ID A0A2A3I3P3_9ACTN Unreviewed; 548 AA.
AC A0A2A3I3P3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=BX265_2499 {ECO:0000313|EMBL:PBC77743.1};
OS Streptomyces sp. TLI_235.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1938860 {ECO:0000313|EMBL:PBC77743.1, ECO:0000313|Proteomes:UP000218662};
RN [1] {ECO:0000313|EMBL:PBC77743.1, ECO:0000313|Proteomes:UP000218662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TLI_235 {ECO:0000313|EMBL:PBC77743.1,
RC ECO:0000313|Proteomes:UP000218662};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2017) 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:PBC77743.1}.
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DR EMBL; NSGV01000001; PBC77743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3I3P3; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000218662; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000218662};
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..30
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 31..548
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023144239"
FT DOMAIN 68..115
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 224..369
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 373..547
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 363
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 450
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 548 AA; 56133 MW; 05EBD8D302963BA4 CRC64;
MKRKLTVGAV LSASAVLASA IQVSAGIAQA SPAPVAHVAP GQQRAALIAQ AGTEAPAAAR
ALGLSGQEQL VVKDAVVDAD GTRHVRYERT FAGLPVLGGD LVVHQDAKGS VKSVDRAVQG
SVAPASLTPK LSAAQAAAKA HGAVAATVGV AKDADEAALT SVAAPANGKL VVWAASGKPR
LAYQTTVEGL RADGTPSRQL LVTDAASGEV LSSHEQVQTA NAAGTGQGVF VGSVALTTNY
TGSTYQLKDA TRGGQYTTTL NNKTNGSGTL LTDADNAWGT GLVSSSQSAA VDAQYGAAAT
WDFYKNTFGR LGIKNNGVGA YSRVHYGRNY VNAFWDDSCF CMTYGDGASN THPLTELDVA
GHEMSHGVTA NTAGLNYSGE SGGLNEATSD IFGTGVEFYA NLASDKPDYL IGELININGD
GTPLRYMDKP SKDGGSADSW SSGVGSLDVH YSSGVGNHFF YLLAEGSGAK TINGVSYNSP
TSNGSTVTGI GRDKALQVWY RALSVYMTST TNYKGARTAT LNAATDLYGA TSTEYAQVAA
AWAAVNVN
//
