ID   Y1796_CLOAB             Reviewed;         339 AA.
AC   Q97I57;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Putative zinc metalloprotease CA_C1796;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=CA_C1796;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK79761.1; -; Genomic_DNA.
DR   PIR; F97121; F97121.
DR   RefSeq; NP_348421.1; NC_003030.1.
DR   RefSeq; WP_010965102.1; NC_003030.1.
DR   AlphaFoldDB; Q97I57; -.
DR   SMR; Q97I57; -.
DR   STRING; 272562.CA_C1796; -.
DR   EnsemblBacteria; AAK79761; AAK79761; CA_C1796.
DR   GeneID; 44998290; -.
DR   KEGG; cac:CA_C1796; -.
DR   PATRIC; fig|272562.8.peg.2002; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_1_3_9; -.
DR   OMA; QYMVGFG; -.
DR   OrthoDB; 1395197at2; -.
DR   Proteomes; UP000000814; 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; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   PANTHER; PTHR42837; PTHR42837; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   TIGRFAMs; TIGR00054; TIGR00054; 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..339
FT                   /note="Putative zinc metalloprotease CA_C1796"
FT                   /id="PRO_0000088438"
FT   TRANSMEM        91..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          99..177
FT                   /note="PDZ"
FT   ACT_SITE        21
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   339 AA;  36581 MW;  F426EE851B44B205 CRC64;
     MSFFNIVIAI LAFGVLILIH ELGHFVLAKL NDVKVEEFAI GMGPKLLGIK GKETQYSIRA
     LPIGGYVKML GDESKSDDPR AFNNKSSARR LSIVIAGPIM NLILAAVLFC IVGMSEGIAL
     PTVGKISANS PAQKIGIKAG DTIVKINNYS VHTWEDISFN MALNKGEGIK LALKNNGTIK
     KVTLVPQYSK KEKMYLIGIS PKFIDKPTII EGAKYGTSET VTMIKTVYLS LKMMVTGKAS
     AKDVSGPVSI IKVTGAAANA GFIRLVNFIA FISAQLGVMN LLPIPALDGG FVFLFLFQMI
     TGKKVDDDKV GFVNTIGFAL LMILMIVVTI KDVVYPINF