SBT55_ARATH
ID SBT55_ARATH Reviewed; 803 AA.
AC F4KEL0; Q9FK77;
DT 20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Subtilisin-like protease SBT5.5 {ECO:0000303|PubMed:16193095};
DE EC=3.4.21.- {ECO:0000255|PROSITE-ProRule:PRU10082};
DE AltName: Full=Subtilase subfamily 5 member 5 {ECO:0000303|PubMed:16193095};
DE Short=AtSBT5.5 {ECO:0000303|PubMed:16193095};
DE Flags: Precursor;
GN Name=SBT5.5 {ECO:0000303|PubMed:16193095};
GN OrderedLocusNames=At5g45640 {ECO:0000312|Araport:AT5G45640};
GN ORFNames=MRA19.4 {ECO:0000312|EMBL:BAB09207.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9734815; DOI=10.1093/dnares/5.3.203;
RA Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT features of the regions of 1,367,185 bp covered by 19 physically assigned
RT P1 and TAC clones.";
RL DNA Res. 5:203-216(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16193095; DOI=10.1371/journal.pcbi.0010040;
RA Rautengarten C., Steinhauser D., Bussis D., Stintzi A., Schaller A.,
RA Kopka J., Altmann T.;
RT "Inferring hypotheses on functional relationships of genes: Analysis of the
RT Arabidopsis thaliana subtilase gene family.";
RL PLoS Comput. Biol. 1:E40-E40(2005).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q84WS0}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AED95279.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAB09207.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB012245; BAB09207.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED95279.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_199377.2; NM_123932.2.
DR AlphaFoldDB; F4KEL0; -.
DR SMR; F4KEL0; -.
DR STRING; 3702.AT5G45640.1; -.
DR MEROPS; S08.A05; -.
DR PeptideAtlas; F4KEL0; -.
DR PRIDE; F4KEL0; -.
DR GeneID; 834604; -.
DR KEGG; ath:AT5G45640; -.
DR Araport; AT5G45640; -.
DR TAIR; locus:2172018; AT5G45640.
DR eggNOG; ENOG502QRC5; Eukaryota.
DR HOGENOM; CLU_000625_4_3_1; -.
DR InParanoid; F4KEL0; -.
DR OrthoDB; 337164at2759; -.
DR PRO; PR:F4KEL0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KEL0; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Autocatalytic cleavage; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..112
FT /note="Activation peptide"
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435257"
FT CHAIN 113..?
FT /note="Subtilisin-like protease SBT5.5"
FT /evidence="ECO:0000255"
FT /id="PRO_5003311630"
FT PROPEP ?..803
FT /evidence="ECO:0000250|UniProtKB:Q39547"
FT /id="PRO_0000435258"
FT DOMAIN 30..108
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 140..656
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 409..504
FT /note="PA"
FT /evidence="ECO:0000255"
FT ACT_SITE 169
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 244
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 589
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 803 AA; 87925 MW; 5A8F1D6DF40135F1 CRC64;
MKRIFGIFIF LSLLLFLVPL LASCTKEKQV YIVYFGEHKG DKAFHEIEAH HHSYLQSVKE
TEEDATSSLL YRRASSINGF AAELTPDQAS RLKELKEVVS VFKSDPRKYK IHTTRSWEFV
GLKEEEGEDY RSDGDAPRHK YDVNDRFRVG RKFLKNAKHG DGVIVGLIDS GVWPESRSFD
DKGMGPIPES WKGICQTGVA FNSSHCNRKI IGARYYARGY ERYYGPFNAE ANKDFLSPRD
ADGHGSHTAS TAVGRRVDGV SALGGIAMGT ASGGASLARL AVYKACWAVP NKEKYATNTC
FDEDMLAAFD DAIADGVNVI SISIGTVEPH TYLEDGIAIG ALHAVKRDIV VAASAGNDGP
ARETLSNPAP WIITVGASSL DRFFVGRLEL GDGYVFESDS LTTLKMDNYA PLVYAPDVVV
PGVSRNDAML CLPNALSPDH VRGKVVLCLR GYGSGSTIGK GLEVKRAGGV GMILANSRDN
DAFDVESHFV PTALVFSSTV DRILDYIYNT YEPVAFIKPA ETVLYRNQPE DSVYPFSSRA
PNWVDANILK PDIIAPGLNI LAAWSGADSA SKDSIDRRVL DYNLDSGTSM SCPHVAGAIA
LLKSMHPTWS SAAIRSALMT TASMTNEDNE PIQDYDGSPA NPFALGSRHF RPTKAASPGL
VYDASYQSYL LYCCSVGLTN LDPTFKCPSR IPPGYNLNYP SISIPYLSGT VTVTRTVTCV
GRTGNSTSVY VFNAQPPNGV LVKAEPNVLV FDKIGQKKRF NIIFTTQRYE FTGEARRDRY
RFGWFSWTDG HHVVRSSIAV SLV
