ID   Q84F18_BACIU            Unreviewed;       381 AA.
AC   Q84F18;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 113.
DE   SubName: Full=Subtilisin {ECO:0000313|EMBL:CAD62180.1};
DE            EC=3.4.21.62 {ECO:0000313|EMBL:CAD62180.1};
GN   Name=aprE {ECO:0000313|EMBL:CAD62180.1};
OS   Bacillus subtilis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423 {ECO:0000313|EMBL:CAD62180.1};
RN   [1] {ECO:0000313|EMBL:CAD62180.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 6633 {ECO:0000313|EMBL:CAD62180.1};
RA   Corvey C.;
RT   "Activation of subtilin precursors by Bacillus subtilis extracellular
RT   serine proteases subtilisin (AprE), WprA and Vpr.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADY38664.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PTCC 1023 {ECO:0000313|EMBL:ADY38664.1};
RX   PubMed=22069026; DOI=10.1007/s12033-011-9467-6;
RA   Ghasemi Y., Dabbagh F., Ghasemian A.;
RT   "Cloning of a fibrinolytic enzyme (subtilisin) gene from Bacillus subtilis
RT   in Escherichia coli.";
RL   Mol. Biotechnol. 52:1-7(2012).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; HQ699519; ADY38664.1; -; Genomic_DNA.
DR   EMBL; AJ539133; CAD62180.1; -; Genomic_DNA.
DR   RefSeq; WP_003224341.1; NZ_ML241274.1.
DR   SMR; Q84F18; -.
DR   MEROPS; S08.036; -.
DR   GeneID; 64302906; -.
DR   PATRIC; fig|1423.172.peg.1018; -.
DR   BRENDA; 3.4.21.62; 658.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07477; Peptidases_S8_Subtilisin_subset; 1.
DR   Gene3D; 3.30.70.80; Peptidase S8 propeptide/proteinase inhibitor I9; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR010259; S8pro/Inhibitor_I9.
DR   InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR   InterPro; IPR034202; Subtilisin_Carlsberg-like.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF05922; Inhibitor_I9; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           30..381
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007712414"
FT   DOMAIN          38..102
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000259|Pfam:PF05922"
FT   DOMAIN          129..372
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        138
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        170
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        327
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   381 AA;  39555 MW;  CE1EDDEFC09B3560 CRC64;
     MRSKKLWISL LFALTLIFTM AFSNMSAQAA GKSSTEKKYI VGFKQTMSAM SSAKKKDVIS
     EKGGKVQKQF KYVNAAAATL DAKAVKELKQ DPSVAYVEED HIAHQYAQSV PYGISQIKAP
     ALHSQGYTGS NVKVAVIDSG IDSSHPDLNV RGGASFVPSE TNPYQDGSSH GTHVAGTVAA
     LNNSIGVLGV APNASLYAVK VLDSTGNGQY SWIINGIEWA ISNKMDVINM SLGGPSGSTA
     LKSVVDRAVA SGIVVVAAAG NEGTSGSSST IGYPAKYPST IAVGAVNSSN QRGSFSSVGP
     ELDVMAPGVS IQSTLPGGTY GAYNGTSMAT PHVAGAAALI LSKHPTWTNA QVRDRLESTT
     TYLGNSFYYG KGLINVQAAA Q
//