Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - B2SU53 (PTHX1_XANOP)

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

TAL effector protein PthXo1

Gene

pthXo1

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

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

Complete GO annotation...

GO - Biological processi

Complete GO annotation...

Keywordsi

Molecular functionDNA-binding
Biological processHypersensitive response elicitation, Transcription, Transcription regulation, Virulence

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 ›
Proteomesi
  • UP000001740 Componenti: 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

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.2 Publications1 Publication

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)DescriptionActionsGraphical viewLength
ChainiPRO_00004306211 – 1373TAL effector protein PthXo1Add BLAST1373

Structurei

Secondary structure

11373
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi222 – 228Combined sources7
Helixi234 – 245Combined sources12
Turni246 – 252Combined sources7
Helixi258 – 266Combined sources9
Helixi268 – 282Combined sources15
Helixi291 – 298Combined sources8
Helixi303 – 313Combined sources11
Helixi315 – 319Combined sources5
Helixi325 – 328Combined sources4
Turni329 – 333Combined sources5
Helixi337 – 354Combined sources18
Helixi359 – 366Combined sources8
Helixi371 – 381Combined sources11
Helixi383 – 389Combined sources7
Helixi393 – 400Combined sources8
Helixi405 – 422Combined sources18
Helixi427 – 434Combined sources8
Beta strandi435 – 438Combined sources4
Helixi440 – 454Combined sources15
Helixi461 – 468Combined sources8
Helixi473 – 488Combined sources16
Helixi495 – 504Combined sources10
Helixi506 – 521Combined sources16
Helixi528 – 535Combined sources8
Turni538 – 540Combined sources3
Helixi541 – 555Combined sources15
Helixi562 – 568Combined sources7
Beta strandi569 – 571Combined sources3
Helixi574 – 591Combined sources18
Helixi597 – 603Combined sources7
Helixi608 – 618Combined sources11
Helixi620 – 622Combined sources3
Turni623 – 626Combined sources4
Helixi631 – 637Combined sources7
Helixi643 – 656Combined sources14
Turni657 – 659Combined sources3
Helixi664 – 670Combined sources7
Helixi676 – 686Combined sources11
Helixi688 – 694Combined sources7
Helixi699 – 702Combined sources4
Turni703 – 706Combined sources4
Helixi711 – 727Combined sources17
Helixi733 – 739Combined sources7
Helixi744 – 754Combined sources11
Helixi757 – 760Combined sources4
Helixi766 – 769Combined sources4
Turni770 – 773Combined sources4
Helixi778 – 788Combined sources11
Helixi800 – 807Combined sources8
Helixi812 – 826Combined sources15
Beta strandi829 – 831Combined sources3
Helixi835 – 841Combined sources7
Helixi846 – 854Combined sources9
Turni855 – 859Combined sources5
Turni861 – 863Combined sources3
Helixi868 – 875Combined sources8
Helixi880 – 897Combined sources18
Helixi902 – 909Combined sources8
Helixi914 – 929Combined sources16
Helixi936 – 943Combined sources8
Helixi948 – 958Combined sources11
Helixi960 – 964Combined sources5
Helixi970 – 976Combined sources7
Beta strandi979 – 981Combined sources3
Turni982 – 984Combined sources3
Helixi985 – 997Combined sources13
Turni998 – 1000Combined sources3
Helixi1004 – 1011Combined sources8
Turni1012 – 1014Combined sources3
Helixi1015 – 1023Combined sources9
Helixi1026 – 1031Combined sources6
Turni1037 – 1039Combined sources3
Beta strandi1040 – 1042Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UGMX-ray3.00A127-1149[»]
SMRiB2SU53.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati221 – 239Cryptic repeat -11 PublicationAdd BLAST19
Repeati256 – 273Cryptic repeat 01 PublicationAdd BLAST18
Repeati289 – 322Core repeat 11 PublicationAdd BLAST34
Repeati323 – 356Core repeat 21 PublicationAdd BLAST34
Repeati357 – 390Core repeat 31 PublicationAdd BLAST34
Repeati391 – 424Core repeat 41 PublicationAdd BLAST34
Repeati425 – 458Core repeat 51 PublicationAdd BLAST34
Repeati459 – 492Core repeat 61 PublicationAdd BLAST34
Repeati493 – 525Core repeat 71 PublicationAdd BLAST33
Repeati526 – 559Core repeat 81 PublicationAdd BLAST34
Repeati560 – 593Core repeat 91 PublicationAdd BLAST34
Repeati594 – 627Core repeat 101 PublicationAdd BLAST34
Repeati628 – 661Core repeat 111 PublicationAdd BLAST34
Repeati662 – 695Core repeat 121 PublicationAdd BLAST34
Repeati696 – 729Core repeat 131 PublicationAdd BLAST34
Repeati714 – 760HEAT 1Sequence analysisAdd BLAST47
Repeati730 – 763Core repeat 141 PublicationAdd BLAST34
Repeati764 – 797Core repeat 151 PublicationAdd BLAST34
Repeati782 – 828HEAT 2Sequence analysisAdd BLAST47
Repeati798 – 831Core repeat 161 PublicationAdd BLAST34
Repeati832 – 865Core repeat 171 PublicationAdd BLAST34
Repeati850 – 893HEAT 3Sequence analysisAdd BLAST44
Repeati866 – 899Core repeat 181 PublicationAdd BLAST34
Repeati900 – 933Core repeat 191 PublicationAdd BLAST34
Repeati918 – 961HEAT 4Sequence analysisAdd BLAST44
Repeati934 – 967Core repeat 201 PublicationAdd BLAST34
Repeati968 – 1001Core repeat 211 PublicationAdd BLAST34
Repeati1002 – 1034Core repeat 221 PublicationAdd BLAST33
Repeati1035 – 1068Core repeat 231 PublicationAdd BLAST34
Repeati1053 – 1091HEAT 5Sequence analysisAdd BLAST39
Repeati1069 – 1087Core repeat 23.51 PublicationAdd BLAST19

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1136 – 1364Acidic activation domainBy similarityAdd BLAST229

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1222 – 1225Nuclear localization signal NLS1By similarity4
Motifi1268 – 1271Nuclear localization signal NLS2By similarity4
Motifi1305 – 1308Nuclear localization signal NLS3By similarity4

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

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000060719.
KOiK18876.

Family and domain databases

Gene3Di3.40.47.10. 2 hits.
InterProiView protein in InterPro
IPR005042. TAL_effector_rpt.
IPR016039. Thiolase-like.
PfamiView protein in Pfam
PF03377. TAL_effector. 24 hits.

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)DescriptionActionsGraphical viewLength
Sequence conflicti358P → T in AAS46025 (PubMed:15553245).Curated1
Sequence conflicti1120M → L in AAS46025 (PubMed:15553245).Curated1
Sequence conflicti1137V → I in AAS46025 (PubMed:15553245).Curated1
Sequence conflicti1142G → P in AAS46025 (PubMed:15553245).Curated1
Sequence conflicti1150 – 1154ADYAQ → PDLAH in AAS46025 (PubMed:15553245).Curated5
Sequence conflicti1160 – 1164EFFQC → GFFQS in AAS46025 (PubMed:15553245).Curated5
Sequence conflicti1170 – 1174YAFDE → QAFDD in AAS46025 (PubMed:15553245).Curated5
Sequence conflicti1184N → H in AAS46025 (PubMed:15553245).Curated1
Sequence conflicti1198 – 1202LEARG → FEARY in AAS46025 (PubMed:15553245).Curated5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000967 Genomic DNA. Translation: ACD58243.2.
AY495676 Genomic DNA. Translation: AAS46025.1.
RefSeqiWP_041182630.1. NC_010717.2.

Genome annotation databases

EnsemblBacteriaiACD58243; ACD58243; PXO_00227.
KEGGixop:PXO_00227.

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 one 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.

Entry informationi

Entry nameiPTHX1_XANOP
AccessioniPrimary (citable) accession number: B2SU53
Secondary accession number(s): Q6RKD2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 29, 2014
Last sequence update: October 16, 2013
Last modified: June 7, 2017
This is version 48 of the entry and version 2 of the sequence. See 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