ID   XEG1_PHYPN              Reviewed;         241 AA.
AC   W2PEP3;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Xyloglucan-specific endo-beta-1,4-glucanase 1 {ECO:0000303|PubMed:28082413};
DE            EC=3.2.1.151 {ECO:0000305|PubMed:28082413};
DE   AltName: Full=Glycoside hydrolase family 12 protein XEG1 {ECO:0000303|PubMed:28082413};
DE            Short=GH12 protein XEG1 {ECO:0000303|PubMed:28082413};
DE   Flags: Precursor;
GN   Name=XEG1 {ECO:0000303|PubMed:28082413}; ORFNames=PPTG_19377;
OS   Phytophthora parasitica (strain INRA-310).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=761204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310;
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310;
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HOST GIP2, 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 (By
CC       similarity). Acts as an important virulence factor during P.parasitica
CC       infection of its host Nicotiana benthamiana (PubMed:28082413). Also
CC       acts as a pathogen-associated molecular pattern (PAMP) in host species,
CC       where it can trigger defense responses including cell death. The PAMP
CC       activity is independent of its xyloglucanase activity (By similarity).
CC       With paralog XLP1, is required to elevate apoplastic sugar during
CC       P.parasitica infection (PubMed:28082413).
CC       {ECO:0000250|UniProtKB:G4ZHR2, ECO:0000269|PubMed:28082413}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=xyloglucan + H2O = xyloglucan oligosaccharides.; EC=3.2.1.151;
CC         Evidence={ECO:0000305|PubMed:28082413};
CC   -!- ACTIVITY REGULATION: The xyloglucanase activity is inhibited by the
CC       binding of the host apoplastic glucanase inhibitor GIP2.
CC       {ECO:0000269|PubMed:28082413}.
CC   -!- SUBUNIT: Interacts with host apoplastic glucanase inhibitor GIP2.
CC       {ECO:0000269|PubMed:28082413}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) family.
CC       {ECO:0000305}.
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DR   EMBL; KI669674; ETM98683.1; -; Genomic_DNA.
DR   RefSeq; XP_008916024.1; XM_008917776.1.
DR   AlphaFoldDB; W2PEP3; -.
DR   SMR; W2PEP3; -.
DR   EnsemblProtists; ETM98683; ETM98683; PPTG_19377.
DR   GeneID; 20188152; -.
DR   VEuPathDB; FungiDB:PPTG_19377; -.
DR   OMA; KSLPSVW; -.
DR   Proteomes; UP000018817; Unassembled WGS sequence.
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; Signal; Virulence.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..241
FT                   /note="Xyloglucan-specific endo-beta-1,4-glucanase 1"
FT                   /id="PRO_5004821512"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000250|UniProtKB:G4ZHR2"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000250|UniProtKB:G4ZHR2"
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: Impairs elevated levels of reducing sugars in
FT                   the host apoplast; when associated wit D-222."
FT                   /evidence="ECO:0000269|PubMed:28082413"
FT   MUTAGEN         222
FT                   /note="E->D: Impairs elevated levels of reducing sugars in
FT                   the host apoplast; when associated wit D-136."
FT                   /evidence="ECO:0000269|PubMed:28082413"
SQ   SEQUENCE   241 AA;  25537 MW;  961EC623B070A318 CRC64;
     MKGLLAGTIA AATFAVASAG EYCGQWDWAK STQYTVYNNL WNKNAAASGS QCTGVDKISG
     STIGWHTSYT WTGGAATEVK SYSNAALIFS PKQIKNIKTI PTKMKYSYSH SSGTFVADVS
     YDLFTSSTAT GKNEYEIMIW LAAYGGAGPI SSTGKAIATV TIGSNSFKLY KGPNGSTTVF
     SFVATKTITN FTADLQKFLT YLVNSQGLPS SQYLITLEAG TEPFVGTNAK MTVSSYSAAV
     N