ID   HPAB3_PSEUB             Reviewed;         579 AA.
AC   Q2QCI9; Q2QCJ1;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Effector protein HopAB3;
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=hopAB3; Synonyms=avrPtoB;
OS   Pseudomonas syringae pv. tomato.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN VIRULENCE AND
RP   AVIRULENCE.
RC   STRAIN=JL1065, PT23, and T1;
RX   PubMed=16391110; DOI=10.1128/aem.72.1.702-712.2006;
RA   Lin N.-C., Abramovitch R.B., Kim Y.-J., Martin G.B.;
RT   "Diverse AvrPtoB homologs from several Pseudomonas syringae pathovars
RT   elicit Pto-dependent resistance and have similar virulence activities.";
RL   Appl. Environ. Microbiol. 72:702-712(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 (By similarity). Enhances the development of disease
CC       symptoms and bacterial growth. {ECO:0000250,
CC       ECO:0000269|PubMed:16391110}.
CC   -!- SUBUNIT: Interacts physically with plant cell Pto.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted via type III secretion
CC       system (TTSS). Localized to the plant cell cytoplasm.
CC   -!- PTM: Auto-ubiquitinated. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the HopAB family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ133535; ABA00713.1; -; Genomic_DNA.
DR   EMBL; DQ133534; ABA00712.1; -; Genomic_DNA.
DR   EMBL; DQ133533; ABA00711.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2QCI9; -.
DR   SMR; Q2QCI9; -.
DR   PRIDE; Q2QCI9; -.
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   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   Hypersensitive response elicitation; Secreted; Transferase;
KW   Ubl conjugation; Ubl conjugation pathway; Virulence.
FT   CHAIN           1..579
FT                   /note="Effector protein HopAB3"
FT                   /id="PRO_0000234082"
FT   REGION          1..336
FT                   /note="Host recognition; Pto interaction"
FT                   /evidence="ECO:0000250"
FT   REGION          1..140
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..579
FT                   /note="E3 ubiquitin-protein ligase"
FT                   /evidence="ECO:0000250"
FT   REGION          384..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..294
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         35
FT                   /note="S -> R (in strain: T1)"
FT   VARIANT         493
FT                   /note="L -> A (in strain: T1)"
FT   VARIANT         515
FT                   /note="V -> D (in strain: T1)"
SQ   SEQUENCE   579 AA;  61819 MW;  1C72306CAD386A7D CRC64;
     MAGINGAGPS GAYFVGHTDP EPASGGAHGS SSGASSSNSP RLPAPPDAPA SQARDRREML
     LRARPLSRQT REWVAQGMPP TAEAGVPIRP QESAEAAAPQ ARAEERHTPE ADAAASHVRT
     EGGRTPQALA GTSPRHTGAV PHANRIVQQL VDAGADLAGI NTMIDNAMRR HAIALPSRTV
     QSILIEHFPH LLAGELISGS ELATAFRAAL RREVRQQEAS APPRTAARSS VRTPERSTVP
     PTSTESSSGS NQRTLLGRFA GLMTPNQRRP SSASNASASQ RPVDRSPPRV NQVPTGANRV
     VMRNHGNNEA DAALQGLAQQ GVDMEDLRAA LERHILHRRP IPMDIAYALQ GVGIAPSIDT
     GESLMENPLM NLSVALHRAL GPRPARAQAP RPAVPVAPAT VSRRPDSARA TRLQVIPARE
     DYENNVAYGV RLLSLNPGAG VRETVAAFVN NRYERQAVVA DIRAALNLSK QFNKLRTVSK
     ADAASNKPGF KDLADHPDDA TQCLFGEELS LTSSVQQVIG LAGKATDMSE SYSREANKDL
     VFMDMKKLAQ FLAGKPEHPM TRETLNAENI AKYAFRIVP