ID B7IWX8_BACC2 Unreviewed; 566 AA.
AC B7IWX8;
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=BCG9842_B4700 {ECO:0000313|EMBL:ACK95104.1};
OS Bacillus cereus (strain G9842).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405531 {ECO:0000313|EMBL:ACK95104.1, ECO:0000313|Proteomes:UP000006744};
RN [1] {ECO:0000313|EMBL:ACK95104.1, ECO:0000313|Proteomes:UP000006744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G9842 {ECO:0000313|EMBL:ACK95104.1,
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 -!- 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; CP001186; ACK95104.1; -; Genomic_DNA.
DR RefSeq; WP_000730377.1; NC_011772.1.
DR AlphaFoldDB; B7IWX8; -.
DR MEROPS; M04.001; -.
DR KEGG; bcg:BCG9842_B4700; -.
DR HOGENOM; CLU_008590_5_2_9; -.
DR Proteomes; UP000006744; 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; 3.10.450.40; -; 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; IPR025711; PepSY.
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; PF03413; PepSY; 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, ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 28..566
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023159511"
FT DOMAIN 84..134
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 154..219
FT /note="PepSY"
FT /evidence="ECO:0000259|Pfam:PF03413"
FT DOMAIN 257..400
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 403..565
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 393
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 481
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 566 AA; 60827 MW; 7C3A8E98BC98F497 CRC64;
MKKKSLALVL ATGMAVTTFG GTGSAFADSK NVLSTKKYNE TVQSPEFISG DLTGATGKKA
ESVVFDYLNA AKGDYKLGEK SAQDSFKVKQ VKKDAVTDST VVRMQQVYEG VPVWGSTQVA
HVSKDGSLKV LSGTVAPDLD KKEKLKNKNK IEGAKAIEIA QQDLGVTPKY EVEPKADLYV
YQNGEETTYA YVVNLNFLDP SPGNYYYFIE ADSGKVLNKY NKLDHVANED KSPVKQEAPK
QDAKAVVKPV TGTNKVGTGK GVLGDTKSLN TTLSGSSYYL QDNTRGATIF TYDAKNRSTL
PGTLWADADN VFNAAYDAAA VDAHYYAGRT YDYYKATFNR NSINDAGAPL KSTVHYGSKY
NNAFWNGSQM VYGDGDGVTF TSLSGGIDVI GHELTHAVTE NSSDLIYQNE SGALNEAISD
IFGTLVEFYD NRNPDWEIGE DIYTPGKAGD ALRSMSDPAK YGDPDHYSKR YTGSSDNGGV
HTNSGIINKQ AYLLANGGTH SGVTVTGIGK DKLGAIYYRA NTQYFTQSTT FSQARAGAVQ
AAADLYGASS AEVNAVKQSF SAVGVN
//
