ID B0LX66_BACIU Unreviewed; 382 AA.
AC B0LX66;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Alkaline protease {ECO:0000313|EMBL:ABY83469.1};
OS Bacillus subtilis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423 {ECO:0000313|EMBL:ABY83469.1};
RN [1] {ECO:0000313|EMBL:ABY83469.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ZJ06 {ECO:0000313|EMBL:ABY83469.1};
RA Xu S., Xu X., Li X., Wang Q.;
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
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; EU386607; ABY83469.1; -; Genomic_DNA.
DR AlphaFoldDB; B0LX66; -.
DR SMR; B0LX66; -.
DR MEROPS; S08.042; -.
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..382
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002751747"
FT DOMAIN 40..105
FT /note="Inhibitor I9"
FT /evidence="ECO:0000259|Pfam:PF05922"
FT DOMAIN 130..371
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 171
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 382 AA; 39178 MW; E23D66F574EA2C15 CRC64;
MRGKKVWISL LFALALIFTM AFGSTSPAHA AGKSNGEKKY IVGFKQTMST MSAAKKKDVI
FEKGGKVQKQ FKYVDAASAT LNEKAVKELK KDPSVAYVEE DHVAQAYAQS VPYGVSQIKA
PALHSQGFTG SNVKVAVIDS GIDSSHPDLK VAGGASMVPS ETNPFQDNNS HGTHVAGTVA
ALNNSVGVLG VAPSASLYAV KVLGADGSGQ YSWIINGIEW AIANNMDVIN MSLGGPSGSA
ALKAAVDKAV ASGIVVVAAA GNEGTSGGSS TVGYPGKYPS VIAVGAVNSS NQRASFSSVG
SELDVMAPGV SIQSTLPGNK YGAYNGTSMA SPHVAGAAAL ILSKHPNWTN TQVRSSLENT
TTKLGDAFYY GKGLINVQAA AQ
//
