AVRP3_PSESH
ID AVRP3_PSESH Reviewed; 267 AA.
AC Q52430;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Cysteine protease avirulence protein AvrPphB;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=7 kDa product;
DE Contains:
DE RecName: Full=28 kDa product;
GN Name=avrPph3;
OS Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv.
OS phaseolicola).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=319;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1301A / Race 3, and 1302A / Race 4;
RX PubMed=1666524;
RA Jenner C., Hitchin E., Mansfield J., Walters K., Betteridge P.,
RA Teverson D., Taylor J.;
RT "Gene-for-gene interactions between Pseudomonas syringae pv. phaseolicola
RT and Phaseolus.";
RL Mol. Plant Microbe Interact. 4:553-562(1991).
RN [2]
RP AUTOCATALYTIC CLEAVAGE.
RX PubMed=9057331; DOI=10.1094/mpmi.1997.10.2.247;
RA Puri N., Jenner C., Bennett M., Stewart R., Mansfield J., Lyons N.,
RA Taylor J.;
RT "Expression of avrPphB, an avirulence gene from Pseudomonas syringae pv.
RT phaseolicola, and the delivery of signals causing the hypersensitive
RT reaction in bean.";
RL Mol. Plant Microbe Interact. 10:247-256(1997).
RN [3]
RP SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-63, AND MUTAGENESIS OF GLY-63.
RX PubMed=10830163; DOI=10.1016/s0092-8674(00)80846-6;
RA Nimchuk Z., Marois E., Kjemtrup S., Leister R.T., Katagiri F., Dangl J.L.;
RT "Eukaryotic fatty acylation drives plasma membrane targeting and enhances
RT function of several type III effector proteins from Pseudomonas syringae.";
RL Cell 101:353-363(2000).
RN [4]
RP FUNCTION OF THE 7 KDA CLEAVAGE PRODUCT.
RX PubMed=11952132; DOI=10.1094/mpmi.2002.15.3.292;
RA Tampakaki A.P., Bastaki M., Mansfield J.W., Panopoulos N.J.;
RT "Molecular determinants required for the avirulence function of AvrPphB in
RT bean and other plants.";
RL Mol. Plant Microbe Interact. 15:292-300(2002).
RN [5]
RP AUTOCATALYTIC CLEAVAGE, AND MUTAGENESIS OF CYS-98; GLN-128; HIS-212 AND
RP ASP-227.
RX PubMed=12062101; DOI=10.1016/s0092-8674(02)00766-3;
RA Shao F., Merritt P.M., Bao Z., Innes R.W., Dixon J.E.;
RT "A Yersinia effector and a Pseudomonas avirulence protein define a family
RT of cysteine proteases functioning in bacterial pathogenesis.";
RL Cell 109:575-588(2002).
RN [6]
RP INTERACTION WITH PBS1, AND CLEAVAGE OF PBS1.
RX PubMed=12947197; DOI=10.1126/science.1085671;
RA Shao F., Golstein C., Ade J., Stoutemyer M., Dixon J.E., Innes R.W.;
RT "Cleavage of Arabidopsis PBS1 by a bacterial type III effector.";
RL Science 301:1230-1233(2003).
RN [7]
RP FUNCTION.
RX PubMed=17277084; DOI=10.1073/pnas.0608779104;
RA Ade J., DeYoung B.J., Golstein C., Innes R.W.;
RT "Indirect activation of a plant nucleotide binding site-leucine-rich repeat
RT protein by a bacterial protease.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2531-2536(2007).
RN [8]
RP FUNCTION.
RX PubMed=20413097; DOI=10.1016/j.chom.2010.03.007;
RA Zhang J., Li W., Xiang T., Liu Z., Laluk K., Ding X., Zou Y., Gao M.,
RA Zhang X., Chen S., Mengiste T., Zhang Y., Zhou J.M.;
RT "Receptor-like cytoplasmic kinases integrate signaling from multiple plant
RT immune receptors and are targeted by a Pseudomonas syringae effector.";
RL Cell Host Microbe 7:290-301(2010).
RN [9]
RP FUNCTION.
RX PubMed=25625821; DOI=10.1094/mpmi-08-14-0248-r;
RA Russell A.R., Ashfield T., Innes R.W.;
RT "Pseudomonas syringae effector AvrPphB suppresses AvrB-induced activation
RT of RPM1 but not AvrRpm1-induced activation.";
RL Mol. Plant Microbe Interact. 28:727-735(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 81-268.
RX PubMed=14694194; DOI=10.1073/pnas.2036536100;
RA Zhu M., Shao F., Innes R.W., Dixon J.E., Xu Z.;
RT "The crystal structure of Pseudomonas avirulence protein AvrPphB: a papain-
RT like fold with a distinct substrate-binding site.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:302-307(2004).
CC -!- FUNCTION: Cysteine protease avirulence protein, which is essential
CC during infection of plant cells from cultivar-specific of beans and
CC Arabidopsis thaliana. The autocleavage of the protein is required for
CC virulence function. May act by affecting the plant defense system. In
CC plants lacking R3 or RPS5 resistance genes, it probably impairs the
CC plant defense system and leads to the bacteria multiplication. In
CC contrast, in plants containing the R3 or RPS5 protein, it is unable to
CC induce disease symptoms, explaining its avirulence name. The 7 kDa
CC product is required for the type-III translocation from Pseudomonas
CC strains to the plant, but are partially dispensable for effector
CC recognition following in planta expression. In infected plants, it acts
CC by cleaving the PBS1 protein, which leads to resistance or disease,
CC depending on the presence or absence of RPS5, respectively
CC (PubMed:11952132, PubMed:17277084). Targets the Arabidopsis kinases
CC PBS1, BIK1, PBL1, PBL2, PBL3, PBL5, PBL7, PBL9 and PBL11 for cleavage
CC in vitro (PubMed:20413097). Can block recognition of AvrB avirulence
CC factor by plant cells by cleaving Arabidopsis RIPK kinase and
CC suppressing Arabidopsis RPM1 activation. Cannot block AvrRpm1-induced
CC activation of RPM1 (PubMed:25625821). {ECO:0000269|PubMed:11952132,
CC ECO:0000269|PubMed:17277084, ECO:0000269|PubMed:20413097,
CC ECO:0000269|PubMed:25625821}.
CC -!- SUBUNIT: In infected plant cells, the 28 kDa product interacts with
CC PBS1. {ECO:0000269|PubMed:12947197}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10830163}. Host
CC membrane {ECO:0000269|PubMed:10830163}. Note=In infected plant cells,
CC it is membrane-associated.
CC -!- PTM: Autocleaved. This function is essential for myristoylation in
CC infected plant cell and for eliciting the plant hypersensitive
CC response. {ECO:0000269|PubMed:10830163}.
CC -!- PTM: Myristoylation of 28 kDa product in infected plant cells; it
CC mediates the localization to membranes. {ECO:0000305|PubMed:10830163}.
CC -!- SIMILARITY: Belongs to the peptidase C58 family. {ECO:0000305}.
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DR EMBL; M86401; AAA25727.1; -; Genomic_DNA.
DR PIR; S28670; S28670.
DR PDB; 1UKF; X-ray; 1.35 A; A=81-267.
DR PDBsum; 1UKF; -.
DR AlphaFoldDB; Q52430; -.
DR SMR; Q52430; -.
DR DIP; DIP-60863N; -.
DR IntAct; Q52430; 1.
DR MEROPS; C58.002; -.
DR iPTMnet; Q52430; -.
DR KEGG; ag:AAA25727; -.
DR EvolutionaryTrace; Q52430; -.
DR PHI-base; PHI:993; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0034053; P:modulation by symbiont of host defense-related programmed cell death; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006473; Peptidase_C58_Yopt.
DR Pfam; PF03543; Peptidase_C58; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR TIGRFAMs; TIGR01586; yopT_cys_prot; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Host membrane; Hydrolase;
KW Hypersensitive response elicitation; Lipoprotein; Membrane; Myristate;
KW Protease; Secreted; Thiol protease; Virulence.
FT CHAIN 1..62
FT /note="7 kDa product"
FT /id="PRO_0000026577"
FT CHAIN 63..267
FT /note="28 kDa product"
FT /id="PRO_0000026578"
FT ACT_SITE 98
FT ACT_SITE 212
FT ACT_SITE 227
FT SITE 62..63
FT /note="Cleavage; by autolysis"
FT LIPID 63
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000305|PubMed:10830163"
FT MUTAGEN 63
FT /note="G->A: Abolishes the localization to plasma membrane
FT in host cells."
FT /evidence="ECO:0000269|PubMed:10830163"
FT MUTAGEN 98
FT /note="C->S: Prevents auto-cleavage and hypersensitive
FT response in infected plants."
FT /evidence="ECO:0000269|PubMed:12062101"
FT MUTAGEN 128
FT /note="Q->A: No effect."
FT /evidence="ECO:0000269|PubMed:12062101"
FT MUTAGEN 212
FT /note="H->A: Prevents auto-cleavage and hypersensitive
FT response in infected plants."
FT /evidence="ECO:0000269|PubMed:12062101"
FT MUTAGEN 227
FT /note="D->A: Prevents auto-cleavage and hypersensitive
FT response in infected plants."
FT /evidence="ECO:0000269|PubMed:12062101"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:1UKF"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:1UKF"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:1UKF"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:1UKF"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:1UKF"
FT HELIX 126..147
FT /evidence="ECO:0007829|PDB:1UKF"
FT HELIX 153..164
FT /evidence="ECO:0007829|PDB:1UKF"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:1UKF"
FT HELIX 182..193
FT /evidence="ECO:0007829|PDB:1UKF"
FT STRAND 199..206
FT /evidence="ECO:0007829|PDB:1UKF"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1UKF"
FT STRAND 210..219
FT /evidence="ECO:0007829|PDB:1UKF"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:1UKF"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1UKF"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:1UKF"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:1UKF"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:1UKF"
FT STRAND 258..267
FT /evidence="ECO:0007829|PDB:1UKF"
SQ SEQUENCE 267 AA; 28704 MW; A503220A905C60A8 CRC64;
MKIGTQATSL AVLHNQESHA PQAPIAVRPE PAHAIPEIPL DLAIRPRTRG IHPFLAMTLG
DKGCASSSGV SLEDDSHTQV SLSDFSVASR DVNHNNICAG LSTEWLVMSS DGDAESRMDH
LDYNGEGQSR GSERHQVYND ALRAALSNDD EAPFFTASTA VIEDAGFSLR REPKTVHASG
GSAQLGQTVA HDVAQSGRKH LLSLRFANVQ GHAIACSCEG SQFKLFDPNL GEFQSSRSAA
PQLIKGLIDH YNSLNYDVAC VNEFRVS
