ID A0A101NCX7_9ACTN Unreviewed; 551 AA.
AC A0A101NCX7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN ORFNames=AQI94_03020 {ECO:0000313|EMBL:KUM90780.1};
OS Streptomyces pseudovenezuelae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM90780.1, ECO:0000313|Proteomes:UP000053039};
RN [1] {ECO:0000313|EMBL:KUM90780.1, ECO:0000313|Proteomes:UP000053039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM90780.1,
RC ECO:0000313|Proteomes:UP000053039};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces pseudovenezuelae DSM 40212, type
RT strain for the species Streptomyces pseudovenezuelae.";
RL Submitted (OCT-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|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:KUM90780.1}.
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DR EMBL; LMWM01000003; KUM90780.1; -; Genomic_DNA.
DR RefSeq; WP_031047027.1; NZ_KQ948144.1.
DR AlphaFoldDB; A0A101NCX7; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000053039; 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 InterPro; IPR006311; TAT_signal.
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.
DR PROSITE; PS51318; TAT; 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..39
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 40..551
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5023151073"
FT DOMAIN 70..112
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 215..372
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 375..550
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT ACT_SITE 365
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 453
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 551 AA; 57425 MW; 00454472251EA2B2 CRC64;
MSRIRPYVRG ARSRRLATAG VAATAATLLA AALSPAAGAA DRPTRATALE NAASVLSDRA
SALGLTSAQD TKVRDVIVDP DGTQHVRYDR TYRQLPVLGG DFVVHLAPDG AYKGSSRATR
SAISLAGITP ALSAPKAADL AANALKAANL GETLKKLTAK PRLVVDALHG APKLAWQTDA
VAQDALGNPV ARTVLTDART GAQIDAWDSI EQAAGDGKSL YSGTVSLETT QSGSAYQLKD
ATRGNTYTGD AANKTDLCFL TICLSRAPAT LFTDADNHWG TGASSDRATA AVDAQYGTDV
TWDYYKKVHG RNGIGGDGKG SYNRVHYGNN YNNAFWDDSC FCMTYGDGDG TQLGPLVSLD
VAGHEMSHGV TSKTAALTYS GESGGLNEAT SDIFGTLVEF YAGNSSDVGD YLIGEKIVRS
GFGRDALRYM DKPSKDGKSA DSWSSSVGNL DVHYSSGVAN HFAYLLAEGS GAKTVNGVSY
NSPTSNGSTV TGIGRDKLGA IWYRALTVYM TSSTNYAGAR TATLNAAKDL YGAGSTEYNA
VGAAWSAVNV N
//
