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B2SU53

- PTHX1_XANOP

UniProt

B2SU53 - PTHX1_XANOP

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Protein

TAL effector protein PthXo1

Gene

pthXo1

Organism
Xanthomonas oryzae pv. oryzae (strain PXO99A)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequence
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

Functioni

Avirulence protein. Acts as a transcription factor in rice, inducing expression of a number of host genes including SWEET11 (Os8N3, XA13, AC Q6YZF3) in susceptible plants with the Xa13 allele. Plants with the xa13 allele, which has an altered promoter, are resistant to bacterial blight caused by this bacterial strain and do not induce SWEET11. The xa13 allele elicits an atypical hypersensitive response (HR). PthXo1 binds SWEET11 promoter DNA in a sequence-specific manner.4 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW

GO - Biological processi

  1. modulation by symbiont of host defense-related programmed cell death Source: UniProtKB-KW
  2. pathogenesis Source: UniProtKB-KW
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Hypersensitive response elicitation, Transcription, Transcription regulation, Virulence

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciXORY360094:GI45-1609-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
TAL effector protein PthXo11 Publication
Alternative name(s):
Avirulence protein PthXo11 Publication
TAL effector protein Tal2b1 Publication
Gene namesi
Name:pthXo1
Synonyms:tal2b
Ordered Locus Names:PXO_00227
OrganismiXanthomonas oryzae pv. oryzae (strain PXO99A)
Taxonomic identifieri360094 [NCBI]
Taxonomic lineageiBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas ›
ProteomesiUP000001740: Chromosome

Subcellular locationi

Secreted By similarity. Host nucleus By similarity
Note: Secreted via a type III secretions system (TTSS). Localizes to the plant cell nucleus.By similarity

GO - Cellular componenti

  1. host cell nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Host nucleus, Secreted

Pathology & Biotechi

Biotechnological usei

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. Other potential uses as transcriptional repressors, for transposon targeting, DNA methylation or histone tail modifictions are also possible.1 Publication2 Publications

Disruption phenotypei

Reduced virulence in susceptible rice; its introduction into a deletion mutant restores virulence to the bacteria in rice plants. No longer induces SWEET11 (Os8N3, XA13, AC Q6YZF3).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13731373TAL effector protein PthXo1PRO_0000430621Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi360094.PXO_00227.

Structurei

Secondary structure

1
1373
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi222 – 2287Combined sources
Helixi234 – 24512Combined sources
Turni246 – 2527Combined sources
Helixi258 – 2669Combined sources
Helixi268 – 28215Combined sources
Helixi291 – 2988Combined sources
Helixi303 – 31311Combined sources
Helixi315 – 3195Combined sources
Helixi325 – 3284Combined sources
Turni329 – 3335Combined sources
Helixi337 – 35418Combined sources
Helixi359 – 3668Combined sources
Helixi371 – 38111Combined sources
Helixi383 – 3897Combined sources
Helixi393 – 4008Combined sources
Helixi405 – 42218Combined sources
Helixi427 – 4348Combined sources
Beta strandi435 – 4384Combined sources
Helixi440 – 45415Combined sources
Helixi461 – 4688Combined sources
Helixi473 – 48816Combined sources
Helixi495 – 50410Combined sources
Helixi506 – 52116Combined sources
Helixi528 – 5358Combined sources
Turni538 – 5403Combined sources
Helixi541 – 55515Combined sources
Helixi562 – 5687Combined sources
Beta strandi569 – 5713Combined sources
Helixi574 – 59118Combined sources
Helixi597 – 6037Combined sources
Helixi608 – 61811Combined sources
Helixi620 – 6223Combined sources
Turni623 – 6264Combined sources
Helixi631 – 6377Combined sources
Helixi643 – 65614Combined sources
Turni657 – 6593Combined sources
Helixi664 – 6707Combined sources
Helixi676 – 68611Combined sources
Helixi688 – 6947Combined sources
Helixi699 – 7024Combined sources
Turni703 – 7064Combined sources
Helixi711 – 72717Combined sources
Helixi733 – 7397Combined sources
Helixi744 – 75411Combined sources
Helixi757 – 7604Combined sources
Helixi766 – 7694Combined sources
Turni770 – 7734Combined sources
Helixi778 – 78811Combined sources
Helixi800 – 8078Combined sources
Helixi812 – 82615Combined sources
Beta strandi829 – 8313Combined sources
Helixi835 – 8417Combined sources
Helixi846 – 8549Combined sources
Turni855 – 8595Combined sources
Turni861 – 8633Combined sources
Helixi868 – 8758Combined sources
Helixi880 – 89718Combined sources
Helixi902 – 9098Combined sources
Helixi914 – 92916Combined sources
Helixi936 – 9438Combined sources
Helixi948 – 95811Combined sources
Helixi960 – 9645Combined sources
Helixi970 – 9767Combined sources
Beta strandi979 – 9813Combined sources
Turni982 – 9843Combined sources
Helixi985 – 99713Combined sources
Turni998 – 10003Combined sources
Helixi1004 – 10118Combined sources
Turni1012 – 10143Combined sources
Helixi1015 – 10239Combined sources
Helixi1026 – 10316Combined sources
Turni1037 – 10393Combined sources
Beta strandi1040 – 10423Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UGMX-ray3.00A127-1149[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati221 – 23919Cryptic repeat -11 PublicationAdd
BLAST
Repeati256 – 27318Cryptic repeat 01 PublicationAdd
BLAST
Repeati289 – 32234Core repeat 11 PublicationAdd
BLAST
Repeati323 – 35634Core repeat 21 PublicationAdd
BLAST
Repeati357 – 39034Core repeat 31 PublicationAdd
BLAST
Repeati391 – 42434Core repeat 41 PublicationAdd
BLAST
Repeati425 – 45834Core repeat 51 PublicationAdd
BLAST
Repeati459 – 49234Core repeat 61 PublicationAdd
BLAST
Repeati493 – 52533Core repeat 71 PublicationAdd
BLAST
Repeati526 – 55934Core repeat 81 PublicationAdd
BLAST
Repeati560 – 59334Core repeat 91 PublicationAdd
BLAST
Repeati594 – 62734Core repeat 101 PublicationAdd
BLAST
Repeati628 – 66134Core repeat 111 PublicationAdd
BLAST
Repeati662 – 69534Core repeat 121 PublicationAdd
BLAST
Repeati696 – 72934Core repeat 131 PublicationAdd
BLAST
Repeati714 – 76047HEAT 1Sequence AnalysisAdd
BLAST
Repeati730 – 76334Core repeat 141 PublicationAdd
BLAST
Repeati764 – 79734Core repeat 151 PublicationAdd
BLAST
Repeati782 – 82847HEAT 2Sequence AnalysisAdd
BLAST
Repeati798 – 83134Core repeat 161 PublicationAdd
BLAST
Repeati832 – 86534Core repeat 171 PublicationAdd
BLAST
Repeati850 – 89344HEAT 3Sequence AnalysisAdd
BLAST
Repeati866 – 89934Core repeat 181 PublicationAdd
BLAST
Repeati900 – 93334Core repeat 191 PublicationAdd
BLAST
Repeati918 – 96144HEAT 4Sequence AnalysisAdd
BLAST
Repeati934 – 96734Core repeat 201 PublicationAdd
BLAST
Repeati968 – 100134Core repeat 211 PublicationAdd
BLAST
Repeati1002 – 103433Core repeat 221 PublicationAdd
BLAST
Repeati1035 – 106834Core repeat 231 PublicationAdd
BLAST
Repeati1053 – 109139HEAT 5Sequence AnalysisAdd
BLAST
Repeati1069 – 108719Core repeat 23.51 PublicationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1136 – 1364229Acidic activation domainBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1222 – 12254Nuclear localization signal NLS1By similarity
Motifi1268 – 12714Nuclear localization signal NLS2By similarity
Motifi1305 – 13084Nuclear localization signal NLS3By similarity

Domaini

The central DNA-binding region is composed of 23.5 tandem core repeats with 1 base-specifying residue (BSR residue 13, also called the repeat variable diresidue, RVD, residues 12 and 13) each of which recognizes 1 base in the target DNA. The BSR is the only residue which contacts DNA in a sequence-specific manner.1 Publication

Sequence similaritiesi

Belongs to the transcription activator-like effector (TALE) family.Curated
Contains 5 HEAT repeats.Sequence Analysis

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000060719.
OrthoDBiEOG64JFJ5.

Family and domain databases

InterProiIPR005042. Avirulence_Avr-rel.
[Graphical view]
PfamiPF03377. Avirulence. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B2SU53-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDPIRSRTPS PARELLPGPQ PDRVQPTADR GGAPPAGGPL DGLPARRTMS 
        60         70         80         90        100
RTRLPSPPAP SPAFSAGSFS DLLRQFDPSL LDTSLLDSMP AVGTPHTAAA 
       110        120        130        140        150
PAECDEVQSG LRAADDPPPT VRVAVTAARP PRAKPAPRRR AAQPSDASPA 
       160        170        180        190        200
AQVDLRTLGY SQQQQEKIKP KVGSTVAQHH EALVGHGFTH AHIVALSRHP 
       210        220        230        240        250
AALGTVAVKY QDMIAALPEA THEDIVGVGK QWSGARALEA LLTVAGELRG 
       260        270        280        290        300
PPLQLDTGQL VKIAKRGGVT AVEAVHASRN ALTGAPLNLT PAQVVAIASN 
       310        320        330        340        350
NGGKQALETV QRLLPVLCQA HGLTPAQVVA IASHDGGKQA LETMQRLLPV 
       360        370        380        390        400
LCQAHGLPPD QVVAIASNIG GKQALETVQR LLPVLCQAHG LTPDQVVAIA 
       410        420        430        440        450
SHGGGKQALE TVQRLLPVLC QAHGLTPDQV VAIASHDGGK QALETVQRLL 
       460        470        480        490        500
PVLCQAHGLT PDQVVAIASN GGGKQALETV QRLLPVLCQA HGLTPDQVVA 
       510        520        530        540        550
IASNGGKQAL ETVQRLLPVL CQAHGLTPDQ VVAIASHDGG KQALETVQRL 
       560        570        580        590        600
LPVLCQTHGL TPAQVVAIAS HDGGKQALET VQQLLPVLCQ AHGLTPDQVV 
       610        620        630        640        650
AIASNIGGKQ ALATVQRLLP VLCQAHGLTP DQVVAIASNG GGKQALETVQ 
       660        670        680        690        700
RLLPVLCQAH GLTPDQVVAI ASNGGGKQAL ETVQRLLPVL CQAHGLTQVQ 
       710        720        730        740        750
VVAIASNIGG KQALETVQRL LPVLCQAHGL TPAQVVAIAS HDGGKQALET 
       760        770        780        790        800
VQRLLPVLCQ AHGLTPDQVV AIASNGGGKQ ALETVQRLLP VLCQAHGLTQ 
       810        820        830        840        850
EQVVAIASNN GGKQALETVQ RLLPVLCQAH GLTPDQVVAI ASNGGGKQAL 
       860        870        880        890        900
ETVQRLLPVL CQAHGLTPAQ VVAIASNIGG KQALETVQRL LPVLCQDHGL 
       910        920        930        940        950
TLAQVVAIAS NIGGKQALET VQRLLPVLCQ AHGLTQDQVV AIASNIGGKQ 
       960        970        980        990       1000
ALETVQRLLP VLCQDHGLTP DQVVAIASNI GGKQALETVQ RLLPVLCQDH 
      1010       1020       1030       1040       1050
GLTLDQVVAI ASNGGKQALE TVQRLLPVLC QDHGLTPDQV VAIASNSGGK 
      1060       1070       1080       1090       1100
QALETVQRLL PVLCQDHGLT PNQVVAIASN GGKQALESIV AQLSRPDPAL 
      1110       1120       1130       1140       1150
AALTNDHLVA LACLGGRPAM DAVKKGLPHA PELIRRVNRR IGERTSHRVA 
      1160       1170       1180       1190       1200
DYAQVVRVLE FFQCHSHPAY AFDEAMTQFG MSRNGLVQLF RRVGVTELEA 
      1210       1220       1230       1240       1250
RGGTLPPASQ RWDRILQASG MKRAKPSPTS AQTPDQASLH AFADSLERDL 
      1260       1270       1280       1290       1300
DAPSPMHEGD QTGASSRKRS RSDRAVTGPS AQHSFEVRVP EQRDALHLPL 
      1310       1320       1330       1340       1350
SWRVKRPRTR IGGGLPDPGT PIAADLAASS TVMWEQDAAP FAGAADDFPA 
      1360       1370 
FNEEELAWLM ELLPQSGSVG GTI
Length:1,373
Mass (Da):143,535
Last modified:October 16, 2013 - v2
Checksum:iC96C8A8A862A8217
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti358 – 3581P → T in AAS46025. (PubMed:15553245)Curated
Sequence conflicti1120 – 11201M → L in AAS46025. (PubMed:15553245)Curated
Sequence conflicti1137 – 11371V → I in AAS46025. (PubMed:15553245)Curated
Sequence conflicti1142 – 11421G → P in AAS46025. (PubMed:15553245)Curated
Sequence conflicti1150 – 11545ADYAQ → PDLAH in AAS46025. (PubMed:15553245)Curated
Sequence conflicti1160 – 11645EFFQC → GFFQS in AAS46025. (PubMed:15553245)Curated
Sequence conflicti1170 – 11745YAFDE → QAFDD in AAS46025. (PubMed:15553245)Curated
Sequence conflicti1184 – 11841N → H in AAS46025. (PubMed:15553245)Curated
Sequence conflicti1198 – 12025LEARG → FEARY in AAS46025. (PubMed:15553245)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000967 Genomic DNA. Translation: ACD58243.2.
AY495676 Genomic DNA. Translation: AAS46025.1.
RefSeqiYP_001912775.1. NC_010717.1.

Genome annotation databases

EnsemblBacteriaiACD58243; ACD58243; PXO_00227.
GeneIDi6305128.
KEGGixop:PXO_00227.
PATRICi24122580. VBIXanOry73153_1663.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 CP000967 Genomic DNA. Translation: ACD58243.2 .
AY495676 Genomic DNA. Translation: AAS46025.1 .
RefSeqi YP_001912775.1. NC_010717.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UGM X-ray 3.00 A 127-1149 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 360094.PXO_00227.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACD58243 ; ACD58243 ; PXO_00227 .
GeneIDi 6305128.
KEGGi xop:PXO_00227.
PATRICi 24122580. VBIXanOry73153_1663.

Phylogenomic databases

HOGENOMi HOG000060719.
OrthoDBi EOG64JFJ5.

Enzyme and pathway databases

BioCyci XORY360094:GI45-1609-MONOMER.

Family and domain databases

InterProi IPR005042. Avirulence_Avr-rel.
[Graphical view ]
Pfami PF03377. Avirulence. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PXO99A.
  2. "Diverse members of the AvrBs3/PthA family of type III effectors are major virulence determinants in bacterial blight disease of rice."
    Yang B., White F.F.
    Mol. Plant Microbe Interact. 17:1192-1200(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-1241, FUNCTION, DISRUPTION PHENOTYPE.
    Strain: PXO99A.
  3. "Os8N3 is a host disease-susceptibility gene for bacterial blight of rice."
    Yang B., Sugio A., White F.F.
    Proc. Natl. Acad. Sci. U.S.A. 103:10503-10508(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INDUCTION OF HOST GENES.
    Strain: PXO99A.
  4. "Promoter elements of rice susceptibility genes are bound and activated by specific TAL effectors from the bacterial blight pathogen, Xanthomonas oryzae pv. oryzae."
    Roemer P., Recht S., Strauss T., Elsaesser J., Schornack S., Boch J., Wang S., Lahaye T.
    New Phytol. 187:1048-1057(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  5. Cited for: BIOTECHNOLOGY.
  6. "TALEN-mediated genome editing: prospects and perspectives."
    Wright D.A., Li T., Yang B., Spalding M.H.
    Biochem. J. 462:15-24(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOTECHNOLOGY USES REVIEW.
  7. "From dead leaf, to new life: TAL effectors as tools for synthetic biology."
    de Lange O., Binder A., Lahaye T.
    Plant J. 78:753-771(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOTECHNOLOGY USES REVIEW.
  8. "The crystal structure of TAL effector PthXo1 bound to its DNA target."
    Mak A.N., Bradley P., Cernadas R.A., Bogdanove A.J., Stoddard B.L.
    Science 335:716-719(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 127-1149 IN COMPLEX WITH DNA, DNA-BINDING, DOMAIN.
    Strain: PXO99A.

Entry informationi

Entry nameiPTHX1_XANOP
AccessioniPrimary (citable) accession number: B2SU53
Secondary accession number(s): Q6RKD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: October 16, 2013
Last modified: January 7, 2015
This is version 36 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
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