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Database: UniProt
Entry: Q069K8_BRELA
LinkDB: Q069K8_BRELA
Original site: Q069K8_BRELA 
ID   Q069K8_BRELA            Unreviewed;       521 AA.
AC   Q069K8;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   Name=npr4 {ECO:0000313|EMBL:ABI93802.1};
OS   Brevibacillus laterosporus (Bacillus laterosporus).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1465 {ECO:0000313|EMBL:ABI93802.1};
RN   [1] {ECO:0000313|EMBL:ABI93802.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tian B.Y., Lian L.H., Yang J.K., Zhang K.Q.;
RT   "Direct Submission.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ABI93802.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17109172; DOI=10.1007/s00253-006-0690-1;
RA   Tian B., Yang J., Lian L., Wang C., Li N., Zhang K.Q.;
RT   "Role of an extracellular neutral protease in infection against nematodes
RT   by Brevibacillus laterosporus strain G4.";
RL   Appl. Microbiol. Biotechnol. 74:372-380(2007).
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|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; DQ983787; ABI93802.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q069K8; -.
DR   MEROPS; M04.014; -.
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:SF1; BACILLOLYSIN; 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   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|RuleBase:RU366073};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           28..521
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023156127"
FT   DOMAIN          78..125
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          139..215
FT                   /note="PepSY"
FT                   /evidence="ECO:0000259|Pfam:PF03413"
FT   DOMAIN          225..372
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          375..520
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        365
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        449
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   521 AA;  56887 MW;  CDAB02D30A12986E CRC64;
     MGLGKKLSVA VAASFMSLTI SLPGVQAAEN PQLKENLTNF VPKHSLVQSE LPSVSDKAIK
     QYLKQNGKVF KGNPSERLKL IDHTTDDLGY KHFRYVPVVN GVPVKDSQVI IHVDKSNNVY
     AINEELNNDA SAKTANSKKL SANQALDHAF KAIGKSPEAV SNGNVANKNK AELKAAATKD
     GKYRLAYDVA IRYIEPEPAN WEVTVDAETG KVLKKQNKVE HAAATGTGTT LKGKTVSLNI
     SSESGKYVMR DLSKPTGTQI ITYDLQNRQY NLPGTLVSST TNQFTTSSQR AAVDAHYNLG
     KVYDYFYQTF KRNSYDNKGG KIVSSVHYGS KYNNAAWIGD QMIYGDGDGS FFSPLSGSMD
     VTAHEMTHGV TQETANLNYE NQPGALNESF SDVFGYFNDT EDWDIGEDIT VSQPALRSLS
     NPTKYGRPDH YKNYRNLPNT DAGDYGGVHT NSGIPNKAAY NTITKIGVKK AEQIYYRALT
     VYLTPSSSFK DAKAALIQSA RDLYGSQDAA SVEAAWNAVG L
//
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