SBT4_LOTJA
ID SBT4_LOTJA Reviewed; 755 AA.
AC A9QY38;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Subtilisin-like protease 4 {ECO:0000303|PubMed:19220794};
DE Short=SbtM4 {ECO:0000303|PubMed:19220794};
DE Short=Subtilase 4 {ECO:0000303|PubMed:19220794};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10080};
DE Flags: Precursor;
GN Name=SBTM4 {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 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). During symbiosis with Rhizobia
CC bacteria (e.g. Mesorhizobium loti), induced in nodules
CC (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). Also observed in root nodules that
CC arise from symbiotic associations with nitrogen-fixing Rhizobia
CC bacteria (e.g. Mesorhizobium loti) (PubMed:19220794).
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; AP009542; BAF95753.1; -; Genomic_DNA.
DR AlphaFoldDB; A9QY38; -.
DR SMR; A9QY38; -.
DR MEROPS; S08.006; -.
DR ProMEX; A9QY38; -.
DR OMA; WKGHCDF; -.
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; 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..755
FT /note="Subtilisin-like protease 4"
FT /id="PRO_5002742806"
FT DOMAIN 41..119
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 128..611
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 376..461
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 153
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 217
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 544
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 706
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 755 AA; 80096 MW; F34E43C2EC7568BC CRC64;
MDYFLFIALT FLLTFHVHNA QGSELPTTTT ESTETSSSKI YIIHVTGPEG KMLTESEDLE
SWYHSFLPPT LMSSEEQPRV IYSYKNVLRG FAASLTQEEL SAVEKKNGFI SAHPQRVLHR
QTTHTPKFLG LQQDTGVWKE SNFGKGVIIG VLDSGITPGH PSFSDVGIPP PPPKWKGRCD
LNVTACNNKL IGARAFNLAA EAMNGKKAEA PIDEDGHGTH TASTAAGAFV NYAEVLGNAK
GTAAGMAPHA HLAIYKVCFG EDCPESDILA ALDAAVEDGV DVISISLGLS EPPPFFNDST
AIGAFAAMQK GIFVSCAAGN SGPFNSSIVN AAPWILTVGA STIDRRIVAT AKLGNGQEFD
GESVFQPSSF TPTLLPLAYA GKNGKEESAF CANGSLDDSA FRGKVVLCER GGGIARIAKG
EEVKRAGGAA MILMNDETNA FSLSADVHAL PATHVSYAAG IEIKAYINST ATPTATILFK
GTVIGNSLAP AVASFSSRGP NLPSPGILKP DIIGPGVNIL AAWPFPLSNS TDSKLTFNIE
SGTSMSCPHL SGIAALLKSS HPHWSPAAIK SAIMTSADTI NLGNKLIVDE TLQPTDLFAT
GSGHVNPSRA NDPGLVYDIQ PDDYIPYLCG LGYSETEVGI IAHRKIKCSA SIPEGELNYP
SFSVELGSSK TFTRTVTNVG EAHSSYDLIV AAPQGVDVKV QPYKLNFSEV NQKETYSVTF
SRTGLGNKTQ EYAQGFLKWV STKHTVRSPI SVKFI
