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Database: UniProt
Entry: A0A0M8WM89_9ACTN
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ID   A0A0M8WM89_9ACTN        Unreviewed;       434 AA.
AC   A0A0M8WM89;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Zinc metalloprotease {ECO:0000313|EMBL:KOV86423.1};
GN   ORFNames=ADL01_06780 {ECO:0000313|EMBL:KOV86423.1};
OS   Streptomyces sp. NRRL WC-3618.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1519490 {ECO:0000313|EMBL:KOV86423.1, ECO:0000313|Proteomes:UP000037738};
RN   [1] {ECO:0000313|EMBL:KOV86423.1, ECO:0000313|Proteomes:UP000037738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3618 {ECO:0000313|EMBL:KOV86423.1,
RC   ECO:0000313|Proteomes:UP000037738};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family.
CC       {ECO:0000256|ARBA:ARBA00007931}.
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:KOV86423.1}.
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DR   EMBL; LGDW01000044; KOV86423.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M8WM89; -.
DR   PATRIC; fig|1519490.3.peg.1492; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000037738; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00989; PDZ_metalloprotease; 1.
DR   CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000313|EMBL:KOV86423.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KOV86423.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037738};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   TRANSMEM        126..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        407..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          149..231
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   434 AA;  46631 MW;  9F9AB630F88DA1FF CRC64;
     MTALMMILGI VVFVIGLLVS IAWHELGHLS TAKLFGIRVP QYMVGFGPTI WSRNKGETEY
     GIKAIPFGGY IRMIGMFPPG PDGRIEARST SPWRGMIEDA RAQSYEELLP GDEKRLFYTR
     KPWKRVIVMF AGPFMNLILA VALFLTVLMG FGVSQQTTSV SSVSKCVIAQ SQGRDDCRKT
     DAASPAAAAG LKAGDKILSF GGVQVDTWNR LSDEIRANPG KEVAIVVERK GADVTLHAKI
     ATNQVAKKDS SGQIVKGKYV TAGFLGFSAA SGIVRQDFGD SLTWMGDRMG EAVDSIASLP
     GKIPALWNAA FDGGERAADS PMGVVGAARV GGEIFTLDIP PTQQLAMALM LVAGFNLSLF
     LFNMLPLLPL DGGHVAGALW ESLRRNLARV LKRPDPGPFD VAKLMPVAYV VAGIFICFTL
     LVLVADVVNP VRIS
//
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