SBT_MEDTR
ID SBT_MEDTR Reviewed; 748 AA.
AC G7KEU7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Subtilisin-like protease {ECO:0000303|PubMed:12953114};
DE Short=Subtilase {ECO:0000303|PubMed:12953114};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10080};
DE Flags: Precursor;
GN Name=SBT {ECO:0000303|PubMed:12953114};
GN OrderedLocusNames=MTR_5g011320 {ECO:0000312|EMBL:AES94154.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17;
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E.D., Geurts R., Cannon S.B.,
RA Udvardi M.K., Benedito V.A., Mayer K.F.X., Gouzy J., Schoof H.,
RA Van de Peer Y., Proost S., Cook D.R., Meyers B.C., Spannagl M., Cheung F.,
RA De Mita S., Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K.,
RA Murray J.D., Naoumkina M.A., Rosen B., Silverstein K.A.T., Tang H.,
RA Rombauts S., Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M.,
RA Bellec A., Berger A., Berges H., Bidwell S., Bisseling T., Choisne N.,
RA Couloux A., Denny R., Deshpande S., Dai X., Doyle J.J., Dudez A.-M.,
RA Farmer A.D., Fouteau S., Franken C., Gibelin C., Gish J., Goldstein S.,
RA Gonzalez A.J., Green P.J., Hallab A., Hartog M., Hua A., Humphray S.J.,
RA Jeong D.-H., Jing Y., Jocker A., Kenton S.M., Kim D.-J., Klee K., Lai H.,
RA Lang C., Lin S., Macmil S.L., Magdelenat G., Matthews L., McCorrison J.,
RA Monaghan E.L., Mun J.-H., Najar F.Z., Nicholson C., Noirot C.,
RA O'Bleness M., Paule C.R., Poulain J., Prion F., Qin B., Qu C., Retzel E.F.,
RA Riddle C., Sallet E., Samain S., Samson N., Sanders I., Saurat O.,
RA Scarpelli C., Schiex T., Segurens B., Severin A.J., Sherrier D.J., Shi R.,
RA Sims S., Singer S.R., Sinharoy S., Sterck L., Viollet A., Wang B.-B.,
RA Wang K., Wang M., Wang X., Warfsmann J., Weissenbach J., White D.D.,
RA White J.D., Wiley G.B., Wincker P., Xing Y., Yang L., Yao Z., Ying F.,
RA Zhai J., Zhou L., Zuber A., Denarie J., Dixon R.A., May G.D.,
RA Schwartz D.C., Rogers J., Quetier F., Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17;
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-228, AND INDUCTION BY GLOMUS VERSIFORME.
RC STRAIN=cv. Jemalong A17;
RX PubMed=12953114; DOI=10.1105/tpc.014183;
RA Liu J., Blaylock L.A., Endre G., Cho J., Town C.D., VandenBosch K.A.,
RA Harrison M.J.;
RT "Transcript profiling coupled with spatial expression analyses reveals
RT genes involved in distinct developmental stages of an arbuscular
RT mycorrhizal symbiosis.";
RL Plant Cell 15:2106-2123(2003).
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: Accumulates in mycorrhizal roots upon colonization by the
CC arbuscular mycorrhiza (AM) fungus Glomus versiforme.
CC {ECO:0000269|PubMed:12953114}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; CM001221; AES94154.1; -; Genomic_DNA.
DR EMBL; AW584611; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_003611196.1; XM_003611148.1.
DR AlphaFoldDB; G7KEU7; -.
DR SMR; G7KEU7; -.
DR STRING; 3880.AES94154; -.
DR EnsemblPlants; AES94154; AES94154; MTR_5g011320.
DR GeneID; 11443095; -.
DR Gramene; AES94154; AES94154; MTR_5g011320.
DR KEGG; mtr:MTR_5g011320; -.
DR eggNOG; ENOG502QPQR; Eukaryota.
DR HOGENOM; CLU_000625_4_6_1; -.
DR OMA; VYPFHPS; -.
DR OrthoDB; 337164at2759; -.
DR Proteomes; UP000002051; Chromosome 5.
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; Reference proteome; Secreted;
KW Serine protease; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..748
FT /note="Subtilisin-like protease"
FT /id="PRO_5014573578"
FT DOMAIN 37..115
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 122..600
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 365..454
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 147
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 533
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 376
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 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 722
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 223..224
FT /note="SV -> KC (in Ref. 3; AW584611)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 748 AA; 80476 MW; EFB315C7B4CA70D7 CRC64;
MMKMELRLLV SLIFILCSIS MLAAEENLEH DQINLMTYIV HVKKSENVAS HQSEDLHSWY
HSFLPQTFPH KERMVFSYRK VASGFAVKLT PEEAKSLQEK GEIVSARPER TLELHTTHTP
TFLGLKQGQG LWSDDNLGKG VIIGIIDTGI FPLHPSFNDE GMPPPPAKWK GHCEFTGGQV
CNNKLIGARN LVKSAIQEPP FENFFHGTHT AAEAAGRFIE DASVFGNAKG VAAGMAPNAH
LAIYKVCNDK IGCTESAILA AMDIAIEDGV DVLSLSLGLG SLPFFEDPIA IGAFAATQNG
VFVSCSAANS GPGYSTLSNE APWILTVGAS TIDRKIVASA KLGNGEEYEG ETLFQPKDFS
QQLLPLVYPG SFGYGNQTQN QSLCLPGSLK NIDLSGKVVL CDVGNVSSIV KGQEVLNSGG
IAMILANSEA LGFSTFAIAH VLPAVEVSYA AGLTIKSYIK STYNPTATLI FKGTIIGDSL
APSVVYFSSR GPSQESPGIL KPDIIGPGVN ILAAWAVSVD NKIPAFDIVS GTSMSCPHLS
GIAALIKSSH PDWSPAAIKS AIMTTANTLN LGGIPILDQR LFPADIFATG AGHVNPVKAN
DPGLVYDIEP EDYVPYLCGL GYSDKEIEVI VQWKVKCSNV KSIPEAQLNY PSFSILLGSD
SQYYTRTLTN VGFANSTYKV ELEVPLALGM SVNPSEITFT EVNEKVSFSV EFIPQIKENR
RNHTFGQGSL TWVSDRHAVR IPISVIFK
