ID A0A0X3W3S1_9ACTN Unreviewed; 462 AA.
AC A0A0X3W3S1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KUL51534.1};
GN ORFNames=ADL30_27070 {ECO:0000313|EMBL:KUL51534.1};
OS Streptomyces sp. NRRL S-1521.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL51534.1, ECO:0000313|Proteomes:UP000053420};
RN [1] {ECO:0000313|EMBL:KUL51534.1, ECO:0000313|Proteomes:UP000053420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL51534.1,
RC ECO:0000313|Proteomes:UP000053420};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KUL51534.1}.
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DR EMBL; LLZK01000228; KUL51534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X3W3S1; -.
DR Proteomes; UP000053420; 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:UP000053420};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 28..162
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 186..366
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 436..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 462 AA; 50267 MW; BF44AEC7885220DF CRC64;
MPMGHTATAE PGSGGLTATE HRLANGLRVV LSEDHLTPVA AVCLWYDVGS RHEVKGRTGL
AHLFEHLMFQ GSKQVSNNGH FELVQGAGGS LNGTTSFERT NYFETMPAHQ LELALWLEAD
RMGSLLSALD EESMENQRDV VKNERRQRYD NVPYGTAFEK LTALSYPEGH PYHHTPIGSM
ADLDAATLED ARQFFRTYYA PNNAVLSVVG DIDPEQTLAW VEKYFGSIPS HDGKQPPRDG
SLPERIGKEL REVVEEEVPA RALMAAYRLP EDGTRACDAA DLALTVLGSG ESSRLYNRLV
RRDRTAVAAG FGLLRLAGAP SLGWLDVKTS GDVEVPVIEA AVDEELARFA AEGPTPEEME
RAQAQLEREW LDRLGTVAGR ADELCRYAVL FGDPQLALTA VGRVLDVTAE EVQEVAKARL
RPDNRAVLVY EPVAAGGAGE TAADGTEETA AGETEQDEEA AK
//
