SBT_PETHY
ID SBT_PETHY Reviewed; 734 AA.
AC A0A0M3R8G2;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-DEC-2015, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Subtilisin-like protease {ECO:0000303|PubMed:25971550};
DE Short=Subtilase {ECO:0000303|PubMed:25971550};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10080};
DE Flags: Precursor;
GN Name=SBT {ECO:0000303|PubMed:25971550};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION BY RAM1 AND RHIZOPHAGUS
RP IRREGULARIS.
RC STRAIN=cv. W138;
RX PubMed=25971550; DOI=10.1104/pp.15.00310;
RA Rich M.K., Schorderet M., Bapaume L., Falquet L., Morel P.,
RA Vandenbussche M., Reinhardt D.;
RT "The Petunia GRAS transcription factor ATA/RAM1 regulates symbiotic gene
RT expression and fungal morphogenesis in arbuscular mycorrhiza.";
RL Plant Physiol. 168:788-797(2015).
CC -!- FUNCTION: Required for arbuscular mycorrhiza (AM) development during AM
CC symbiosis with AM fungi (e.g. Glomeromycota intraradices).
CC {ECO:0000250|UniProtKB:A9QY40}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250|UniProtKB:A9QY40}. Note=Accumulates in the intercellular
CC spaces and the periarbuscular space (PAS) during arbuscular mycorrhizal
CC (AM) symbiosis. {ECO:0000250|UniProtKB:A9QY40}.
CC -!- INDUCTION: Regulated by RAM1 during arbuscular mycorrhiza (AM)
CC formation after inoculation with Rhizophagus irregularis.
CC {ECO:0000269|PubMed:25971550}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; KR612269; ALC79559.1; -; mRNA.
DR AlphaFoldDB; A0A0M3R8G2; -.
DR SMR; A0A0M3R8G2; -.
DR GO; GO:0048046; C:apoplast; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0009610; P:response to symbiotic fungus; IEP:UniProtKB.
DR CDD; cd04852; Peptidases_S8_3; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034197; Peptidases_S8_3.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR InterPro; IPR045051; SBT.
DR InterPro; IPR041469; Subtilisin-like_FN3.
DR PANTHER; PTHR10795; PTHR10795; 1.
DR Pfam; PF17766; fn3_6; 1.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF02225; PA; 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.
PE 2: Evidence at transcript level;
KW Apoplast; Glycoprotein; Hydrolase; Protease; Secreted; Serine protease;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..734
FT /note="Subtilisin-like protease"
FT /id="PRO_5005788367"
FT DOMAIN 28..109
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 114..591
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 357..442
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 141
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240,
FT ECO:0000255|PROSITE-ProRule:PRU10080"
FT ACT_SITE 199
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 524
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 509
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 734 AA; 77596 MW; 90CEBBC1BDED5BFD CRC64;
MTCICIFSIA FLLSFHLTTA QRSTGLQTYI VHVDKPDAQV LANSADLESY YNSFLPATVS
GSEVPSRIIH SYHHVATGFA AKLSGEEVKE MEKKAGFVSA KLEKVLTLHT THTPNFLGLY
QNMGFWQESN YGKGVIIGLL DTGITPGHPS FSDVNMPSPP AKWKGKCEFT GNATCNKKII
GARNFISGSG VPPTDEEGHG THTASTAAGN FVNDANVFGN ANGTAVGMAP LAHIAMYKVC
SEDGCSDADI LAALDAAIDD GVDVLSLSLG GYSDPFYYDN IAIGAFAAIR KGIFVSASAG
NDGPLNSTLS NEAPWILTVG ASTHDRKIVA TAVLGNGQQY DGESAFQPAD FPHTLLPLVY
PGTSDEEAAF CSSGSLDKFD VKGKVVVCDR GGDVARLEKS QTVKDAGGAA MILANLEIDG
EGTFADAHVL PATHVGYAAG EMIKSYINST STPTAGILFK GTIIGFKSSP SVSSFSSRGP
NLASPGIVKP DIIGPGVNIL AAWPVSVENK TGTDLTFNII SGTSMSCPHL SGIVALLKSA
HPDWSPAAIK SAIMTSADQS NLEGQPILDE RNLPADIFAT GAGHVNPSKA SDPGLIYDIQ
LEDYIQYLCG LGYREKDIGL IVQETVKCES SISEAELNYP SFSIILGPKT QNYTRTVTNV
GDASSTYTVN IAKTQGVDIV VEPATLVFTK MYQQATYTVS FTQSGDFTDR FVQGAISWSS
NEYVVRSPIS VKLE
