AVRB3_XANEU
ID AVRB3_XANEU Reviewed; 1164 AA.
AC P14727;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Avirulence protein AvrBs3 {ECO:0000305};
DE AltName: Full=TAL effector protein AvrBs3 {ECO:0000305};
GN Name=avrBs3;
OS Xanthomonas euvesicatoria.
OG Plasmid pXV11.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=456327;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND REPEAT.
RC STRAIN=Isolate 71-21;
RX PubMed=2550761; DOI=10.1007/bf00330575;
RA Bonas U., Stall R.E., Staskawicz B.;
RT "Genetic and structural characterization of the avirulence gene avrBs3 from
RT Xanthomonas campestris pv. vesicatoria.";
RL Mol. Gen. Genet. 218:127-136(1989).
RN [2]
RP SEQUENCE REVISION.
RA Bonas U.;
RL Submitted (JUL-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND DOMAIN.
RX DOI=10.1038/356172a0;
RA Herbers K., Conrads-Strauch J., Bonas U.;
RT "Race-specificity of plant resistance to bacterial spot disease determined
RT by repetitive motifs in a bacterial virulence protein.";
RL Nature 356:172-174(1992).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF LYS-1021;
RP LYS-1067; 1067-ARG--PRO-1106; SER-1069; LYS-1104 AND PRO-1106.
RX PubMed=8980236; DOI=10.1016/s0092-8674(00)81825-5;
RA Van den Ackerveken G., Marois E., Bonas U.;
RT "Recognition of the bacterial avirulence protein AvrBs3 occurs inside the
RT host plant cell.";
RL Cell 87:1307-1316(1996).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=82-8;
RX PubMed=10430949; DOI=10.1073/pnas.96.16.9368;
RA Rossier O., Wengelnik K., Hahn K., Bonas U.;
RT "The Xanthomonas Hrp type III system secretes proteins from plant and
RT mammalian bacterial pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:9368-9373(1999).
RN [6]
RP ACTIVATION DOMAIN.
RX PubMed=9675896; DOI=10.1094/mpmi.1998.11.8.824;
RA Zhu W.G., Yang B., Chittoor J.M., Johnson L.B., White F.F.;
RT "AvrXa10 contains an acidic transcriptional activation domain in the
RT functionally conserved C terminus.";
RL Mol. Plant Microbe Interact. 11:824-832(1998).
RN [7]
RP INTERACTION WITH CAIMP ALPHA-1 AND CAIMP ALPHA-2, SUBUNIT, DOMAIN,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 1117-PRO--GLU-1153.
RX PubMed=11439138; DOI=10.1046/j.0960-7412.2001.01046.x;
RA Szurek B., Marois E., Bonas U., Van den Ackerveken G.;
RT "Eukaryotic features of the Xanthomonas type III effector AvrBs3: protein
RT domains involved in transcriptional activation and the interaction with
RT nuclear import receptors from pepper.";
RL Plant J. 26:523-534(2001).
RN [8]
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 3-PRO--THR-27.
RX PubMed=12366827; DOI=10.1046/j.1365-2958.2002.03139.x;
RA Szurek B., Rossier O., Hause G., Bonas U.;
RT "Type III-dependent translocation of the Xanthomonas AvrBs3 protein into
RT the plant cell.";
RL Mol. Microbiol. 46:13-23(2002).
RN [9]
RP FUNCTION.
RX PubMed=12118879; DOI=10.1094/mpmi.2002.15.7.637;
RA Marois E., Van den Ackerveken G., Bonas U.;
RT "The xanthomonas type III effector protein AvrBs3 modulates plant gene
RT expression and induces cell hypertrophy in the susceptible host.";
RL Mol. Plant Microbe Interact. 15:637-646(2002).
RN [10]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15807781; DOI=10.1111/j.1365-313x.2005.02370.x;
RA Guerlebeck D., Szurek B., Bonas U.;
RT "Dimerization of the bacterial effector protein AvrBs3 in the plant cell
RT cytoplasm prior to nuclear import.";
RL Plant J. 42:175-187(2005).
RN [11]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=17962564; DOI=10.1126/science.1144958;
RA Romer P., Hahn S., Jordan T., Strauss T., Bonas U., Lahaye T.;
RT "Plant pathogen recognition mediated by promoter activation of the pepper
RT Bs3 resistance gene.";
RL Science 318:645-648(2007).
RN [12]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=17962565; DOI=10.1126/science.1144956;
RA Kay S., Hahn S., Marois E., Hause G., Bonas U.;
RT "A bacterial effector acts as a plant transcription factor and induces a
RT cell size regulator.";
RL Science 318:648-651(2007).
RN [13]
RP FUNCTION IN DNA RECOGNITION, DOMAIN, BIOTECHNOLOGY, AND DNA-BINDING.
RX PubMed=19933107; DOI=10.1126/science.1178811;
RA Boch J., Scholze H., Schornack S., Landgraf A., Hahn S., Kay S., Lahaye T.,
RA Nickstadt A., Bonas U.;
RT "Breaking the code of DNA binding specificity of TAL-type III effectors.";
RL Science 326:1509-1512(2009).
RN [14]
RP FUNCTION IN DNA RECOGNITION.
RX PubMed=19933106; DOI=10.1126/science.1178817;
RA Moscou M.J., Bogdanove A.J.;
RT "A simple cipher governs DNA recognition by TAL effectors.";
RL Science 326:1501-1501(2009).
RN [15]
RP BIOTECHNOLOGY.
RX PubMed=20660643; DOI=10.1534/genetics.110.120717;
RA Christian M., Cermak T., Doyle E.L., Schmidt C., Zhang F., Hummel A.,
RA Bogdanove A.J., Voytas D.F.;
RT "Targeting DNA double-strand breaks with TAL effector nucleases.";
RL Genetics 186:757-761(2010).
RN [16]
RP BIOTECHNOLOGY USES REVIEW.
RX PubMed=25057889; DOI=10.1042/bj20140295;
RA Wright D.A., Li T., Yang B., Spalding M.H.;
RT "TALEN-mediated genome editing: prospects and perspectives.";
RL Biochem. J. 462:15-24(2014).
RN [17]
RP BIOTECHNOLOGY USES REVIEW.
RX PubMed=24602153; DOI=10.1111/tpj.12431;
RA de Lange O., Binder A., Lahaye T.;
RT "From dead leaf, to new life: TAL effectors as tools for synthetic
RT biology.";
RL Plant J. 78:753-771(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 153-897 IN COMPLEX WITH DNA,
RP DOMAIN, AND DNA-BINDING.
RX PubMed=23999294; DOI=10.1107/s0907444913016429;
RA Stella S., Molina R., Yefimenko I., Prieto J., Silva G., Bertonati C.,
RA Juillerat A., Duchateau P., Montoya G.;
RT "Structure of the AvrBs3-DNA complex provides new insights into the initial
RT thymine-recognition mechanism.";
RL Acta Crystallogr. D 69:1707-1716(2013).
CC -!- FUNCTION: Avirulence protein. Acts as a transcription factor in
CC C.annuum plants. In susceptible plants lacking the Bs3 resistance gene
CC induces expression of a number of genes, including genes homologous to
CC a family of auxin-induced genes, alpha-expansin genes, pectate lyase,
CC anthocyanidin glucoside rhamnosyl transferase and at least one
CC transcription factor, UPA20. Their expression leads to plant
CC hypertrophy in mesophyll cells, probably mainly mediated by UPA20
CC (PubMed:17962565). In resistant plants induces the hypersensitive
CC response (HR), by inducing transcription of plant Bs3 which induces HR;
CC a mutated AvrBs3 missing repeats 11-14 does not induce expression of
CC Bs3 but does induce Bs3-E, a Bs3 allele with a modified promoter
CC (PubMed:17962564). Binds DNA corresponding to the upa-box in sequence-
CC specific manner. {ECO:0000269|PubMed:12118879,
CC ECO:0000269|PubMed:17962564, ECO:0000269|PubMed:17962565,
CC ECO:0000269|PubMed:19933106, ECO:0000269|PubMed:19933107,
CC ECO:0000269|PubMed:8980236, ECO:0000269|Ref.3}.
CC -!- SUBUNIT: Forms a homodimer in the plant cell cytoplasm, prior to
CC nuclear import. Interacts with the plant cell importin alpha-1 (Caimp
CC alpha-1) and importin alpha-2 (Caimp alpha-2) via the nuclear
CC localization signal NLS2, but not via NLS3.
CC {ECO:0000269|PubMed:11439138, ECO:0000269|PubMed:15807781}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10430949,
CC ECO:0000269|PubMed:11439138, ECO:0000269|PubMed:12366827,
CC ECO:0000269|PubMed:15807781, ECO:0000269|PubMed:8980236}. Host nucleus
CC {ECO:0000269|PubMed:12366827}. Note=Secreted via type III secretion
CC system (TTSS) (PubMed:10430949, PubMed:12366827). Localizes to the
CC plant cell nucleus in both susceptible (bs3) and resistant (Bs3) plants
CC (PubMed:12366827). {ECO:0000269|PubMed:10430949,
CC ECO:0000269|PubMed:12366827, ECO:0000269|PubMed:8980236}.
CC -!- DOMAIN: The N-terminus is responsible for protein export from the
CC bacteria. {ECO:0000269|PubMed:12366827}.
CC -!- DOMAIN: The central DNA-binding region is composed of 17.5 tandem core
CC repeats with 1 base-specifying residue (BSR residue 13, also called
CC repeat variable diresidue, RVD, residues 12 and 13) which recognizes 1
CC base in the target DNA; 10.5 or more repeats are required for strong
CC gene expression (tested using an artificial TALE, PubMed:19933107). The
CC BSR is the only residue which contacts DNA in a sequence-specific
CC manner (PubMed:23999294). The number and order of core repeats
CC determines its specificity for different resistance alleles in plants.
CC Deleting and/or swapping core repeats alters the interplay between
CC bacterial avirulence and plant resistance genes. Replacement with
CC repeat domains from other proteins (AvrXa7 or AvrXa10 of X.oryzae pv.
CC oryzae (AC Q56830)) does not elicit the HR in susceptible plants
CC (PubMed:9675896). {ECO:0000269|PubMed:19933107,
CC ECO:0000269|PubMed:23999294, ECO:0000269|PubMed:9675896,
CC ECO:0000269|Ref.3, ECO:0000303|PubMed:19933106,
CC ECO:0000303|PubMed:24602153}.
CC -!- DOMAIN: An intact NLS2 or NLS3 is required for the plant HR response,
CC whereas NLS1 plays a minor role. Replacement of NLS1-NLS3 or NLS2-NLS3
CC (residues 1021-1106 or 1067-1106) with the large T-antigen NLS from the
CC SV40 virus fully restores HR activity. {ECO:0000269|PubMed:8980236}.
CC -!- DOMAIN: The activation domain is necessary for activity in planta.
CC {ECO:0000269|PubMed:11439138, ECO:0000303|PubMed:9675896}.
CC -!- BIOTECHNOLOGY: By varying the BSR in each core repeat, DNA-binding
CC domains can be generated that target specific DNA sequences and thus
CC act as transcription factors (PubMed:19933107). By combining the
CC central DNA-binding domain with the catalytic domain of the restriction
CC endonuclease FokI, TALE-nuclease (TALEN) enzymes able to target
CC specific dsDNA sequences can be created that enable eukaryotic genome
CC modification (PubMed:20660643). Other potential uses as transcriptional
CC repressors, for transposon targeting, DNA methylation or histone tail
CC modifictions are also possible. {ECO:0000269|PubMed:19933107,
CC ECO:0000269|PubMed:20660643, ECO:0000303|PubMed:24602153,
CC ECO:0000303|PubMed:25057889}.
CC -!- SIMILARITY: Belongs to the transcription activator-like effector (TALE)
CC family. {ECO:0000305}.
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DR EMBL; X16130; CAA34257.1; -; Genomic_DNA.
DR PIR; JQ0316; JQ0316.
DR PDB; 2YPF; X-ray; 2.55 A; A=153-897.
DR PDBsum; 2YPF; -.
DR AlphaFoldDB; P14727; -.
DR SMR; P14727; -.
DR PHI-base; PHI:7758; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0034053; P:modulation by symbiont of host defense-related programmed cell death; IDA:UniProtKB.
DR GO; GO:0052026; P:modulation by symbiont of host transcription; IDA:UniProtKB.
DR InterPro; IPR005042; TAL_effector_rpt.
DR Pfam; PF03377; TAL_effector; 19.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Host nucleus;
KW Hypersensitive response elicitation; Plasmid; Repeat; Secreted;
KW Transcription; Transcription regulation; Virulence.
FT CHAIN 1..1164
FT /note="Avirulence protein AvrBs3"
FT /id="PRO_0000066138"
FT REPEAT 225..254
FT /note="Cryptic repeat -1"
FT /evidence="ECO:0000303|PubMed:23999294"
FT REPEAT 255..288
FT /note="Cryptic repeat 0"
FT /evidence="ECO:0000303|PubMed:23999294"
FT REPEAT 289..322
FT /note="Core repeat 1"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 323..356
FT /note="Core repeat 2"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 357..390
FT /note="Core repeat 3"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 391..424
FT /note="Core repeat 4"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 425..458
FT /note="Core repeat 5"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 459..492
FT /note="Core repeat 6"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 493..526
FT /note="Core repeat 7"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 527..560
FT /note="Core repeat 8"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 561..594
FT /note="Core repeat 9"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 595..628
FT /note="Core repeat 10"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 629..662
FT /note="Core repeat 11"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 663..696
FT /note="Core repeat 12"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 697..730
FT /note="Core repeat 13"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 731..764
FT /note="Core repeat 14"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 765..798
FT /note="Core repeat 15"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 799..832
FT /note="Core repeat 16"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 833..866
FT /note="Core repeat 17"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REPEAT 867..886
FT /note="Core repeat 17.5"
FT /evidence="ECO:0000303|PubMed:2550761"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1135..1164
FT /note="Acidic activation domain AAD"
FT /evidence="ECO:0000303|PubMed:11439138,
FT ECO:0000303|PubMed:9675896"
FT MOTIF 1021..1024
FT /note="Nuclear localization signal NLS1"
FT /evidence="ECO:0000269|PubMed:8980236"
FT MOTIF 1067..1070
FT /note="Nuclear localization signal NLS2"
FT /evidence="ECO:0000269|PubMed:8980236"
FT MOTIF 1104..1107
FT /note="Nuclear localization signal NLS3"
FT /evidence="ECO:0000269|PubMed:8980236"
FT COMPBIAS 1048..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 3..27
FT /note="Missing: Loss of protein secretion, loss of
FT hypersensitive response (HR) activity in planta."
FT /evidence="ECO:0000269|PubMed:12366827"
FT MUTAGEN 1021
FT /note="K->T: No loss of HR activity. No loss of HR
FT activity; when associated with T-1067 and A-1069, or with
FT T-1104 and A-1106. Reduced HR activity when associated with
FT T-1067; A-1069; T-1104 and A-1106."
FT /evidence="ECO:0000269|PubMed:8980236"
FT MUTAGEN 1067..1106
FT /note="KRSRSDRAVTGPSAQQSFEVRVPEQRDALHLPLSWRVKRP->TA:
FT Complete loss of HR activity (loss of NLS2 and NLS3)."
FT /evidence="ECO:0000269|PubMed:8980236"
FT MUTAGEN 1067
FT /note="K->T: No loss of HR activity; when associated with
FT A-1069, or with T-1021 and A-1069. Reduced HR activity when
FT associated with A-1069; T-1104 and A-1106, or with T-1021;
FT A-1069; T-1104 and A-1106."
FT /evidence="ECO:0000269|PubMed:8980236"
FT MUTAGEN 1069
FT /note="S->A: No loss of HR activity; when associated with
FT T-1067, or with T-1021 and T-1067. Reduced HR activity when
FT associated with T-1067; T-1104 and A-1106, or with T-1021;
FT T-1067; T-1104 and A-1106."
FT /evidence="ECO:0000269|PubMed:8980236"
FT MUTAGEN 1104
FT /note="K->T: No loss of HR activity; when associated with
FT A-1106, or with T-1021 and A-1106. Reduced HR activity when
FT associated with T-1067; A-1069 and A-1106, or with T-1021;
FT T-1067; A-1069; and A-1106."
FT /evidence="ECO:0000269|PubMed:8980236"
FT MUTAGEN 1106
FT /note="P->A: No loss of HR activity; when associated with
FT T-1104, or with T-1021 and T-1104. Reduced HR activity when
FT associated with T-1067; A-1069 and T-1104, or with T-1021;
FT T-1067; A-1069; and T-1104."
FT /evidence="ECO:0000269|PubMed:8980236"
FT MUTAGEN 1117..1153
FT /note="PGTPTAADLAASSTVMREQDEDPFAGAADDFPAFNEE->L: Loss of HR
FT activity (loss of AAD)."
FT /evidence="ECO:0000269|PubMed:11439138"
SQ 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
