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Database: UniProt
Entry: V9W901_9BACL
LinkDB: V9W901_9BACL
Original site: V9W901_9BACL 
ID   V9W901_9BACL            Unreviewed;       529 AA.
AC   V9W901;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   Name=npr1 {ECO:0000313|EMBL:AHD05592.1};
GN   ORFNames=ERIC2_c17790 {ECO:0000313|EMBL:AHD05592.1};
OS   Paenibacillus larvae subsp. larvae DSM 25430.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=697284 {ECO:0000313|EMBL:AHD05592.1, ECO:0000313|Proteomes:UP000029431};
RN   [1] {ECO:0000313|EMBL:AHD05592.1, ECO:0000313|Proteomes:UP000029431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25430 {ECO:0000313|EMBL:AHD05592.1,
RC   ECO:0000313|Proteomes:UP000029431};
RX   PubMed=24599066;
RA   Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA   Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT   "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT   Mechanisms of Paenibacillus larvae.";
RL   PLoS ONE 9:E90914-E90914(2014).
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; CP003355; AHD05592.1; -; Genomic_DNA.
DR   RefSeq; WP_024094035.1; NZ_CP019652.1.
DR   AlphaFoldDB; V9W901; -.
DR   MEROPS; M04.018; -.
DR   KEGG; plv:ERIC2_c17790; -.
DR   PATRIC; fig|697284.3.peg.1705; -.
DR   eggNOG; COG3227; Bacteria.
DR   HOGENOM; CLU_008590_5_2_9; -.
DR   Proteomes; UP000029431; 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; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000029431};
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..23
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           24..529
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5039758834"
FT   DOMAIN          78..129
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          226..368
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          371..528
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        361
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        444
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   529 AA;  57255 MW;  C7CEB3161B57C7F7 CRC64;
     MKKTLVTILA GAFLVGTSLS AGAAGVAGAE DPNRELAPKT IVGENWNPPS GASEEEAIWK
     YLSNKEEKLD ISKEEIKDQL KIVKKEKDSK SGTSHYKLKQ YIQGIPVYGA DQTVHFNKEG
     EITSLIGSVL PSDYQNLLPS GTKPQISPTE AIQAAEKDAE KQIGKLGKPE AAPKADLNVY
     LDKGKAFLVY VTEVNVLEPQ ALRTRYFINA QDGSIVSKYS LLDHATGTGT GVLGDKKSFI
     TTKSGSTFQL SDTTRGNGIK TYSASNRYTL PGLLLTNTNN DNWTDGAAVD AHTYAETVYD
     FYKNKFNRNS LDGKGLQIKS TVHYGAKYNN AFWNGQQIVF GDGDGKTFIP FSGDLDVVGH
     ELTHGVTEHT ANLEYENESG ALNESISDII GNAIKGKGWL IGEDVYTPNI PEDALRSLED
     PTLYGQPDHY SNRYKGPSDN GGVHTNSGIN NKAYYLLAQG GTHKGITIDG IGRDNAVNIY
     YHALVYYLTP NSNFSAMRAA AIQSATDLFG ADSSEVDSVN KAYDAVGVK
//
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