ID A0A1Q4WAQ5_9ACTN Unreviewed; 433 AA.
AC A0A1Q4WAQ5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Zinc metalloprotease {ECO:0000313|EMBL:OKI07161.1};
GN ORFNames=A6A06_36290 {ECO:0000313|EMBL:OKI07161.1};
OS Streptomyces sp. CB02923.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKI07161.1, ECO:0000313|Proteomes:UP000185893};
RN [1] {ECO:0000313|EMBL:OKI07161.1, ECO:0000313|Proteomes:UP000185893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02923 {ECO:0000313|EMBL:OKI07161.1,
RC ECO:0000313|Proteomes:UP000185893};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI07161.1}.
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DR EMBL; LWKZ01000005; OKI07161.1; -; Genomic_DNA.
DR RefSeq; WP_073760740.1; NZ_LWKZ01000005.1.
DR AlphaFoldDB; A0A1Q4WAQ5; -.
DR STRING; 1718985.A6A06_36290; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000185893; 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:OKI07161.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OKI07161.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185893};
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 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..153
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 149..230
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 433 AA; 46892 MW; 52EA8CE18A1140F2 CRC64;
MTTWMTILGI VVFVVGLLFS IAWHELGHLS TAKLFGIRVP QYMVGFGPTL FSRRKGDTEY
GIKAIPLGGY IRMIGMFPPG EDGALQARST SPWRGMIEDA RSAAFEELQP GDDKRLFYTR
KPWKRVIVMF AGPFMNLVLA VVIFMSVLMG FGINTQTTQV SSVSDCVIAA SAKTDKCTAG
AKDSPAKAAG LRAGDKIVDF DGKPVPDWSA LQQSIRDTTG PATITIERDG KRQQLHADLI
ENKVAKTDGH GAYVPDEYVT AGFLGFTPAT GVVPQTFGQS VDRMGSMVEQ GFQSLVNLPA
KVPDLWNAAF NGGERKQDSP MGVVGAARVG GEVFSLNIPP EQRVATMLFL VAGFNLSLFL
FNMLPLLPLD GGHIAGALWE SVRRAFARVF RRPDPGPFDV AKLMPVAYVV AGIFICFTLL
VLVADVVNPV KLT
//
