SBTS_LOTJA
ID SBTS_LOTJA Reviewed; 759 AA.
AC A9JQS7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Subtilisin-like serine-protease S {ECO:0000303|PubMed:15980262};
DE Short=SbtS {ECO:0000303|PubMed:15980262};
DE Short=Subtilase S {ECO:0000303|PubMed:15980262};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10080};
DE Flags: Precursor;
GN Name=SbtS {ECO:0000303|PubMed:15980262};
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].
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 INDUCTION BY GLOMEROMYCOTA INTRARADICES AND MESORHIZOBIUM LOTI.
RX PubMed=15980262; DOI=10.1105/tpc.105.032714;
RA Kistner C., Winzer T., Pitzschke A., Mulder L., Sato S., Kaneko T.,
RA Tabata S., Sandal N., Stougaard J., Webb K.J., Szczyglowski K.,
RA Parniske M.;
RT "Seven Lotus japonicus genes required for transcriptional reprogramming of
RT the root during fungal and bacterial symbiosis.";
RL Plant Cell 17:2217-2229(2005).
RN [3]
RP INDUCTION BY GLOMEROMYCOTA INTRARADICES AND MESORHIZOBIUM LOTI, AND
RP DEVELOPMENTAL STAGE.
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: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 -!- 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 (PubMed:19220794). Also induced transiently in roots
CC epidermal cells (including root hair cells in nodule vicinity) during
CC symbiosis with Rhizobia bacteria (e.g. Mesorhizobium loti), but not
CC observed in nodules (PubMed:19220794). {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) (PubMed:19220794, PubMed:15980262). Up-regulated
CC transiently during root nodule symbiosis with Mesorhizobium loti
CC (PubMed:19220794, PubMed:15980262). {ECO:0000269|PubMed:15980262,
CC ECO:0000269|PubMed:19220794}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; AP006864; BAF95887.1; -; Genomic_DNA.
DR AlphaFoldDB; A9JQS7; -.
DR SMR; A9JQS7; -.
DR OMA; KMSFRVD; -.
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:0009609; P:response to symbiotic bacterium; IEP:UniProtKB.
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; IPR023828; Peptidase_S8_Ser-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; PS00138; SUBTILASE_SER; 1.
PE 2: Evidence at transcript level;
KW Apoplast; Glycoprotein; Hydrolase; Protease; Secreted; Serine protease;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..759
FT /note="Subtilisin-like serine-protease S"
FT /evidence="ECO:0000255"
FT /id="PRO_5002736790"
FT DOMAIN 28..105
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 110..613
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 390..462
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 215
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 545
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 759 AA; 81241 MW; 602E8B53A45AAE94 CRC64;
MGSAKILSFT LLLFVGYTLV HGSTPKHYIV YMGDRSHPNS ESVVRANHEI LASVTGSLND
AKAAAIHHYS RSFQGFSAMI TPEQAKKLAD HNSVVSVFES KMNKLHTTHS WDFLGLDTVY
KNNPSALDSA SNVIVGVIDS GVWPESESFN DYGLGPVPEK FKGECVTGDN FTLANCNKKI
IGARFYSKGL EAEIGPLENI VDSIFFRSPR DSDGHGTHTA STIAGSIVSN VSLFGMAKGT
ARGGAPSARL SIYKACWFGF CSDADVFAAM DDAIHDGVDI LSLSLGPDPP QPLYFENAIS
VGAFHAFQKG ILVSASAGNS VFPRTACNVA PWIFTVAAST VDREFRSDIY LGNSKVLKGL
SLNPIKMEGS YGLIYGSAAA AAGDAALNAS FCKEHTLDPT LIKGKIVICT VEKFTDNRRE
KAIIIKQGGG VGMILIDHNA RDVGFQFVIP STMIGQDAVE ELQAYMKTEK NPTATIFPTL
TLVGTKPAPE SAAFSSVGPN IITPDIIKPD ITGPGVNILA AWSPVATEAT VEQKSVNYNI
ISGTSMSCPH ISAISAIIKS HHPSWSPAAI MSAIMTSATV MDNTHSLIGR DPNGTQATPF
DYGSGHVNPV ASLNPGLVYD FSSQDVLNFL CSNGASPAQL KNLTGELTQC QKSPTASYNF
NYPSIGVSNL NGSLSVYRTV TYYGQEPTEY FASVERPSGV IVRVTPAKLK FWKAGEKITF
RIDFTPFKNS NGNFVFGALT WNNGKQRVRS PIGLNVLST
