -.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0034053; P:modulation by symbiont of host defense-related programmed cell death; IDA:UniProtKB.
GO; GO:0052026; P:modulation by symbiont of host transcription; IDA:UniProtKB.
GO; GO:0009405; P:pathogenesis; IMP:CACAO.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR005042; TAL_effector_rpt.
Pfam; PF03377; TAL_effector; 19.
1: Evidence at protein level;
3D-structure; DNA-binding; Host nucleus;
Hypersensitive response elicitation; Plasmid; Repeat; Secreted;
Transcription; Transcription regulation; Virulence.
CHAIN 1 1164 Avirulence protein AvrBs3.
/FTId=PRO_0000066138.
REPEAT 225 254 Cryptic repeat -1.
{ECO:0000303|PubMed:23999294}.
REPEAT 255 288 Cryptic repeat 0.
{ECO:0000303|PubMed:23999294}.
REPEAT 289 322 Core repeat 1.
{ECO:0000303|PubMed:2550761}.
REPEAT 323 356 Core repeat 2.
{ECO:0000303|PubMed:2550761}.
REPEAT 357 390 Core repeat 3.
{ECO:0000303|PubMed:2550761}.
REPEAT 391 424 Core repeat 4.
{ECO:0000303|PubMed:2550761}.
REPEAT 425 458 Core repeat 5.
{ECO:0000303|PubMed:2550761}.
REPEAT 459 492 Core repeat 6.
{ECO:0000303|PubMed:2550761}.
REPEAT 493 526 Core repeat 7.
{ECO:0000303|PubMed:2550761}.
REPEAT 527 560 Core repeat 8.
{ECO:0000303|PubMed:2550761}.
REPEAT 561 594 Core repeat 9.
{ECO:0000303|PubMed:2550761}.
REPEAT 595 628 Core repeat 10.
{ECO:0000303|PubMed:2550761}.
REPEAT 629 662 Core repeat 11.
{ECO:0000303|PubMed:2550761}.
REPEAT 663 696 Core repeat 12.
{ECO:0000303|PubMed:2550761}.
REPEAT 697 730 Core repeat 13.
{ECO:0000303|PubMed:2550761}.
REPEAT 731 764 Core repeat 14.
{ECO:0000303|PubMed:2550761}.
REPEAT 765 798 Core repeat 15.
{ECO:0000303|PubMed:2550761}.
REPEAT 799 832 Core repeat 16.
{ECO:0000303|PubMed:2550761}.
REPEAT 833 866 Core repeat 17.
{ECO:0000303|PubMed:2550761}.
REPEAT 867 886 Core repeat 17.5.
{ECO:0000303|PubMed:2550761}.
REGION 1135 1164 Acidic activation domain AAD.
{ECO:0000303|PubMed:11439138,
ECO:0000303|PubMed:9675896}.
MOTIF 1021 1024 Nuclear localization signal NLS1.
{ECO:0000269|PubMed:8980236}.
MOTIF 1067 1070 Nuclear localization signal NLS2.
{ECO:0000269|PubMed:8980236}.
MOTIF 1104 1107 Nuclear localization signal NLS3.
{ECO:0000269|PubMed:8980236}.
MUTAGEN 3 27 Missing: Loss of protein secretion, loss
of hypersensitive response (HR) activity
in planta. {ECO:0000269|PubMed:12366827}.
MUTAGEN 1021 1021 K->T: No loss of HR activity. No loss of
HR activity; when associated with T-1067
and A-1069, or with T-1104 and A-1106.
Reduced HR activity when associated with
T-1067; A-1069; T-1104 and A-1106.
{ECO:0000269|PubMed:8980236}.
MUTAGEN 1067 1106 KRSRSDRAVTGPSAQQSFEVRVPEQRDALHLPLSWRVKRP
->TA: Complete loss of HR activity (loss
of NLS2 and NLS3).
{ECO:0000269|PubMed:8980236}.
MUTAGEN 1067 1067 K->T: No loss of HR activity; when
associated with A-1069, or with T-1021
and A-1069. Reduced HR activity when
associated with A-1069; T-1104 and A-
1106, or with T-1021; A-1069; T-1104 and
A-1106. {ECO:0000269|PubMed:8980236}.
MUTAGEN 1069 1069 S->A: No loss of HR activity; when
associated with T-1067, or with T-1021
and T-1067. Reduced HR activity when
associated with T-1067; T-1104 and A-
1106, or with T-1021; T-1067; T-1104 and
A-1106. {ECO:0000269|PubMed:8980236}.
MUTAGEN 1104 1104 K->T: No loss of HR activity; when
associated with A-1106, or with T-1021
and A-1106. Reduced HR activity when
associated with T-1067; A-1069 and A-
1106, or with T-1021; T-1067; A-1069; and
A-1106. {ECO:0000269|PubMed:8980236}.
MUTAGEN 1106 1106 P->A: No loss of HR activity; when
associated with T-1104, or with T-1021
and T-1104. Reduced HR activity when
associated with T-1067; A-1069 and T-
1104, or with T-1021; T-1067; A-1069; and
T-1104. {ECO:0000269|PubMed:8980236}.
MUTAGEN 1117 1153 PGTPTAADLAASSTVMREQDEDPFAGAADDFPAFNEE->L:
Loss of HR activity (loss of AAD).
{ECO:0000269|PubMed:11439138}.
SEQUENCE 1164 AA; 122277 MW; FA0F81BEB9FB7515 CRC64;
MDPIRSRTPS PARELLPGPQ PDGVQPTADR GVSPPAGGPL DGLPARRTMS RTRLPSPPAP
SPAFSAGSFS DLLRQFDPSL FNTSLFDSLP PFGAHHTEAA TGEWDEVQSG LRAADAPPPT
MRVAVTAARP PRAKPAPRRR AAQPSDASPA AQVDLRTLGY SQQQQEKIKP KVRSTVAQHH
EALVGHGFTH AHIVALSQHP AALGTVAVKY QDMIAALPEA THEAIVGVGK QWSGARALEA
LLTVAGELRG PPLQLDTGQL LKIAKRGGVT AVEAVHAWRN ALTGAPLNLT PEQVVAIASH
DGGKQALETV QRLLPVLCQA HGLTPQQVVA IASNGGGKQA LETVQRLLPV LCQAHGLTPQ
QVVAIASNSG GKQALETVQR LLPVLCQAHG LTPEQVVAIA SNGGGKQALE TVQRLLPVLC
QAHGLTPEQV VAIASNIGGK QALETVQALL PVLCQAHGLT PEQVVAIASN IGGKQALETV
QALLPVLCQA HGLTPEQVVA IASNIGGKQA LETVQALLPV LCQAHGLTPE QVVAIASHDG
GKQALETVQR LLPVLCQAHG LTPEQVVAIA SHDGGKQALE TVQRLLPVLC QAHGLTPQQV
VAIASNGGGK QALETVQRLL PVLCQAHGLT PEQVVAIASN SGGKQALETV QALLPVLCQA
HGLTPEQVVA IASNSGGKQA LETVQRLLPV LCQAHGLTPE QVVAIASHDG GKQALETVQR
LLPVLCQAHG LTPEQVVAIA SHDGGKQALE TVQRLLPVLC QAHGLTPEQV VAIASHDGGK
QALETVQRLL PVLCQAHGLT PQQVVAIASN GGGRPALETV QRLLPVLCQA HGLTPEQVVA
IASHDGGKQA LETVQRLLPV LCQAHGLTPQ QVVAIASNGG GRPALESIVA QLSRPDPALA
ALTNDHLVAL ACLGGRPALD AVKKGLPHAP ALIKRTNRRI PERTSHRVAD HAQVVRVLGF
FQCHSHPAQA FDDAMTQFGM SRHGLLQLFR RVGVTELEAR SGTLPPASQR WDRILQASGM
KRAKPSPTST QTPDQASLHA FADSLERDLD APSPMHEGDQ TRASSRKRSR SDRAVTGPSA
QQSFEVRVPE QRDALHLPLS WRVKRPRTSI GGGLPDPGTP TAADLAASST VMREQDEDPF
AGAADDFPAF NEEELAWLME LLPQ


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