ID   B7IUG3_BACC2            Unreviewed;       399 AA.
AC   B7IUG3;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Zinc protease, insulinase family {ECO:0000313|EMBL:ACK97733.1};
GN   OrderedLocusNames=BCG9842_B1341 {ECO:0000313|EMBL:ACK97733.1};
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405531 {ECO:0000313|EMBL:ACK97733.1, ECO:0000313|Proteomes:UP000006744};
RN   [1] {ECO:0000313|EMBL:ACK97733.1, ECO:0000313|Proteomes:UP000006744}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842 {ECO:0000313|EMBL:ACK97733.1,
RC   ECO:0000313|Proteomes:UP000006744};
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   EMBL; CP001186; ACK97733.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7IUG3; -.
DR   MEROPS; M16.A15; -.
DR   KEGG; bcg:BCG9842_B1341; -.
DR   HOGENOM; CLU_009902_3_0_9; -.
DR   Proteomes; UP000006744; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:ACK97733.1};
KW   Protease {ECO:0000313|EMBL:ACK97733.1}.
FT   DOMAIN          2..145
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          152..324
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   399 AA;  45301 MW;  7E71BE96855C8A67 CRC64;
     MENIPTVRSV AIGIWIHAGS RNENEKNNGI SHFLEHMFFK GTETRSAREI AESFDSIGGQ
     VNAFTSKEYT CYYAKVLDEH AKYALDVLAD MFFNSTFDEE ELKKEKNVVC EEIKMYEDAP
     DDIVHDMLTK ATYETHPLGY PILGTEETLN TFTGDTLRQY IKDHYTPENV VVSVAGNIDE
     AFLQTVEQYF GSYEGTTNRE QVHSPIFHFN KVARKKETEQ AHLCLGYKGL QMGHEDIYNL
     IVLNNVLGGS MSSRLFQEVR EQRGLAYSVF SYHSSYEDTG MLTLYGGTGS QQLDTLYETM
     QETLETLKNT GITEKELMNS KEQLKGNLML SLESTNSRMS RNGKNELLLR KHRSLDEIIE
     SVNTVTKENV DGLIRNMFTD EFSAALISPD GKLPKGIKL
//