ID   A0A1C6UT49_9ACTN        Unreviewed;       512 AA.
AC   A0A1C6UT49;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, 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=GA0070603_2329 {ECO:0000313|EMBL:SCL57013.1};
OS   Micromonospora chersina.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47854 {ECO:0000313|EMBL:SCL57013.1, ECO:0000313|Proteomes:UP000198605};
RN   [1] {ECO:0000313|EMBL:SCL57013.1, ECO:0000313|Proteomes:UP000198605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44151 {ECO:0000313|EMBL:SCL57013.1,
RC   ECO:0000313|Proteomes:UP000198605};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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|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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FMIB01000002; SCL57013.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C6UT49; -.
DR   STRING; 47854.GA0070603_2329; -.
DR   OrthoDB; 345880at2; -.
DR   Proteomes; UP000198605; 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; 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; 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}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           29..512
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023154544"
FT   DOMAIN          57..105
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          194..340
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          343..511
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        333
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        418
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   512 AA;  52516 MW;  2E95E6217791242D CRC64;
     MRRTTLLGGL ATAALLAAAG TLPATASAAP VSTDAFTRAV AQLKAHSGSA LVADGQSFTL
     KNVQTDADGT EHVRLNRYAD GLPVLGGDTV VHLGRGNTWK GASQSLVAAP TRGAKARVSA
     ATAGRVALGA STAATRRVDG TQLVHDADAA GTTLAYEVVV GGAYADGTPS ELHVLVDATT
     GKVRDSWEGV QRDGTGNTFH SGTVTVGSTL SGSTYQLADA TRGGHKTYDL NGGTSGTGTL
     VTSASNVFGD GTLANRQTAA ADAAYGAQMT WDYYKTVHGR NGIRNDGVGA YSRVHYSSNY
     ANAFWSDSCF CMTYGDGGSG WYPLTSLDVA GHEMTHGVTS NTAGLRYSGE SGGLNEATSD
     IFGTLVEFSA ANSKDPGDYL IGEKLRSSGV PLRYMDKPSK DGSSADCWSS SVGRLDVHYS
     SGVANHFFYL LAVGSGSSSY GNSPTCNGST VTGIGNAKAG AIWYRALTRY MTSRTNYAGA
     RTASLSAAAD LYGSGSAEYN AVAAAWSAVS VN
//