ID Q0PA85_CAMJE Unreviewed; 416 AA.
AC Q0PA85;
DT 19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 19-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Zinc protease {ECO:0000313|EMBL:CAL34933.1};
GN OrderedLocusNames=Cj0805 {ECO:0000313|EMBL:CAL34933.1};
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222 {ECO:0000313|EMBL:CAL34933.1, ECO:0000313|Proteomes:UP000000799};
RN [1] {ECO:0000313|EMBL:CAL34933.1, ECO:0000313|Proteomes:UP000000799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000313|Proteomes:UP000000799};
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K., Ketley J.M., Churcher C., Basham D.,
RA Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K.,
RA Karlyshev A., Moule S., Pallen M.J., Penn C.W., Quail M., Rajandream M.A.,
RA Rutherford K.M., VanVliet A., Whitehead S., 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 -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; AL111168; CAL34933.1; -; Genomic_DNA.
DR PIR; E81352; E81352.
DR RefSeq; WP_002852436.1; NZ_SZUC01000001.1.
DR RefSeq; YP_002344212.1; NC_002163.1.
DR AlphaFoldDB; Q0PA85; -.
DR IntAct; Q0PA85; 2.
DR STRING; 192222.Cj0805; -.
DR PaxDb; 192222-Cj0805; -.
DR EnsemblBacteria; CAL34933; CAL34933; Cj0805.
DR GeneID; 905108; -.
DR KEGG; cje:Cj0805; -.
DR PATRIC; fig|192222.6.peg.793; -.
DR eggNOG; COG0612; Bacteria.
DR HOGENOM; CLU_009902_1_0_7; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR43690; NARDILYSIN; 1.
DR PANTHER; PTHR43690:SF17; PROTEIN YHJJ; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CAL34933.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000799};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 20..131
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 170..346
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 416 AA; 48043 MW; 9A40AC42050B0DCE CRC64;
MIAYEKIQLK NKLEVYALPV NKNSDVISVD IFYKVGSRNE IMGKSGIAHM LEHLNFKSTK
NLKAGEFDEI VKGFGGVDNA STGFDYTHYY IKCAKKNLDK ALELFAELMA NLNLKDEEFQ
PERAVVLEER RWRTDNNPLG YLYFRLFNHA FMYHPYHWTP IGFFKDIENW SIEDIKEFHS
IYYQPKNAIL LVSGDIESKE VFELSKKHFE KIKNTKTIPK IHTKEPKQDG VKRIYLHKNS
DTELLALAYK IPNFKHKDIP ALNALSELLG SGKSSLMSEI LIDKLNLIND YYAYVNDCID
ENLFIFICNC NPNVNAEKVE KELLKIIDKL KMGKISQKDL QRVKNNVKSD FIFSLNNASA
VANIYGSYLA RGDINPLLNY EKDIQNLELK DLISCAKKYF IQENSTTVIL RKDSNG
//
