ID   I0ZIY8_HELPX            Unreviewed;       433 AA.
AC   I0ZIY8;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Processing zinc-metalloprotease {ECO:0000313|EMBL:EIE30607.1};
GN   ORFNames=HP17_06182 {ECO:0000313|EMBL:EIE30607.1};
OS   Helicobacter pylori NCTC 11637 = CCUG 17874 = ATCC 43504 = JCM 12093.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=102618 {ECO:0000313|EMBL:EIE30607.1, ECO:0000313|Proteomes:UP000004458};
RN   [1] {ECO:0000313|EMBL:EIE30607.1, ECO:0000313|Proteomes:UP000004458}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17874 {ECO:0000313|Proteomes:UP000004458};
RX   PubMed=22493206; DOI=10.1128/JB.00230-12;
RA   Clancy C.D., Forde B.M., Moore S.A., O'Toole P.W.;
RT   "Draft Genome Sequences of Helicobacter pylori Strains 17874 and P79.";
RL   J. Bacteriol. 194:2402-2402(2012).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EIE30607.1}.
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DR   EMBL; AIHX01000008; EIE30607.1; -; Genomic_DNA.
DR   RefSeq; WP_000722016.1; NZ_AIHX01000008.1.
DR   AlphaFoldDB; I0ZIY8; -.
DR   PATRIC; fig|102618.3.peg.75; -.
DR   Proteomes; UP000004458; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF225; NON-PEPTIDASE HOMOLOG YMXG; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EIE30607.1};
KW   Metalloprotease {ECO:0000313|EMBL:EIE30607.1};
KW   Protease {ECO:0000313|EMBL:EIE30607.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..433
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003637781"
FT   DOMAIN          53..179
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          185..359
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   433 AA;  48851 MW;  49BB38B84CB68D9F CRC64;
     MKKILITLLL GVFMGLQASA LTHQEINQAK VPVIYEENHL LPMGFIHLAF RGGGSLSDKN
     QLGLAKLFAQ VLNEGTKELG AVGFAQLLEQ KAISLNVDTS TEDLQITLEF LKEYEDEAIM
     HLKELLKSPN FTQNALEKVK TQMLAALLQK ESDFDYLAKL TLKQELFANT PLANAALGTK
     ESLQKIKLED LKQQFAKVFE LNKLVVVLGG DLKIDQTLKR LDNALNFLPQ GKAYEEPYFE
     TSDKKSEKVL YKDTEQAFVY FGAPFKIKDL KQDLAKSKVM MFVLGGGFGS RLMEKIRVQE
     GLAYSVYIRS NFSKVAHFAS GYLQTKLSTQ AKSVALVKKI VKEFIEKGMT QQELDDAKKF
     LLGSEPLRNE TISSRLNTTY NYFYLGLPLN FNQTLLDQIQ KMSLKEINDF IKAHTEINDL
     TFAIVSNKKS KDK
//