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
//