ID   Y1068_CAMJE             Reviewed;         368 AA.
AC   Q9PNM6; Q0P9I6;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Putative zinc metalloprotease Cj1068;
DE            EC=3.4.24.-;
GN   OrderedLocusNames=Cj1068;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR   EMBL; AL111168; CAL35185.1; -; Genomic_DNA.
DR   PIR; G81309; G81309.
DR   RefSeq; WP_002934663.1; NC_002163.1.
DR   RefSeq; YP_002344461.1; NC_002163.1.
DR   AlphaFoldDB; Q9PNM6; -.
DR   SMR; Q9PNM6; -.
DR   STRING; 192222.Cj1068; -.
DR   PaxDb; Q9PNM6; -.
DR   PRIDE; Q9PNM6; -.
DR   EnsemblBacteria; CAL35185; CAL35185; Cj1068.
DR   GeneID; 905359; -.
DR   KEGG; cje:Cj1068; -.
DR   PATRIC; fig|192222.6.peg.1050; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_1_0_7; -.
DR   OMA; QYMVGFG; -.
DR   Proteomes; UP000000799; 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; 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   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; SSF50156; 1.
DR   TIGRFAMs; TIGR00054; TIGR00054; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   CHAIN           1..368
FT                   /note="Putative zinc metalloprotease Cj1068"
FT                   /id="PRO_0000088434"
FT   TRANSMEM        112..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          126..197
FT                   /note="PDZ"
FT   ACT_SITE        37
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   368 AA;  40960 MW;  E85582F73955B898 CRC64;
     MRSLLLLIVI LILGIKFYSI EFLATVLVIS FLIFFHELGH FLAARSLGVK VEVFSIGFGK
     SLIEREFKGT NYRLSTLPLG GYVKLKGQDD MRPGFENLDK DSYSILSPLK KIYILFAGPF
     FNLILAFFLY IIIGNLGLNK LAPQIGNIAP NSAAQEIGLQ KNDTILEING IRIQTFDEIS
     KHLSLDPLKI LINREGKNLE FILTPKIGQG YNDFGQIVEK PQLGVSPNGT STLVKHQGLE
     SFKYAAQESF QASTLIIKGI VKLISGEVEA KNLGGIITMT EITSKAAQNS FTLLLFITAL
     ISINLGILNL LPIPMLDGGH ILFNLYEMIF RRKVPQRTFE YLSYTGMAIL LSLMLFATYN
     DISRIIGE