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Database: UniProt
Entry: A0A0M8VIV8_9ACTN
LinkDB: A0A0M8VIV8_9ACTN
Original site: A0A0M8VIV8_9ACTN 
ID   A0A0M8VIV8_9ACTN        Unreviewed;       573 AA.
AC   A0A0M8VIV8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=ADK64_17585 {ECO:0000313|EMBL:KOV64267.1};
OS   Streptomyces sp. MMG1121.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1415544 {ECO:0000313|EMBL:KOV64267.1, ECO:0000313|Proteomes:UP000037687};
RN   [1] {ECO:0000313|Proteomes:UP000037687}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MMG1121 {ECO:0000313|Proteomes:UP000037687};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-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|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:KOV64267.1}.
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DR   EMBL; LGDV01000186; KOV64267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8VIV8; -.
DR   STRING; 1415544.ADK64_17585; -.
DR   PATRIC; fig|1415544.3.peg.3769; -.
DR   Proteomes; UP000037687; 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; 3.10.450.490; -; 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   Cell projection {ECO:0000313|EMBL:KOV64267.1};
KW   Cilium {ECO:0000313|EMBL:KOV64267.1};
KW   Flagellum {ECO:0000313|EMBL:KOV64267.1};
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:UP000037687};
KW   Secreted {ECO:0000256|RuleBase:RU366073};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          49..88
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          110..169
FT                   /note="PepSY"
FT                   /evidence="ECO:0000259|Pfam:PF03413"
FT   DOMAIN          225..376
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          395..563
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        370
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        466
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   573 AA;  60129 MW;  B572ACF0DA26E197 CRC64;
     MAGTAFAGPD TGVERSAASA DTNATTVVTA ARTAAFAHAS ATGVSQGDEL HAQDVMIDPE
     GARHVRFVRT HNSLPVLGGD LVVHLDRKLA YTGVTRAADH AVEPAGRARL TADQAAAKAA
     QVAKGDAGTA QLVVDARGGS SALAYQVAVT DEQGTSTVVV DAVTGKVRSN TPDSDEFLSP
     KVLDNLRKHG ETADPATGTA AADPAAGLLG SGVSGVTKYP SAAKGTGKTL YVGSVGLTTT
     ATSKGHYQLK DPSRYGTETR DAKGSTTEKF SAGAKFTSTT DVWGNGATSS RASAAADAQY
     GITKTLDFYK NTFGRKGIAN NSKAAQGMVH WGSKVANAFW DPTCNCMLYG DGDGKTFKKP
     LVVLDVTGHE LTHGVVDATA KLEPTYVDPN GNQYGEPGAL NESLADIFGS NVEFYANNKK
     DTPDYLIGEK LGLAQKFLRR LDHPSLDKLE GTIDYWSPDT YYTEVHAGSG VSSHAYYLLA
     EGSGKKTING VAYDSPTYNH STVKGIGRTK ATAIFYRALT RYMVSTTDFH DARKATLQAA
     KDLYGANSTE YKTVDKAWAA VDVTVANTPA ARH
//
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