ID A0A069K052_9ACTN Unreviewed; 683 AA.
AC A0A069K052;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=DT87_21145 {ECO:0000313|EMBL:KDQ69605.1};
OS Streptomyces sp. NTK 937.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ69605.1, ECO:0000313|Proteomes:UP000027475};
RN [1] {ECO:0000313|EMBL:KDQ69605.1, ECO:0000313|Proteomes:UP000027475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ69605.1,
RC ECO:0000313|Proteomes:UP000027475};
RA Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT producer of the benzoxazol antibiotic caboxamycin.";
RL Submitted (APR-2014) 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 -!- 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:KDQ69605.1}.
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DR EMBL; JJOB01000001; KDQ69605.1; -; Genomic_DNA.
DR RefSeq; WP_037879569.1; NZ_JJOB01000001.1.
DR AlphaFoldDB; A0A069K052; -.
DR MEROPS; M04.017; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000027475; 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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
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; PF01483; P_proprotein; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS51829; P_HOMO_B; 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..33
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 34..683
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023019018"
FT DOMAIN 564..683
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
FT ACT_SITE 372
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 459
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 683 AA; 70170 MW; FB9F5F0B3968D841 CRC64;
MRSTPSRRAT ATGALITAAA LLAVGVQTNG ATAAPVSGTA APAAAVKGAD PGALPAQLSP
SQRAELIRQA GATTAATAEE LGLGAKEKLV VRDVVQDVDG TTHTRYERTL DGLPVLGGDL
VVAESKAGKT EGVTKASKAT TAQLKAVSTA ADIAPAAAEK QALTAAKADG SKSTEASKAP
RKVVWLASGT PQLAYETVVG GLQHDGTPNE LHVITDAASG AKLYEWQAIE NGTGNTQYSG
TVTLGTSGSG SSYNLTDTGR GNHKTYNLNN GTSSGTGTLF SGPDDIWGNG NPTNVETAAA
DAHYGAAETW DFYKNVMGRT GIRGDGVGAY SRVHYGNSYV NAFWSDSCFC MTYGDGSGNK
APLTSLDVAA HEMTHGVTSN TAGLNYSGES GGLNEATSDI FATGVEFYSN TATDPGDYLI
GEKIDINGNG TPLRYMDKPS KDGASKDSWY SGLGSIDVHY SSGPANHFFY LLSEGSGAKT
VNGVAYNSPT SDGLPVTGIG RDKALQIWYK ALTTKFTSTT NYAAARTGTL AVAGELYGTG
STEYAGVANA WAAINVGSRP GGSTDPEPGG TVFQNTTKKA LVDRGTTTIP VVVSGVTGNA
PSNLSVAVDI SHTWRGDLVL DLVAPDGTAF RLKNSSLSDS ADNVVETYTV NASAKAANGT
WNLRIQDVYS GDTGTFNSVK LTF
//
