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
//