SBT1_LOTJA
ID SBT1_LOTJA Reviewed; 750 AA.
AC A9QY40;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Subtilisin-like protease 1 {ECO:0000303|PubMed:19220794};
DE Short=SbtM1 {ECO:0000303|PubMed:19220794};
DE Short=Subtilase 1 {ECO:0000303|PubMed:19220794};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10080};
DE Flags: Precursor;
GN Name=SBTM1 {ECO:0000303|PubMed:19220794};
OS Lotus japonicus (Lotus corniculatus var. japonicus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; robinioid clade; Loteae; Lotus.
OX NCBI_TaxID=34305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Miyakojima MG-20;
RX PubMed=18511435; DOI=10.1093/dnares/dsn008;
RA Sato S., Nakamura Y., Kaneko T., Asamizu E., Kato T., Nakao M.,
RA Sasamoto S., Watanabe A., Ono A., Kawashima K., Fujishiro T., Katoh M.,
RA Kohara M., Kishida Y., Minami C., Nakayama S., Nakazaki N., Shimizu Y.,
RA Shinpo S., Takahashi C., Wada T., Yamada M., Ohmido N., Hayashi M.,
RA Fukui K., Baba T., Nakamichi T., Mori H., Tabata S.;
RT "Genome structure of the legume, Lotus japonicus.";
RL DNA Res. 15:227-239(2008).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, INDUCTION BY GLOMEROMYCOTA INTRARADICES,
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Gifu / B-129, and cv. Miyakojima MG-20;
RX PubMed=19220794; DOI=10.1111/j.1365-313x.2009.03824.x;
RA Takeda N., Sato S., Asamizu E., Tabata S., Parniske M.;
RT "Apoplastic plant subtilases support arbuscular mycorrhiza development in
RT Lotus japonicus.";
RL Plant J. 58:766-777(2009).
CC -!- FUNCTION: Required for arbuscular mycorrhiza (AM) development during AM
CC symbiosis with AM fungi (e.g. Glomeromycota intraradices).
CC {ECO:0000269|PubMed:19220794}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:19220794}. Note=Accumulates in the intercellular
CC spaces and the periarbuscular space (PAS) during arbuscular mycorrhizal
CC (AM) symbiosis. {ECO:0000269|PubMed:19220794}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in root cells that are adjacent to
CC intra-radical fungal hyphae or in cells that harbor them during
CC arbuscular mycorrhizal (AM) symbiosis, especially in epidermal and
CC cortical cells. {ECO:0000269|PubMed:19220794}.
CC -!- INDUCTION: Rapidly induced in roots during development of arbuscular
CC mycorrhiza (AM) upon colonization by AM fungus (e.g. Glomeromycota
CC intraradices). {ECO:0000269|PubMed:19220794}.
CC -!- DISRUPTION PHENOTYPE: Decreased fungal colonization and impaired
CC arbuscular mycorrhiza (AM) development during AM symbiosis with AM
CC fungi (e.g. Glomeromycota intraradices). {ECO:0000269|PubMed:19220794}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; AP009544; BAF95755.1; -; Genomic_DNA.
DR AlphaFoldDB; A9QY40; -.
DR SMR; A9QY40; -.
DR MEROPS; S08.006; -.
DR OMA; VYPFHPS; -.
DR GO; GO:0048046; C:apoplast; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0036377; P:arbuscular mycorrhizal association; IMP: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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..750
FT /note="Subtilisin-like protease 1"
FT /id="PRO_5002740348"
FT DOMAIN 40..118
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 125..602
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 370..456
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 150
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 209
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 535
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 724
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 750 AA; 80220 MW; 821BC6C6A941C468 CRC64;
MEQTKYRMEL VLLLGLISML SFIPASIAAE EGQEHDNLTT YIVHVKKLEI EGPLQSTEEL
HTWHHSFLPE TSNKDRMVFS YRNVASGFAV RLTPEEANAL QEKEEVMSIR PERTLSLHTT
HTPSFLGLRQ GQGLWNDSNL GKGVIIGVID TGIYPFHLSF NDEGMPPPPA KWKGHCEFTG
GSVCNNKLIG ARNLVKSAIQ EPPYEDFFHG THTAAEAAGR FVEGASVFGN ARGTAAGMAP
DAHLAIYKVC SSKVKDECPE SAILAAMDIA IEDGVDVLSL SLGLGSLPFF EDPIAIGAFA
ATQKGIFVSC SAANSGPHYS SLSNEAPWIL TVGASTIDRK ISASAKLGNG AEYEGETLFQ
PKDFSSQLLP LVYAAAEKNN SSALCAPGSL RNINVKGKVV VCDLGGGIPF IAKGQEVLDA
GGSAMILANI ENFGFTTLAN AHVLPAVHVS YAASLAIKAY INSTYTPTAT VLFQGTIIGD
SLAPSVAAFS SRGPSQQSPG ILKPDIIGPG VNILAAWAVS VDNKIPAFDI ISGTSMSCPH
LSGIAALLKS AHPDWSPAAI KSAIMTTANT LNLRGLPILD QRLQPADIFA TGAGHVNPVR
ANDPGLVYDI QPEDYVPYLC GLGYSDREVT IIVQRSVRCF NVKSIAQAEL NYPSFSILLG
SDSQFYTRTL TNVGPANSTY TVKIDVPLAM GISVSPSQIT FTQVNQKVAY FVDFIPQIKE
NRGNHTFAQG AITWVSDKHV VRTPISVIFK
