ID A0A0A8ENN9_9ACTN Unreviewed; 433 AA.
AC A0A0A8ENN9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Peptidase M50 {ECO:0000313|EMBL:AJC55666.1};
GN ORFNames=GZL_03080 {ECO:0000313|EMBL:AJC55666.1};
OS Streptomyces sp. 769.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1262452 {ECO:0000313|EMBL:AJC55666.1, ECO:0000313|Proteomes:UP000031113};
RN [1] {ECO:0000313|EMBL:AJC55666.1, ECO:0000313|Proteomes:UP000031113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=769 {ECO:0000313|EMBL:AJC55666.1,
RC ECO:0000313|Proteomes:UP000031113};
RA Du Q., Wang Q., Li Q., Wang L., Zhang Z., Ren J., Wang J., Wang M.;
RT "Complete Genome Sequence of Streptomyces gongzhulingensis.";
RL Submitted (DEC-2012) 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}.
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DR EMBL; CP003987; AJC55666.1; -; Genomic_DNA.
DR RefSeq; WP_039632311.1; NZ_CP003987.1.
DR AlphaFoldDB; A0A0A8ENN9; -.
DR KEGG; stre:GZL_03080; -.
DR HOGENOM; CLU_025778_1_2_11; -.
DR Proteomes; UP000031113; Chromosome.
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; 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 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 Protease {ECO:0000256|ARBA:ARBA00022670};
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 7..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..151
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"
FT DOMAIN 180..228
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF17820"
SQ SEQUENCE 433 AA; 46758 MW; DB237C4CC459D2BE CRC64;
MTTWMTILGI VVFVVGLLFS IAWHELGHLT TAKMFGIRVP QYMVGFGPTL FSRKKGDTEY
GVKAVPLGGY IRMIGMFPPG DDGKLQARST SPFRGMIEDA RSAAFEELQP GDEHRLFYTR
KPWKRVIVMF AGPFMNLVLA VVIFMSVLMG FGINTQTTQV GSVSDCVISA SAKTDKCPAG
AKDSPAKAAG LRAGDKIVTF NGRAVPDWGT LQEQIRRTTG PATLVVERHG AKVTLQADLI
ENKVARTDGH GGYVPGEYVT AGFLGFTPAS GIVQQTFGQS VDRMGNMVTQ GVQSLVQVPG
KIPDLWNAVF NGAERKQDSP MGVVGAARVG GEVFSLHIPP EQRVATMLFL VAGFNLSLFL
FNMLPLLPLD GGHIAGALWE SLRRAFAKVV RRPDPGPFDV AKLMPIAYVV AGIFICFTLL
VLVADVVNPV KLT
//
