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Database: UniProt
Entry: A0A0X3UT48_9ACTN
LinkDB: A0A0X3UT48_9ACTN
Original site: A0A0X3UT48_9ACTN 
ID   A0A0X3UT48_9ACTN        Unreviewed;       457 AA.
AC   A0A0X3UT48;
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=Zinc protease {ECO:0000313|EMBL:KUL35771.1};
GN   ORFNames=ADL15_13460 {ECO:0000313|EMBL:KUL35771.1};
OS   Actinoplanes awajinensis subsp. mycoplanecinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=135947 {ECO:0000313|EMBL:KUL35771.1, ECO:0000313|Proteomes:UP000053244};
RN   [1] {ECO:0000313|EMBL:KUL35771.1, ECO:0000313|Proteomes:UP000053244}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16712 {ECO:0000313|EMBL:KUL35771.1,
RC   ECO:0000313|Proteomes:UP000053244};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:KUL35771.1}.
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DR   EMBL; LLZH01000097; KUL35771.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0X3UT48; -.
DR   Proteomes; UP000053244; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:KUL35771.1};
KW   Protease {ECO:0000313|EMBL:KUL35771.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053244}.
FT   DOMAIN          48..195
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          202..380
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   457 AA;  49116 MW;  712DC3FEABBC1600 CRC64;
     MTANNRGPAE RPARVATPSN HPAAALKRMK TSILQDGVRR TVLPSGLRII TEVIPHTRSA
     ALGIWVGIGS RDETPAMSGA SHFLEHLLFK GTHKRTAMEI SSEIEAVGGE TNAFTTKEYT
     CYYARVLDSD LSLAVDVLVD AVADSLLEPA DVETERGVIL EEIAMHEDEP GDEVHDIFAE
     AIYGSHPLGR LISGTPESVT PMTRNQIDSF YRRRYKAPEV VVAAAGNLDH ATVVRLVRKA
     LAGSPLDTGD AAPAKPRAAD KRVRVLKPQN VVVHRDTEQA HIVLGGAGMS RYDERRFAMG
     VLNNVLGGGM SSRLFQEIRE KRGLAYSVYS YAAQYADSGL FGVYAGCAPG KAGEVLDLIR
     TELERVAESG ITPDELVRGK GMVKGSYVLG LEDTGSRMSR LAKSELLHGD LMGVDELLGR
     VDAVTLADVG QVAADLLTRK HSLAVVGPFD EGAFPPG
//
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