ID   Y1693_CLOPE             Reviewed;         335 AA.
AC   Q8XJR2;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Putative zinc metalloprotease CPE1693;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=CPE1693;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR   EMBL; BA000016; BAB81399.1; -; Genomic_DNA.
DR   RefSeq; WP_003466788.1; NC_003366.1.
DR   AlphaFoldDB; Q8XJR2; -.
DR   SMR; Q8XJR2; -.
DR   STRING; 195102.gene:10490957; -.
DR   EnsemblBacteria; BAB81399; BAB81399; BAB81399.
DR   KEGG; cpe:CPE1693; -.
DR   HOGENOM; CLU_025778_1_3_9; -.
DR   OMA; QYMVGFG; -.
DR   Proteomes; UP000000818; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837; PTHR42837; 1.
DR   Pfam; PF13180; PDZ_2; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   TIGRFAMs; TIGR00054; TIGR00054; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..335
FT                   /note="Putative zinc metalloprotease CPE1693"
FT                   /id="PRO_0000088439"
FT   TRANSMEM        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          96..174
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         17
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   335 AA;  36491 MW;  A99EB230F59C3797 CRC64;
     MYIIFALLAF SALILVHELG HFIVAKLNGI YVEEFAIGMG PKLFGVKVGE TEYNLRILPF
     GGFVKMLGEE DESDDSRSLN AKTPIQRILV MGAGAFMNYV LALIIFIGLA MSSGFAENKV
     ASVVPNSPAQ EIGIEQGDEF LKIDGNKIHT TDDFRMGLAL AKGNPVELEI KRGNDVLTKT
     VQPILNESGM YQVGISYALV EKPTLLQGIK QGFNETRSLV SQSFIALKTI VTGEANLKTD
     VGGPVTIIKM SGQAAKAGAN TLLWFMAFLS VQLAVFNLLP FPALDGGRIF IELIQMIIRK
     EIPAKYIEAV NTVGFMLLMG LMVLVTIKDI IFPIL