HPAB2_PSESM
ID HPAB2_PSESM Reviewed; 553 AA.
AC Q8RSY1; Q7C4D6;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Effector protein HopAB2;
DE AltName: Full=Avirulence protein AvrPtoB;
DE Includes:
DE RecName: Full=E3 ubiquitin-protein ligase;
DE EC=2.3.2.-;
DE AltName: Full=E3 ubiquitin-protein transferase {ECO:0000305};
GN Name=hopAB2; Synonyms=avrPtoB; OrderedLocusNames=PSPTO_3087;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN AVIRULENCE, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF GLY-325; ILE-326; ASN-327; ASP-331 AND
RP GLY-333.
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12062102; DOI=10.1016/s0092-8674(02)00743-2;
RA Kim Y.-J., Lin N.-C., Martin G.B.;
RT "Two distinct Pseudomonas effector proteins interact with the Pto kinase
RT and activate plant immunity.";
RL Cell 109:589-598(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
RN [3]
RP INDUCTION BY HRPL.
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=11854524; DOI=10.1073/pnas.032514099;
RA Fouts D.E., Abramovitch R.B., Alfano J.R., Baldo A.M., Buell C.R.,
RA Cartinhour S., Chatterjee A.K., D'Ascenzo M., Gwinn M.L., Lazarowitz S.G.,
RA Lin N.-C., Martin G.B., Rehm A.H., Schneider D.J., van Dijk K., Tang X.,
RA Collmer A.;
RT "Genomewide identification of Pseudomonas syringae pv. tomato DC3000
RT promoters controlled by the HrpL alternative sigma factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2275-2280(2002).
RN [4]
RP FUNCTION IN VIRULENCE.
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12505984; DOI=10.1093/emboj/cdg006;
RA Abramovitch R.B., Kim Y.-J., Chen S., Dickman M.B., Martin G.B.;
RT "Pseudomonas type III effector AvrPtoB induces plant disease susceptibility
RT by inhibition of host programmed cell death.";
RL EMBO J. 22:60-69(2003).
RN [5]
RP FUNCTION IN ETHYLENE-DEPENDENT CELL DEATH.
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=16167902; DOI=10.1111/j.1365-313x.2005.02516.x;
RA Cohn J.R., Martin G.B.;
RT "Pseudomonas syringae pv. tomato type III effectors AvrPto and AvrPtoB
RT promote ethylene-dependent cell death in tomato.";
RL Plant J. 44:139-154(2005).
RN [6]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE.
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=16477026; DOI=10.1073/pnas.0507892103;
RA Abramovitch R.B., Janjusevic R., Stebbins C.E., Martin G.B.;
RT "Type III effector AvrPtoB requires intrinsic E3 ubiquitin ligase activity
RT to suppress plant cell death and immunity.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:2851-2856(2006).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 436-553, MUTAGENESIS OF LYS-453;
RP LYS-464; LYS-512; 520-LYS-LYS-521; LYS-529; PRO-533 AND LYS-546, AND
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE.
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=16373536; DOI=10.1126/science.1120131;
RA Janjusevic R., Abramovitch R.B., Martin G.B., Stebbins C.E.;
RT "A bacterial inhibitor of host programmed cell death defenses is an E3
RT ubiquitin ligase.";
RL Science 311:222-226(2006).
CC -!- FUNCTION: Effector protein involved in gene-for-gene resistance in
CC tomato plants. It is recognized by the host Pto resistance protein and
CC elicits Pto and Prf-dependent hypersensitive response (HR) and
CC programmed cell death (PCD), resulting in host immunity. In susceptible
CC plants, acts as a virulence factor by suppressing PCD and HR-based
CC plant immunity. This function requires its E3 ubiquitin ligase activity
CC probably by recruiting E2 enzymes and transferring ubiquitin molecules
CC to cellular proteins involved in regulation of PCD and targeting them
CC for degradation. Also, induces expression of host genes involved in
CC ethylene biosynthesis and signaling, in particular ACO1 and ACO2,
CC encoding the ethylene-forming enzyme ACC oxidase.
CC {ECO:0000269|PubMed:12062102, ECO:0000269|PubMed:12505984,
CC ECO:0000269|PubMed:16167902, ECO:0000269|PubMed:16373536,
CC ECO:0000269|PubMed:16477026}.
CC -!- SUBUNIT: Interacts physically with plant cell Pto.
CC -!- INTERACTION:
CC Q8RSY1; P62980: UBI3; Xeno; NbExp=3; IntAct=EBI-15569263, EBI-15569288;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12062102}.
CC Note=Secreted via type III secretion system (TTSS). Localized to the
CC plant cell cytoplasm.
CC -!- INDUCTION: Transcriptionally induced by HrpL.
CC {ECO:0000269|PubMed:11854524}.
CC -!- PTM: Auto-ubiquitinated.
CC -!- MISCELLANEOUS: Unlike many effector proteins, it is widely conserved
CC among diverse genera of plant pathogens including Xanthomonas, Erwinia
CC and many strains of Pseudomonas.
CC -!- MISCELLANEOUS: Acts as a general eukaryotic PCD inhibitor in plants and
CC yeast.
CC -!- SIMILARITY: Belongs to the HopAB family. {ECO:0000305}.
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DR EMBL; AY074795; AAL71883.1; -; Genomic_DNA.
DR EMBL; AE016853; AAO56576.1; -; Genomic_DNA.
DR RefSeq; NP_792881.1; NC_004578.1.
DR RefSeq; WP_011104378.1; NC_004578.1.
DR PDB; 2FD4; X-ray; 1.80 A; A=436-553.
DR PDB; 3HGK; X-ray; 3.30 A; E/F/G/H=121-205.
DR PDB; 3HGL; X-ray; 1.90 A; A=121-205.
DR PDB; 3TL8; X-ray; 2.50 A; B/F/K/L=250-359.
DR PDBsum; 2FD4; -.
DR PDBsum; 3HGK; -.
DR PDBsum; 3HGL; -.
DR PDBsum; 3TL8; -.
DR AlphaFoldDB; Q8RSY1; -.
DR SMR; Q8RSY1; -.
DR DIP; DIP-60253N; -.
DR IntAct; Q8RSY1; 4.
DR STRING; 223283.PSPTO_3087; -.
DR PRIDE; Q8RSY1; -.
DR EnsemblBacteria; AAO56576; AAO56576; PSPTO_3087.
DR GeneID; 1184744; -.
DR KEGG; pst:PSPTO_3087; -.
DR PATRIC; fig|223283.9.peg.3153; -.
DR eggNOG; ENOG5030NBE; Bacteria.
DR HOGENOM; CLU_505137_0_0_6; -.
DR OMA; TSCLFGE; -.
DR OrthoDB; 2112897at2; -.
DR EvolutionaryTrace; Q8RSY1; -.
DR PHI-base; PHI:2743; -.
DR PHI-base; PHI:990; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0034053; P:modulation by symbiont of host defense-related programmed cell death; IEA:UniProtKB-KW.
DR GO; GO:0052018; P:modulation by symbiont of RNA levels in host; IDA:JCVI.
DR CDD; cd12803; HopAB_BID; 1.
DR CDD; cd12802; HopAB_PID; 1.
DR Gene3D; 1.20.1280.220; -; 1.
DR Gene3D; 3.30.40.110; -; 1.
DR InterPro; IPR015133; E3_ubiquit_lig_AvrPtoB.
DR InterPro; IPR031759; HopAB_BAK-bd.
DR InterPro; IPR038342; HopAB_BAK-bd_sf.
DR InterPro; IPR038448; HopAB_E3_ubiquit_lig_sf.
DR InterPro; IPR033743; HopAB_PID.
DR Pfam; PF09046; AvrPtoB-E3_ubiq; 1.
DR Pfam; PF16847; AvrPtoB_bdg; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hypersensitive response elicitation; Reference proteome;
KW Secreted; Transferase; Ubl conjugation; Ubl conjugation pathway; Virulence.
FT CHAIN 1..553
FT /note="Effector protein HopAB2"
FT /id="PRO_0000234081"
FT REGION 1..308
FT /note="Host recognition; Pto interaction"
FT REGION 1..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..553
FT /note="E3 ubiquitin-protein ligase"
FT REGION 361..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..529
FT /note="Required for E3 ubiquitin-protein ligase and anti-
FT PCD activities and pathogenesis"
FT MOTIF 325..328
FT /note="Interaction with Pto-kinase"
FT COMPBIAS 28..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..58
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 479
FT /note="E2-binding"
FT /evidence="ECO:0000305"
FT SITE 525
FT /note="E2-binding"
FT /evidence="ECO:0000305"
FT SITE 533
FT /note="E2-binding"
FT /evidence="ECO:0000305"
FT MUTAGEN 325
FT /note="G->A: Reduces interaction with Pto and fails to
FT elicit Pto-dependent defense response in tomato leaves."
FT /evidence="ECO:0000269|PubMed:12062102"
FT MUTAGEN 326
FT /note="I->T: Reduces interaction with Pto and fails to
FT elicit Pto-dependent defense response in tomato leaves."
FT /evidence="ECO:0000269|PubMed:12062102"
FT MUTAGEN 327
FT /note="N->A: Reduces interaction with Pto."
FT /evidence="ECO:0000269|PubMed:12062102"
FT MUTAGEN 331
FT /note="D->A: No effect in the interaction with Pto."
FT /evidence="ECO:0000269|PubMed:12062102"
FT MUTAGEN 333
FT /note="G->A: No effect in the interaction with Pto and no
FT effect in the induction of Pto-dependent defense response."
FT /evidence="ECO:0000269|PubMed:12062102"
FT MUTAGEN 453
FT /note="K->R: No effect in ubiquitination."
FT /evidence="ECO:0000269|PubMed:16373536"
FT MUTAGEN 464
FT /note="K->R: No effect in ubiquitination."
FT /evidence="ECO:0000269|PubMed:16373536"
FT MUTAGEN 479
FT /note="F->A: Loses ubiquitination activity."
FT MUTAGEN 512
FT /note="K->R: 5- to 50-fold reduction in ubiquitin
FT interactions. Suppress PCD in susceptible tomato leaves."
FT /evidence="ECO:0000269|PubMed:16373536"
FT MUTAGEN 520..521
FT /note="KK->RR: 5- to 50-fold reduction in ubiquitin
FT interactions. Suppress PCD in susceptible tomato leaves."
FT /evidence="ECO:0000269|PubMed:16373536"
FT MUTAGEN 525
FT /note="F->A: Loses ubiquitination activity."
FT MUTAGEN 529
FT /note="K->R: 5- to 50-fold reduction in ubiquitin
FT interactions. Suppress PCD in susceptible tomato leaves."
FT /evidence="ECO:0000269|PubMed:16373536"
FT MUTAGEN 533
FT /note="P->A: Loses ubiquitination activity."
FT /evidence="ECO:0000269|PubMed:16373536"
FT MUTAGEN 546
FT /note="K->R: No effect in ubiquitination."
FT /evidence="ECO:0000269|PubMed:16373536"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:3HGL"
FT HELIX 143..154
FT /evidence="ECO:0007829|PDB:3HGL"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:3HGL"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:3HGL"
FT HELIX 186..200
FT /evidence="ECO:0007829|PDB:3HGL"
FT HELIX 271..291
FT /evidence="ECO:0007829|PDB:3TL8"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:3TL8"
FT HELIX 315..323
FT /evidence="ECO:0007829|PDB:3TL8"
FT HELIX 340..351
FT /evidence="ECO:0007829|PDB:3TL8"
FT HELIX 442..447
FT /evidence="ECO:0007829|PDB:2FD4"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:2FD4"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:2FD4"
FT STRAND 492..498
FT /evidence="ECO:0007829|PDB:2FD4"
FT STRAND 514..518
FT /evidence="ECO:0007829|PDB:2FD4"
FT HELIX 519..528
FT /evidence="ECO:0007829|PDB:2FD4"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:2FD4"
FT TURN 541..543
FT /evidence="ECO:0007829|PDB:2FD4"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:2FD4"
FT STRAND 548..552
FT /evidence="ECO:0007829|PDB:2FD4"
SQ SEQUENCE 553 AA; 59453 MW; 6C638B7DF2D7B399 CRC64;
MAGINRAGPS GAYFVGHTDP EPVSGQAHGS GSGASSSNSP QVQPRPSNTP PSNAPAPPPT
GRERLSRSTA LSRQTREWLE QGMPTAEDAS VRRRPQVTAD AATPRAEARR TPEATADASA
PRRGAVAHAN SIVQQLVSEG ADISHTRNML RNAMNGDAVA FSRVEQNIFR QHFPNMPMHG
ISRDSELAIE LRGALRRAVH QQAASAPVRS PTPTPASPAA SSSGSSQRSL FGRFARLMAP
NQGRSSNTAA SQTPVDRSPP RVNQRPIRVD RAAMRNRGND EADAALRGLV QQGVNLEHLR
TALERHVMQR LPIPLDIGSA LQNVGINPSI DLGESLVQHP LLNLNVALNR MLGLRPSAER
APRPAVPVAP ATASRRPDGT RATRLRVMPE REDYENNVAY GVRLLNLNPG VGVRQAVAAF
VTDRAERPAV VANIRAALDP IASQFSQLRT ISKADAESEE LGFKDAADHH TDDVTHCLFG
GELSLSNPDQ QVIGLAGNPT DTSQPYSQEG NKDLAFMDMK KLAQFLAGKP EHPMTRETLN
AENIAKYAFR IVP
