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Database: UniProt
Entry: B7H6C2_BACC4
LinkDB: B7H6C2_BACC4
Original site: B7H6C2_BACC4 
ID   B7H6C2_BACC4            Unreviewed;       565 AA.
AC   B7H6C2;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   OrderedLocusNames=BCB4264_A3392 {ECO:0000313|EMBL:ACK59004.1};
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532 {ECO:0000313|EMBL:ACK59004.1, ECO:0000313|Proteomes:UP000007096};
RN   [1] {ECO:0000313|EMBL:ACK59004.1, ECO:0000313|Proteomes:UP000007096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264 {ECO:0000313|EMBL:ACK59004.1,
RC   ECO:0000313|Proteomes:UP000007096};
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 B4264.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Extracellular zinc metalloprotease.
CC       {ECO:0000256|RuleBase:RU366073}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU366073};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|RuleBase:RU366073}.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
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DR   EMBL; CP001176; ACK59004.1; -; Genomic_DNA.
DR   RefSeq; WP_001058955.1; NZ_VEHB01000007.1.
DR   AlphaFoldDB; B7H6C2; -.
DR   KEGG; bcb:BCB4264_A3392; -.
DR   HOGENOM; CLU_008590_2_2_9; -.
DR   Proteomes; UP000007096; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09597; M4_TLP; 1.
DR   Gene3D; 3.10.170.10; -; 1.
DR   Gene3D; 3.10.450.490; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR023612; Peptidase_M4.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR001570; Peptidase_M4_C_domain.
DR   InterPro; IPR013856; Peptidase_M4_domain.
DR   PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF3; NEUTRAL PROTEASE B; 1.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU366073};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366073};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT   DOMAIN          81..129
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          245..398
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          402..563
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        392
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        481
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   565 AA;  62483 MW;  C4F89259F0701B1B CRC64;
     MNNFVKVGLT TGVVLSAIMP YGGVHAETED LKVETKEDTF RTGNLTAPSQ NSAENVAKDA
     LKGKTEQALS SKQVNTESKV NYNVTQSRKS YDGTTLVRLQ QTYEGRDVYG YQLTAHINDD
     GVLTSVSGDS AQNLQQQEDL KQPITLSEED AKKQLFNIYG NDLTFIEEPE IKQVVYVDEN
     TNKATNAYQI TFSASTPEYV SGTVLIDAFG GNLLKELVQK LGIQVESSIV QSATSNKSTD
     PSKLTGTGKD DLGINRTFGI TQRSDGTYML ADYSRGKGIE TYTANYKDYN NYRRNVWGYL
     DDLVTSNSTN FTDPKAVSAH YLATKVYDFY QEKYGRNSFD NNGQKVISVV HGWNTNGTNK
     GNPKQWFNAF SNGAMLVYGD PIVRAFDVAG HEFTHAVTRN ESGLEYAGEA GAINEALSDI
     LGVAVEKYAN NGKFNWTMGE QSGRIFRDMK NPSSISSRYP EDYRHYNNLP IDADHDHGGV
     HTNSSIINKV AYLIASGGSH NGVNVHGIGE DKMFDIFYYA NTDELNMTSD FKELKEACIR
     VATNLYGKDS LEVQAVQQAF KAAYI
//
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