ID A0A0W7X6D4_9ACTN Unreviewed; 433 AA.
AC A0A0W7X6D4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Zinc metalloprotease {ECO:0000313|EMBL:KUF18502.1};
GN ORFNames=AT728_19375 {ECO:0000313|EMBL:KUF18502.1};
OS Streptomyces silvensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1765722 {ECO:0000313|EMBL:KUF18502.1, ECO:0000313|Proteomes:UP000054804};
RN [1] {ECO:0000313|EMBL:KUF18502.1, ECO:0000313|Proteomes:UP000054804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53525 {ECO:0000313|EMBL:KUF18502.1,
RC ECO:0000313|Proteomes:UP000054804};
RA Johnston C.W., Li Y., Magarvey N.A.;
RT "Draft genome sequence of Streptomyces silvensis ATCC 53525, a producer of
RT novel hormone antagonists.";
RL Submitted (DEC-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:KUF18502.1}.
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DR EMBL; LOCL01000030; KUF18502.1; -; Genomic_DNA.
DR RefSeq; WP_058847412.1; NZ_LOCL01000030.1.
DR AlphaFoldDB; A0A0W7X6D4; -.
DR STRING; 1765722.AT728_19375; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000054804; 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; 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; PF02163; Peptidase_M50; 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:KUF18502.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KUF18502.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054804};
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..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 406..427
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..386
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 433 AA; 46931 MW; 5FCB35DA9BFE2DAA CRC64;
MTTLMMILGI VVFVVGLLFS IAWHELGHLS TAKMFGIRVP QYMVGFGPTL FSRKRGDTEY
GVKAIPLGGY IRMIGMFPPG PDGRIEARST SPWRGMIEDA RSAAFEELKP GDESRLFYTR
KPWKRVIVMF AGPFMNLILA VVIFLGVMMT FGISTQTTSV GKVSDCVIEA GQNRSTCEKG
DKPAPAKAAG LKAGDKIVAF QGKPVGDWSA LQTRIRETVG PATITVERAG ERLDLHANLI
KNQVSKTDGE GGYVEGKYVY AGFLGFTPAS GIVQQSFGES VDRMGTMMEN GVESIIALPS
KVPDLWNAAF GDGDRKQDSP MGVVGAARVG GEVFTLDIPP ENQIAMMLFL LAGFNLSLFL
FNMLPLLPLD GGHIAGALWE SLRRNVAKVF RRPDPGPFDV AKLMPVAYVV AGIFICFTIL
VLIADVVNPV RIS
//
