XEG1_PHYSP
ID XEG1_PHYSP Reviewed; 241 AA.
AC G4ZHR2;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Xyloglucan-specific endo-beta-1,4-glucanase 1 {ECO:0000303|PubMed:26163574};
DE EC=3.2.1.151 {ECO:0000269|PubMed:26163574};
DE AltName: Full=Glycoside hydrolase family 12 protein XEG1 {ECO:0000303|PubMed:26163574};
DE Short=GH12 protein XEG1 {ECO:0000303|PubMed:26163574};
DE Flags: Precursor;
GN Name=XEG1 {ECO:0000303|PubMed:26163574}; ORFNames=PHYSODRAFT_559651;
OS Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS (Phytophthora megasperma f. sp. glycines).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1094619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6497;
RX PubMed=16946064; DOI=10.1126/science.1128796;
RA Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H.Y., Aerts A.,
RA Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA Damasceno C.M.B., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.-K.,
RA McDonald W.H., Medina M., Meijer H.J.G., Nordberg E.K., Maclean D.J.,
RA Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA Rose J.K.C., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA Smith B.M., Sobral B.W.S., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT of pathogenesis.";
RL Science 313:1261-1266(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INDUCTION, DISRUPTION
RP PHENOTYPE, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, ACTIVE SITE, AND
RP MUTAGENESIS OF GLU-136 AND GLU-222.
RX PubMed=26163574; DOI=10.1105/tpc.15.00390;
RA Ma Z., Song T., Zhu L., Ye W., Wang Y., Shao Y., Dong S., Zhang Z., Dou D.,
RA Zheng X., Tyler B.M., Wang Y.;
RT "A Phytophthora sojae glycoside hydrolase 12 protein is a major virulence
RT factor during soybean infection and is recognized as a PAMP.";
RL Plant Cell 27:2057-2072(2015).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HOST GIP1, MUTAGENESIS OF
RP GLU-136 AND GLU-222, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=28082413; DOI=10.1126/science.aai7919;
RA Ma Z., Zhu L., Song T., Wang Y., Zhang Q., Xia Y., Qiu M., Lin Y., Li H.,
RA Kong L., Fang Y., Ye W., Wang Y., Dong S., Zheng X., Tyler B.M., Wang Y.;
RT "A paralogous decoy protects Phytophthora sojae apoplastic effector PsXEG1
RT from a host inhibitor.";
RL Science 355:710-714(2017).
CC -!- FUNCTION: Glycoside hydrolase that exhibits xyloglucanase activity
CC (PubMed:26163574). Acts as an important virulence factor during P.sojae
CC infection but also acts as a pathogen-associated molecular pattern
CC (PAMP) in soybean and solanaceous species, where it can trigger defense
CC responses including cell death. XEG1-induced cell death can be
CC suppressed by P.sojae RxLR effectors. The PAMP activity is independent
CC of its xyloglucanase activity (PubMed:26163574). XEG1 induces plant
CC defense responses in a RLP kinase Serk3/Bak1-dependent manner in
CC Nicotiana benthamiana. Moreover, the perception of XEG1 occurs
CC independently of the perception of ethylene-inducing xylanase Eix2 in
CC Tomato (PubMed:26163574). With truncated paralog XLP1, is required to
CC elevate apoplastic sugar during P.sojae infection (PubMed:28082413).
CC {ECO:0000269|PubMed:26163574, ECO:0000269|PubMed:28082413}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=xyloglucan + H2O = xyloglucan oligosaccharides.; EC=3.2.1.151;
CC Evidence={ECO:0000269|PubMed:26163574};
CC -!- ACTIVITY REGULATION: The xyloglucanase activity is inhibited by the
CC binding of the host apoplastic glucanase inhibitor GIP1.
CC {ECO:0000269|PubMed:28082413}.
CC -!- SUBUNIT: Interacts with host apoplastic glucanase inhibitor GIP1.
CC {ECO:0000269|PubMed:28082413}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26163574,
CC ECO:0000269|PubMed:28082413}. Host {ECO:0000269|PubMed:26163574}.
CC Note=Targeted to the host apoplast in order to trigger cell death.
CC {ECO:0000269|PubMed:26163574}.
CC -!- INDUCTION: Expression is strongly induced within 30 min of infection of
CC soybean and then slowly declines. {ECO:0000269|PubMed:26163574}.
CC -!- DISRUPTION PHENOTYPE: Severely reduces virulence.
CC {ECO:0000269|PubMed:26163574}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) family.
CC {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; JH159154; EGZ16757.1; -; Genomic_DNA.
DR RefSeq; XP_009525815.1; XM_009527520.1.
DR AlphaFoldDB; G4ZHR2; -.
DR SMR; G4ZHR2; -.
DR EnsemblProtists; EGZ16757; EGZ16757; PHYSODRAFT_559651.
DR GeneID; 20663425; -.
DR KEGG; psoj:PHYSODRAFT_559651; -.
DR InParanoid; G4ZHR2; -.
DR OMA; KSLPSVW; -.
DR PHI-base; PHI:6868; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0018995; C:host cellular component; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:0033946; F:xyloglucan-specific endo-beta-1,4-glucanase activity; IEA:UniProtKB-EC.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.180; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR013319; GH11/12.
DR InterPro; IPR002594; GH12.
DR PANTHER; PTHR34002; PTHR34002; 1.
DR Pfam; PF01670; Glyco_hydro_12; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:26163574"
FT CHAIN 20..241
FT /note="Xyloglucan-specific endo-beta-1,4-glucanase 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5003472095"
FT ACT_SITE 136
FT /evidence="ECO:0000305|PubMed:26163574"
FT ACT_SITE 222
FT /evidence="ECO:0000305|PubMed:26163574"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 136
FT /note="E->D: Abolishes xyloglucan-degrading endoglucanase
FT activity, but does not affect elicitor activity."
FT /evidence="ECO:0000269|PubMed:26163574,
FT ECO:0000269|PubMed:28082413"
FT MUTAGEN 222
FT /note="E->D: Abolishes xyloglucan-degrading endoglucanase
FT activity, but does not affect elicitor activity."
FT /evidence="ECO:0000269|PubMed:26163574,
FT ECO:0000269|PubMed:28082413"
SQ SEQUENCE 241 AA; 25500 MW; 2356A68E942DC665 CRC64;
MKGFFAGVVA AATLAVASAG DYCGQWDWAK STNYIVYNNL WNKNAAASGS QCTGVDKISG
STIAWHTSYT WTGGAATEVK SYSNAALVFS KKQIKNIKSI PTKMKYSYSH SSGTFVADVS
YDLFTSSTAS GSNEYEIMIW LAAYGGAGPI SSTGKAIATV TIGSNSFKLY KGPNGSTTVF
SFVATKTITN FSADLQKFLS YLTKNQGLPS SQYLITLEAG TEPFVGTNAK MTVSSFSAAV
N
