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Database: UniProt
Entry: A0A2V4NJX5_9ACTN
LinkDB: A0A2V4NJX5_9ACTN
Original site: A0A2V4NJX5_9ACTN 
ID   A0A2V4NJX5_9ACTN        Unreviewed;       446 AA.
AC   A0A2V4NJX5;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:PYC86157.1};
GN   ORFNames=C7C46_05845 {ECO:0000313|EMBL:PYC86157.1};
OS   Streptomyces tateyamensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=565073 {ECO:0000313|EMBL:PYC86157.1, ECO:0000313|Proteomes:UP000248039};
RN   [1] {ECO:0000313|EMBL:PYC86157.1, ECO:0000313|Proteomes:UP000248039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 21389 {ECO:0000313|EMBL:PYC86157.1,
RC   ECO:0000313|Proteomes:UP000248039};
RA   Schwalen C.J., Hudson G.A., Mitchell D.A.;
RT   "Bioinformatic expansion and discovery of thiopeptide antibiotics.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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:PYC86157.1}.
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DR   EMBL; PYBW01000020; PYC86157.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2V4NJX5; -.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000248039; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248039};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          30..168
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          188..367
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   446 AA;  48499 MW;  CC6D31666B7B643A CRC64;
     MANPAAEATS TGGTGAPIAI TEHRLANGLR VVLSEDHLTP VAAVCLWYDV GSRHEVKGRT
     GLAHLFEHLM FQGSANVSGN GHFELVQGAG GSLNGTTSFE RTNYFETMPA HQLELALWLE
     ADRMGSLLAA LDETSMENQR DVVKNERRQR YDNVPYGTAL EKLTALAYPE GHPYHHTPIG
     SMADLDAATL ADAQEFFRTY YAPNNAVLSV VGDIDLEQTI AWVEKYFGSI PEHHGKQPPR
     DGTLPDTMGG ELREELHEEV PSRALMSAYR LPHDGTREAD AADLALTVLG SGESSRLYNR
     LVRRDRTAVS AGFGLLRLAG APSLGWLDVK SSGEATIAQI DQAIDEELAR FAADGPTAEE
     LERAQAQIER EWLDRLTTVA GRADELCRYA VLFGDPKLVN GALGRVLDVT ADEVRAVAAA
     RLRPDNRAVL VYEPTTDATE TEEDAA
//
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