XLP1_PHYSP
ID XLP1_PHYSP Reviewed; 189 AA.
AC G4ZHR3;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Inactive glycoside hydrolase XLP1;
DE AltName: Full=Glycoside hydrolase family 12 protein XLP1 {ECO:0000303|PubMed:16946064};
DE Short=GH12 protein XLP1 {ECO:0000303|PubMed:28082413};
DE AltName: Full=XEG1-like protein 1 {ECO:0000303|PubMed:28082413};
DE Flags: Precursor;
GN Name=XLP1 {ECO:0000303|PubMed:28082413}; ORFNames=PHYSODRAFT_360375;
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 FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH HOST
RP GIP1, DOMAIN, AND MUTAGENESIS OF TRP-26; 39-ASN--ASN-44; 77-THR-GLU-78;
RP GLU-136 AND 146-GLY--ILE-150.
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: Secreted XEG1-like protein that has lost enzyme activity but
CC binds to host soybean apoplastic glucanase inhibitor protein GIP1 more
CC tightly than does XEG1, thus it outcompetes XEG1 for GIP1 binding and
CC frees functional XEG1 to support P.sojae infection (PubMed:28082413).
CC With XEG1, is required to elevate apoplastic sugar during P.sojae
CC infection (PubMed:28082413). {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:28082413}.
CC -!- DOMAIN: Conserved residues in regions X1 (position 26), X2 (positions
CC 39 to 44), X3 (positions 77 and 78), and X5 (positions 146 to 150) are
CC all required for full binding activity of XLP1 to host soybean GIP1.
CC {ECO:0000269|PubMed:28082413}.
CC -!- DISRUPTION PHENOTYPE: Leads to strongly decreased virulence.
CC {ECO:0000269|PubMed:28082413}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 12 (cellulase H) family.
CC {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Glu residue in position 222 essential
CC activity and has thereforelost enzyme activity.
CC {ECO:0000269|PubMed:28082413}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Lure - Issue 218 of October
CC 2019;
CC URL="https://web.expasy.org/spotlight/back_issues/218/";
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DR EMBL; JH159154; EGZ16758.1; -; Genomic_DNA.
DR RefSeq; XP_009525816.1; XM_009527521.1.
DR AlphaFoldDB; G4ZHR3; -.
DR SMR; G4ZHR3; -.
DR EnsemblProtists; EGZ16758; EGZ16758; PHYSODRAFT_360375.
DR GeneID; 20650108; -.
DR KEGG; psoj:PHYSODRAFT_360375; -.
DR InParanoid; G4ZHR3; -.
DR OMA; WAGGNIH; -.
DR PHI-base; PHI:6869; -.
DR Proteomes; UP000002640; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008810; F:cellulase activity; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
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 Glycoprotein; Reference proteome; Secreted; Signal; Virulence.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..189
FT /note="Inactive glycoside hydrolase XLP1"
FT /id="PRO_5003472208"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 26
FT /note="W->A: In X1; affects the binding to host GIP1."
FT /evidence="ECO:0000269|PubMed:28082413"
FT MUTAGEN 39..44
FT /note="NLWNKN->ALAAAA: In X2; affects the binding to host
FT GIP1."
FT /evidence="ECO:0000269|PubMed:28082413"
FT MUTAGEN 77..78
FT /note="TE->AA: In X3; affects the binding to host GIP1."
FT /evidence="ECO:0000269|PubMed:28082413"
FT MUTAGEN 136
FT /note="E->A: Does not affect the binding to host GIP1."
FT /evidence="ECO:0000269|PubMed:28082413"
FT MUTAGEN 146..150
FT /note="GAGPI->AAAAA: In X5; affects the binding to host
FT GIP1."
FT /evidence="ECO:0000269|PubMed:28082413"
SQ SEQUENCE 189 AA; 20077 MW; D555879EF9A45361 CRC64;
MKSFLQLVVV VAALLSVSTA DFCSQWRLSK AGKYVIYNNL WNKNAAASGS QCTGVDKISG
STIAWHTSYT WTGGAATEVK SYSNAALVFS KKQIKNIKSI PTKMKYSYSH SSGTFVADVS
YDLFTSSTAS GSNEYEIMIW LAAYGGAGPI SSTGKAIATV TIGSNSFKLY KGPNGSTTVY
QPPGLPLST
