ID HOPD2_PSESM Reviewed; 468 AA.
AC Q79LY0; Q87W44;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=Effector protein hopD2;
DE EC=3.1.3.48;
DE AltName: Full=Tyrosine-protein phosphatase hopPtoD2;
GN Name=hopD2; Synonyms=hopA01, hopPtoD2; OrderedLocusNames=PSPTO_4722;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12437299; DOI=10.1094/mpmi.2002.15.10.1014;
RA Badel J.L., Charkowski A.O., Deng W.-L., Collmer A.;
RT "A gene in the Pseudomonas syringae pv. tomato Hrp pathogenicity island
RT conserved effector locus, hopPtoA1, contributes to efficient formation of
RT bacterial colonies in planta and is duplicated elsewhere in the genome.";
RL Mol. Plant Microbe Interact. 15:1014-1024(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RA Buell C.R., Berry K.J., Fedorova N.B., Feldblynm T.V., Gwinn M.L.,
RA Haft D.H., Khouri H.M., Nelson W.C., Peterson J., Russell D., Tran B.,
RA Umayam L., Utterback T.R., Van Aken S.E.;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A PHOSPHATASE, INDUCTION,
RP AND MUTAGENESIS OF CYS-378.
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12828636; DOI=10.1046/j.1365-2958.2003.03588.x;
RA Espinosa A., Guo M., Tam V.C., Fu Z.Q., Alfano J.R.;
RT "The Pseudomonas syringae type III-secreted protein HopPtoD2 possesses
RT protein tyrosine phosphatase activity and suppresses programmed cell death
RT in plants.";
RL Mol. Microbiol. 49:377-387(2003).
RN [4]
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 [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12032338; DOI=10.1073/pnas.112183899;
RA Petnicki-Ocwieja T., Schneider D.J., Tam V.C., Chancey S.T., Shan L.,
RA Jamir Y., Schechter L.M., Janes M.D., Buell C.R., Tang X., Collmer A.,
RA Alfano J.R.;
RT "Genomewide identification of proteins secreted by the Hrp type III protein
RT secretion system of Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7652-7657(2002).
RN [6]
RP FUNCTION AS A PHOSPHATASE, DOMAIN, AND INDUCTION.
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12828637; DOI=10.1046/j.1365-2958.2003.03616.x;
RA Bretz J.R., Mock N.M., Charity J.C., Zeyad S., Baker C.J., Hutcheson S.W.;
RT "A translocated protein tyrosine phosphatase of Pseudomonas syringae pv.
RT tomato DC3000 modulates plant defence response to infection.";
RL Mol. Microbiol. 49:389-400(2003).
RN [7]
RP FUNCTION, INTERACTION WITH EFR AND FLS2, AND MUTAGENESIS OF CYS-378.
RX PubMed=24357608; DOI=10.1002/embj.201284303;
RA Ross A., Yamada K., Hiruma K., Yamashita-Yamada M., Lu X., Takano Y.,
RA Tsuda K., Saijo Y.;
RT "The Arabidopsis PEPR pathway couples local and systemic plant immunity.";
RL EMBO J. 33:62-75(2014).
CC -!- FUNCTION: Effector showing tyrosine-phosphatase activity required for
CC host defense suppression. Functions inside plant cells causing
CC suppression of HR (hypersensitive response), PR1 gene expression and
CC oxidative burst probably by interfering with a MAPK (mitogen-activated
CC protein kinase) pathway. MAPK cascades are known to activate defense-
CC related transcription factors. Inhibits plant pattern-recognition
CC receptors (PRRs) activation. {ECO:0000269|PubMed:12828636,
CC ECO:0000269|PubMed:12828637, ECO:0000269|PubMed:24357608}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- ACTIVITY REGULATION: Inhibited by sodium orthovanadate.
CC -!- SUBUNIT: Interacts with EFR and FLS2 (via the kinase and cytoplasmic
CC domains). {ECO:0000269|PubMed:24357608}.
CC -!- INTERACTION:
CC Q79LY0; C0LGT6: EFR; Xeno; NbExp=3; IntAct=EBI-16096022, EBI-8801168;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12032338}.
CC Note=Secreted via type III secretion system (T3SS).
CC -!- INDUCTION: Transcriptionally induced by HrpL.
CC {ECO:0000269|PubMed:12828636, ECO:0000269|PubMed:12828637}.
CC -!- DOMAIN: The N-terminal domain (residues 1-142) retains 70% identity to
CC the N-terminal 142 residues of AvrPphD, and is required for
CC translocation into plant cells via T3SS. {ECO:0000269|PubMed:12828637}.
CC -!- MISCELLANEOUS: HopPtoD2 is not present in all strains of P.syringae.
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; AF469470; AAO33450.1; -; Genomic_DNA.
DR EMBL; AY198373; AAO43976.1; -; Genomic_DNA.
DR EMBL; AE016853; AAO58160.1; -; Genomic_DNA.
DR RefSeq; NP_794465.1; NC_004578.1.
DR RefSeq; WP_011105134.1; NC_004578.1.
DR AlphaFoldDB; Q79LY0; -.
DR SMR; Q79LY0; -.
DR DIP; DIP-61675N; -.
DR IntAct; Q79LY0; 2.
DR STRING; 223283.PSPTO_4722; -.
DR DNASU; 1186405; -.
DR GeneID; 83340040; -.
DR KEGG; pst:PSPTO_4722; -.
DR PATRIC; fig|223283.9.peg.4834; -.
DR eggNOG; COG5599; Bacteria.
DR HOGENOM; CLU_586436_0_0_6; -.
DR OrthoDB; 21920at2; -.
DR PHI-base; PHI:7237; -.
DR PHI-base; PHI:7265; -.
DR PHI-base; PHI:992; -.
DR Proteomes; UP000002515; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0034053; P:symbiont-mediated perturbation of host defense-related programmed cell death; IEA:UniProtKB-KW.
DR CDD; cd14495; PTPLP-like; 1.
DR Gene3D; 3.30.70.1690; -; 1.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR23339:SF98; CYCLIN-DEPENDENT KINASE INHIBITOR 3-RELATED; 1.
DR PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR Pfam; PF14566; PTPlike_phytase; 1.
DR SMART; SM01301; PTPlike_phytase; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Hypersensitive response elicitation; Phosphoprotein;
KW Protein phosphatase; Reference proteome; Secreted; Virulence.
FT CHAIN 1..468
FT /note="Effector protein hopD2"
FT /id="PRO_0000094863"
FT DOMAIN 143..468
FT /note="Tyrosine-protein phosphatase"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 378
FT /note="Phosphocysteine intermediate"
FT MUTAGEN 378
FT /note="C->S: Loss of phosphatase activity and decreased
FT inhibition of EFR phosphorylation."
FT /evidence="ECO:0000269|PubMed:12828636,
FT ECO:0000269|PubMed:24357608"
SQ SEQUENCE 468 AA; 51380 MW; 351D7B79664F9E81 CRC64;
MNPLQPIQHS ITNSQMSGGQ QLEAEGSQAH NSYSHPDRIS LSQLSQSAHL ALDHLSTQPN
TDHQRVASLV RNAVQDGKFQ LQSSNDTQVT YKTSVCPPAN ADTMGAAHLI NNELTVQARL
NDQLEYDIVS AHLYGPSEAI SIDASSPPSA NDLASSGLSE RTHLGMNRVL LRYAVPPRET
EDQCVMVIDK MPPPKHGKMS FFRTTNDLSK LPLGMETGGL SDLKLAGCER ISSVEQVKSI
RAALGGGPLT VLDLREESHA IVNGLPITLR GPMDWANAGL SQVDGAARES AMITELKRTK
SLTLVDANYV KGKKSNPQTT ELKNLNVRSE REVVTEAGAT YRRVAITDHN RPSPEATDEL
VDIMRHCLQA NESLVVHCNG GRGRTTTAMI MVDMLKNARN HSAETLITRM AKLSYDYNMT
DLGSISALKR PFLEDRLKFL QAFHDYARNN PSGLSLNWTQ WRAKIALE
//
