BRG11_RALSO
ID BRG11_RALSO Reviewed; 1245 AA.
AC Q8XYE3;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=TAL effector protein Brg11 {ECO:0000305};
GN Name=brg11 {ECO:0000303|PubMed:15225308};
GN Synonyms=RTL2 {ECO:0000303|PubMed:23300258}; OrderedLocusNames=RSc1815;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(2002).
RN [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=GMI1000;
RX PubMed=15225308; DOI=10.1111/j.1365-2958.2004.04118.x;
RA Cunnac S., Occhialini A., Barberis P., Boucher C., Genin S.;
RT "Inventory and functional analysis of the large Hrp regulon in Ralstonia
RT solanacearum: identification of novel effector proteins translocated to
RT plant host cells through the type III secretion system.";
RL Mol. Microbiol. 53:115-128(2004).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=GMI1000;
RX PubMed=20687809; DOI=10.1094/mpmi-23-9-1197;
RA Macho A.P., Guidot A., Barberis P., Beuzon C.R., Genin S.;
RT "A competitive index assay identifies several Ralstonia solanacearum type
RT III effector mutant strains with reduced fitness in host plants.";
RL Mol. Plant Microbe Interact. 23:1197-1205(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, BIOTECHNOLOGY, REPEAT, DNA-BINDING,
RP AND MUTAGENESIS OF LYS-615; ASN-685; LYS-720 AND 1213-THR--THR-1245.
RX PubMed=23692030; DOI=10.1111/nph.12324;
RA de Lange O., Schreiber T., Schandry N., Radeck J., Braun K.H.,
RA Koszinowski J., Heuer H., Strauss A., Lahaye T.;
RT "Breaking the DNA-binding code of Ralstonia solanacearum TAL effectors
RT provides new possibilities to generate plant resistance genes against
RT bacterial wilt disease.";
RL New Phytol. 199:773-786(2013).
RN [5]
RP SUBCELLULAR LOCATION, DOMAIN, BIOTECHNOLOGY, AND REPEAT.
RX PubMed=23300258; DOI=10.1093/mp/sst006;
RA Li L., Atef A., Piatek A., Ali Z., Piatek M., Aouida M., Sharakuu A.,
RA Mahjoub A., Wang G., Khan S., Fedoroff N.V., Zhu J.K., Mahfouz M.M.;
RT "Characterization and DNA-binding specificities of Ralstonia TAL-like
RT effectors.";
RL Mol. Plant 6:1318-1330(2013).
RN [6]
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).
CC -!- FUNCTION: Exported into plant cells, where it is targeted to the
CC nucleus and probably acts as a transcription factor. Binds DNA in a
CC sequence-specific manner. May contribute to plant pathogenicity.
CC {ECO:0000269|PubMed:20687809, ECO:0000269|PubMed:23692030}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P14727}. Host
CC nucleus {ECO:0000269|PubMed:23300258, ECO:0000269|PubMed:23692030}.
CC Note=Secreted via type III secretion system (TTSS).
CC {ECO:0000250|UniProtKB:Q68A49}.
CC -!- INDUCTION: Regulated by hrpB, which controls the type III secretion
CC system. {ECO:0000269|PubMed:15225308}.
CC -!- DOMAIN: The central DNA-binding region is composed of 16 tandem core
CC repeats with 1 base-specifying residue (BSR residue 13, also called
CC repeat variable diresidue, RVD, residues 12 and 13). The BSR is
CC probably the only residue to contact DNA in a sequence-specific manner,
CC although other repeat residues effect repeat activity and specificity.
CC {ECO:0000269|PubMed:23692030, ECO:0000303|PubMed:23300258}.
CC -!- DOMAIN: There are at least 4 possible nuclear localization signals,
CC both N- and C-terminal regions contribute to nuclear localization.
CC {ECO:0000250|UniProtKB:Q68A49}.
CC -!- DOMAIN: The C-terminus encodes a plant transcriptional activation
CC domain. Replacement of the 295 last residues of AvrBs3 (AC P14727) with
CC the same region of this protein activates transcription in transformed
CC N.benthamiana leaves. {ECO:0000269|PubMed:23692030}.
CC -!- DISRUPTION PHENOTYPE: No alteration in pathogenicity on tomato
CC (S.lycopersicum cv Supermarmande) (PubMed:15225308), another study
CC found decreased pathogenicity on eggplant (S.melongena cv. Zebrina,
CC PubMed:20687809). {ECO:0000269|PubMed:15225308,
CC ECO:0000269|PubMed:20687809}.
CC -!- BIOTECHNOLOGY: By combining the DNA-binding domain with the catalytic
CC domain of the restriction endonuclease FokI, TALE-nuclease (TALEN)
CC enzymes able to target specific dsDNA sequences are created that enable
CC eukaryotic genome modification. Other potential uses as transcriptional
CC repressors, for transposon targeting, DNA methylation or histone tail
CC modifictions are also possible. {ECO:0000303|PubMed:23300258,
CC ECO:0000303|PubMed:23692030, ECO:0000303|PubMed:24602153}.
CC -!- SIMILARITY: Belongs to the transcription activator-like effector (TALE)
CC family. RipTAL/RTL subfamily. {ECO:0000305}.
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DR EMBL; AL646052; CAD15517.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8XYE3; -.
DR SMR; Q8XYE3; -.
DR STRING; 267608.RSc1815; -.
DR PRIDE; Q8XYE3; -.
DR EnsemblBacteria; CAD15517; CAD15517; RSc1815.
DR KEGG; rso:RSc1815; -.
DR PATRIC; fig|267608.8.peg.1857; -.
DR eggNOG; COG2201; Bacteria.
DR HOGENOM; CLU_003229_1_0_4; -.
DR OMA; SHNGGKQ; -.
DR PHI-base; PHI:2922; -.
DR PHI-base; PHI:5143; -.
DR PHI-base; PHI:5179; -.
DR Proteomes; UP000001436; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR005042; TAL_effector_rpt.
DR Pfam; PF03377; TAL_effector; 17.
PE 1: Evidence at protein level;
KW DNA-binding; Host nucleus; Reference proteome; Repeat; Secreted;
KW Transcription; Transcription regulation.
FT CHAIN 1..1245
FT /note="TAL effector protein Brg11"
FT /id="PRO_0000430627"
FT REPEAT 286..320
FT /note="Cryptic repeat -1"
FT /evidence="ECO:0000303|PubMed:23300258,
FT ECO:0000303|PubMed:23692030"
FT REPEAT 321..354
FT /note="Cryptic repeat 0"
FT /evidence="ECO:0000303|PubMed:23300258,
FT ECO:0000303|PubMed:23692030"
FT REPEAT 355..389
FT /note="Core repeat 1"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 390..424
FT /note="Core repeat 2"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 425..459
FT /note="Core repeat 3"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 460..494
FT /note="Core repeat 4"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 495..529
FT /note="Core repeat 5"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 530..564
FT /note="Core repeat 6"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 565..599
FT /note="Core repeat 7"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 600..634
FT /note="Core repeat 8"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 635..669
FT /note="Core repeat 9"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 670..704
FT /note="Core repeat 10"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 705..739
FT /note="Core repeat 11"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 740..774
FT /note="Core repeat 12"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 775..809
FT /note="Core repeat 13"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 810..844
FT /note="Core repeat 14"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 845..879
FT /note="Core repeat 15"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 880..914
FT /note="Core repeat 16"
FT /evidence="ECO:0000303|PubMed:15225308,
FT ECO:0000303|PubMed:23300258"
FT REPEAT 915..948
FT /note="Cryptic repeat +1"
FT /evidence="ECO:0000303|PubMed:23692030"
FT REPEAT 949..982
FT /note="Cryptic repeat +2"
FT /evidence="ECO:0000303|PubMed:23692030"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1245
FT /note="Activation domain"
FT /evidence="ECO:0000303|PubMed:23692030"
FT MOTIF 185..191
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250|UniProtKB:Q68A49"
FT MOTIF 980..983
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250|UniProtKB:Q68A49"
FT MOTIF 1108..1111
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000250|UniProtKB:Q68A49"
FT MOTIF 1145..1148
FT /note="Nuclear localization signal 4"
FT /evidence="ECO:0000250|UniProtKB:Q68A49"
FT COMPBIAS 22..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 615
FT /note="K->N: Decreased promoter activation in plants; when
FT associated with N-720."
FT /evidence="ECO:0000269|PubMed:23692030"
FT MUTAGEN 685
FT /note="N->K: Increased promoter activation in plants."
FT /evidence="ECO:0000269|PubMed:23692030"
FT MUTAGEN 720
FT /note="K->N: Decreased promoter activation in plants; when
FT associated with N-615."
FT /evidence="ECO:0000269|PubMed:23692030"
FT MUTAGEN 1213..1245
FT /note="Missing: Loss of transcription activation by an
FT AvrBs3-Brg11 chimera in plants."
FT /evidence="ECO:0000269|PubMed:23692030"
SQ SEQUENCE 1245 AA; 130712 MW; DCF30BB20411110E CRC64;
MRIGKSSGWL NESVSLEYEH VSPPTRPRDT RRRPRAAGDG GLAHLHRRLA VGYAEDTPRT
EARSPAPRRP LPVAPASAPP APSLVPEPPM PVSLPAVSSP RFSAGSSAAI TDPFPSLPPT
PVLYAMAREL EALSDATWQP AVPLPAEPPT DARRGNTVFD EASASSPVIA SACPQAFASP
PRAPRSARAR RARTGGDAWP APTFLSRPSS SRIGRDVFGK LVALGYSREQ IRKLKQESLS
EIAKYHTTLT GQGFTHADIC RISRRRQSLR VVARNYPELA AALPELTRAH IVDIARQRSG
DLALQALLPV ATALTAAPLR LSASQIATVA QYGERPAIQA LYRLRRKLTR APLHLTPQQV
VAIASNTGGK RALEAVCVQL PVLRAAPYRL STEQVVAIAS NKGGKQALEA VKAHLLDLLG
APYVLDTEQV VAIASHNGGK QALEAVKADL LDLRGAPYAL STEQVVAIAS HNGGKQALEA
VKADLLELRG APYALSTEQV VAIASHNGGK QALEAVKAHL LDLRGVPYAL STEQVVAIAS
HNGGKQALEA VKAQLLDLRG APYALSTAQV VAIASNGGGK QALEGIGEQL LKLRTAPYGL
STEQVVAIAS HDGGKQALEA VGAQLVALRA APYALSTEQV VAIASNKGGK QALEAVKAQL
LELRGAPYAL STAQVVAIAS HDGGNQALEA VGTQLVALRA APYALSTEQV VAIASHDGGK
QALEAVGAQL VALRAAPYAL NTEQVVAIAS SHGGKQALEA VRALFPDLRA APYALSTAQL
VAIASNPGGK QALEAVRALF RELRAAPYAL STEQVVAIAS NHGGKQALEA VRALFRGLRA
APYGLSTAQV VAIASSNGGK QALEAVWALL PVLRATPYDL NTAQIVAIAS HDGGKPALEA
VWAKLPVLRG APYALSTAQV VAIACISGQQ ALEAIEAHMP TLRQASHSLS PERVAAIACI
GGRSAVEAVR QGLPVKAIRR IRREKAPVAG PPPASLGPTP QELVAVLHFF RAHQQPRQAF
VDALAAFQAT RPALLRLLSS VGVTEIEALG GTIPDATERW QRLLGRLGFR PATGAAAPSP
DSLQGFAQSL ERTLGSPGMA GQSACSPHRK RPAETAIAPR SIRRSPNNAG QPSEPWPDQL
AWLQRRKRTA RSHIRADSAA SVPANLHLGT RAQFTPDRLR AEPGPIMQAH TSPASVSFGS
HVAFEPGLPD PGTPTSADLA SFEAEPFGVG PLDFHLDWLL QILET
