ASES_SARSR
ID ASES_SARSR Reviewed; 388 AA.
AC R4IR27;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2013, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Subtilisin-like serine protease AsES {ECO:0000303|PubMed:23530047};
DE EC=3.4.21.- {ECO:0000269|PubMed:23530047};
DE AltName: Full=Alkaline serine protease AsES {ECO:0000305};
DE AltName: Full=Extra-cellular elicitor protein AsES {ECO:0000303|PubMed:23530047};
DE Flags: Precursor;
GN Name=AsES {ECO:0000303|PubMed:23530047};
OS Sarocladium strictum (Black bundle disease fungus) (Acremonium strictum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Sarocladiaceae; Sarocladium.
OX NCBI_TaxID=5046;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 106-115; 202-226 AND
RP 360-379, SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RC STRAIN=SS71;
RX PubMed=23530047; DOI=10.1074/jbc.m112.429423;
RA Chalfoun N.R., Grellet-Bournonville C.F., Martinez-Zamora M.G.,
RA Diaz-Perales A., Castagnaro A.P., Diaz-Ricci J.C.;
RT "Purification and characterization of AsES protein: a subtilisin secreted
RT by Acremonium strictum is a novel plant defense elicitor.";
RL J. Biol. Chem. 288:14098-14113(2013).
RN [2]
RP FUNCTION.
RX PubMed=26562675; DOI=10.1016/j.plaphy.2015.10.029;
RA Martos G.G., Teran M.M., Diaz Ricci J.C.;
RT "The defence elicitor AsES causes a rapid and transient membrane
RT depolarization, a triphasic oxidative burst and the accumulation of nitric
RT oxide.";
RL Plant Physiol. Biochem. 97:443-450(2015).
RN [3]
RP FUNCTION.
RX PubMed=26706064; DOI=10.1016/j.plantsci.2015.09.025;
RA Hael-Conrad V., Abou-Mansour E., Diaz-Ricci J.C., Metraux J.P., Serrano M.;
RT "The novel elicitor AsES triggers a defense response against Botrytis
RT cinerea in Arabidopsis thaliana.";
RL Plant Sci. 241:120-127(2015).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=29946326; DOI=10.3389/fpls.2018.00763;
RA Chalfoun N.R., Durman S.B., Gonzalez-Montaner J., Reznikov S., De Lisi V.,
RA Gonzalez V., Moretti E.R., Devani M.R., Ploper L.D., Castagnaro A.P.,
RA Welin B.;
RT "Elicitor-Based biostimulant PSP1 protects soybean against late season
RT diseases in field trials.";
RL Front. Plant Sci. 9:763-763(2018).
RN [5]
RP BIOTECHNOLOGY.
RX PubMed=30087681; DOI=10.3389/fpls.2018.00844;
RA Chalfoun N.R., Durman S.B., Budeguer F., Caro M.D.P., Bertani R.P.,
RA Di Peto P., Stenglein S.A., Filippone M.P., Moretti E.R., Diaz Ricci J.C.,
RA Welin B., Castagnaro A.P.;
RT "Development of PSP1, a biostimulant based on the elicitor AsES for disease
RT management in monocot and dicot crops.";
RL Front. Plant Sci. 9:844-844(2018).
RN [6]
RP FUNCTION.
RX PubMed=28635519; DOI=10.1094/mpmi-05-17-0121-fi;
RA Hael-Conrad V., Perato S.M., Arias M.E., Martinez-Zamora M.G.,
RA Di Peto P.L.A., Martos G.G., Castagnaro A.P., Diaz-Ricci J.C.,
RA Chalfoun N.R.;
RT "The elicitor protein AsES induces a systemic acquired resistance response
RT accompanied by systemic microbursts and micro-hypersensitive responses in
RT Fragaria ananassa.";
RL Mol. Plant Microbe Interact. 31:46-60(2018).
CC -!- FUNCTION: Extracellular elicitor protein that induces a strong defense
CC response in strawberry and confers both local and systemic plant
CC resistance against the fungal pathogen Colletotricum acutatum, the
CC casual agent of anthracnose disease (PubMed:23530047). AsES activates a
CC cascade of defense responses, including calcium influx, oxidative
CC burst, hypersensitive cell-death response (HR), accumulation of
CC autofluorescent compounds, cell-wall reinforcement with callose and
CC lignin deposition, salicylic acid accumulation, and expression of
CC defense-related genes, such as PR1, PG1, MYB30, RBOH-D, RBOH-F, CHI23,
CC and FLS (PubMed:23530047, PubMed:26706064, PubMed:28635519). The
CC oxidative burst consists in a progressive extracellular accumulation of
CC H(2)O(2) that starts immediately after the contact with AsES and is
CC preceded by a rapid and transient cell membrane depolarization. During
CC this phase takes place also a rapid intracellular accumulation of NO at
CC the chloroplasts. After the first extracellular H(2)O(2) production
CC phase, two intracellular H(2)O(2) accumulation events occur, the first
CC 2 hours after induction, and the second 7 hours after induction. AsES
CC also produces a transient increase of ion leakage, and a progressive
CC alkalinization of the extracellular medium (PubMed:26562675). Confers
CC also local and systemic plant resistance against Botrytis cinerea in
CC Arabidopsis thaliana. Systemic, but not local resistance is dependent
CC on the length of exposure to AsES. The protection to B.cinerea is due
CC to the induction of the plant defenses via the salicylic acid, jasmonic
CC acid and ethylene signaling pathways (PubMed:26706064). Exhibits
CC subtilisin-like proteolytic activity which is necessary but not
CC sufficient for its elicitor function in strawberry plants. Probably
CC induces defense by means of proteolysis of one or multiple host
CC proteins that are specific targets of this protease (PubMed:23530047).
CC {ECO:0000269|PubMed:23530047, ECO:0000269|PubMed:26562675,
CC ECO:0000269|PubMed:26706064, ECO:0000269|PubMed:28635519}.
CC -!- ACTIVITY REGULATION: The elicitor proteolytic activity is completely
CC inhibited by PMSF. The activity is also significantly reduced by
CC aprotinin (leading to 37% residual activity), by leupeptin (leading to
CC 54% residual activity), by the ovomucoid trypsin inhibitor (leading to
CC 65% residual activity), and by p-aminobenzamidine (leading to 26%
CC residual activity). {ECO:0000269|PubMed:23530047}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:23530047}.
CC -!- BIOTECHNOLOGY: AsES can be combined well with commercial spray
CC adjuvants, insecticides, herbicides and fungicides without losing any
CC defense-inducing activity. The agricultural biostimulant PSP1, a
CC formulation based on AsES is therefore a very promising candidate to
CC efficiently control multiple fungal diseases under field conditions in
CC monocot and dicot crops. {ECO:0000269|PubMed:29946326,
CC ECO:0000269|PubMed:30087681}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; JX684014; AFZ84667.2; -; mRNA.
DR AlphaFoldDB; R4IR27; -.
DR SMR; R4IR27; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Protease; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT PROPEP 16..105
FT /note="Removed in mature form"
FT /evidence="ECO:0000305|PubMed:23530047"
FT /id="PRO_0000447370"
FT CHAIN 106..388
FT /note="Subtilisin-like serine protease AsES"
FT /id="PRO_5013379825"
FT DOMAIN 114..388
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 146
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 176
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 331
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT SITE 268
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q5JIZ5"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 141..230
FT /evidence="ECO:0000305|PubMed:23530047"
FT DISULFID 285..357
FT /evidence="ECO:0000305|PubMed:23530047"
SQ SEQUENCE 388 AA; 39721 MW; DE9EC39A83634372 CRC64;
MRLSLVLALL PVAFGAPTRR DEPAPLHVPR DVDSLIKDTY IVKYKDITAF SAVDEGLKLL
SGKPKHIYKG AFKGFSGKID AKTLELLRDD PSVDFIEQDA IVTLAAYTTQ ASAPWGLARI
STRQRGPTGY TYDDSAGAGT CSYIIDTGIQ ANHPNFGGRA FQLVSYQGSN ADGNGHGTHV
AGTIGSTTYG VAKRTTLLGV KVLSDSGSGS TSGIIAGINY VVSDSRSRSC PNGSVANMSL
GGGYSASLNS AAKSLIDNNI FLAVAAGNEN QNAANVSPAS EPTVCTVGAT TSADAKASFS
NYGSGVDIFA PGQSILSTWI GSSTNTISGT SMASPHIAGL AAYLAGLEGF PGAQALCNRI
VALATTGVIT GLPSGTPNRL AFNGNPSG
