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Database: UniProt
Entry: A0A0M0L7B7_9BACI
LinkDB: A0A0M0L7B7_9BACI
Original site: A0A0M0L7B7_9BACI 
ID   A0A0M0L7B7_9BACI        Unreviewed;       558 AA.
AC   A0A0M0L7B7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=AMD01_07595 {ECO:0000313|EMBL:KOO46782.1};
OS   Priestia koreensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=284581 {ECO:0000313|EMBL:KOO46782.1, ECO:0000313|Proteomes:UP000037558};
RN   [1] {ECO:0000313|Proteomes:UP000037558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16467 {ECO:0000313|Proteomes:UP000037558};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Fjat-14210 dsm16467.";
RL   Submitted (AUG-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KOO46782.1}.
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DR   EMBL; LILC01000011; KOO46782.1; -; Genomic_DNA.
DR   RefSeq; WP_053400788.1; NZ_LILC01000011.1.
DR   AlphaFoldDB; A0A0M0L7B7; -.
DR   PATRIC; fig|284581.3.peg.3568; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000037558; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000037558};
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..28
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           29..558
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5039743485"
FT   DOMAIN          93..141
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          157..229
FT                   /note="PepSY"
FT                   /evidence="ECO:0000259|Pfam:PF03413"
FT   DOMAIN          248..392
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          395..557
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        385
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        473
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   558 AA;  60361 MW;  EBBBDD67E675F489 CRC64;
     MIKGVVRVKK RLLTIGLVLG LSSSVSFPYH TLAADVKEKI NWNAKTNTPE FVSGNLATAK
     GLVAQNPKNL VFSYFNENKG LFKLGHQEAE KALVVKEERV DDLGYTFLRL QQTYKGVPVY
     GGTITAHINK EGTLTAVSGT LLPNLETSKS VNKKASITAT QAKNKAEKDL KGLLKSSPSY
     EKAPTSNLVI VSKGGTPQLA YAVNFNFLSP APGNWTYMVD ARDGKIIEKF NELDQAKQGP
     SVTGTATTGS GKGVLGATRT LNTTFSSNSY YLQDSTRGNG IFTYDAKNRQ QVPGALWVDA
     DNQLFTTYDA PAVDAHYYVG VTYDFYKNVF GRNSYDNKGA TLKSTVHYGR SYNNAFWNGS
     QMVYGDGDGQ TFVPLSGALD VTAHELTHAV TEYTAGLVYQ NESGAINEAV SDIFGTLAEI
     WANDNPDWEI GEDVYTPKIS GDALRSMSDP TKYGDPDHYS KRYTGTQDNG GVHTNSGIVN
     KAAYLLSQGG THYGITVQGV GSDKLGKILY RTLTQYLTAN ATFSQLRSAT VQAATDLYGS
     GSQEVKSVNQ AFDAVGVK
//
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