ID E6NQZ4_HELPQ Unreviewed; 444 AA.
AC E6NQZ4;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Putative zinc protease {ECO:0000313|EMBL:BAJ59560.1};
GN OrderedLocusNames=HPF57_0486 {ECO:0000313|EMBL:BAJ59560.1};
OS Helicobacter pylori (strain F57).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=866346 {ECO:0000313|EMBL:BAJ59560.1, ECO:0000313|Proteomes:UP000008082};
RN [1] {ECO:0000313|EMBL:BAJ59560.1, ECO:0000313|Proteomes:UP000008082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F57 {ECO:0000313|EMBL:BAJ59560.1,
RC ECO:0000313|Proteomes:UP000008082};
RX PubMed=21575176; DOI=10.1186/1471-2180-11-104;
RA Kawai M., Furuta Y., Yahara K., Tsuru T., Oshima K., Handa N.,
RA Takahashi N., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT "Evolution in an oncogenic bacterial species with extreme genome
RT plasticity: Helicobacter pylori East Asian genomes.";
RL BMC Microbiol. 11:104-104(2011).
RN [2] {ECO:0000313|EMBL:BAJ59560.1, ECO:0000313|Proteomes:UP000008082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F57 {ECO:0000313|EMBL:BAJ59560.1,
RC ECO:0000313|Proteomes:UP000008082};
RX PubMed=21212362; DOI=10.1073/pnas.1012579108;
RA Furuta Y., Kawai M., Yahara K., Takahashi N., Handa N., Tsuru T.,
RA Oshima K., Yoshida M., Azuma T., Hattori M., Uchiyama I., Kobayashi I.;
RT "Birth and death of genes linked to chromosomal inversion.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:1501-1506(2011).
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; AP011945; BAJ59560.1; -; Genomic_DNA.
DR RefSeq; WP_000680233.1; NC_017367.1.
DR AlphaFoldDB; E6NQZ4; -.
DR KEGG; hex:HPF57_0486; -.
DR PATRIC; fig|866346.4.peg.517; -.
DR HOGENOM; CLU_009902_1_0_7; -.
DR Proteomes; UP000008082; 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; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 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:0000313|EMBL:BAJ59560.1};
KW Protease {ECO:0000313|EMBL:BAJ59560.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..444
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003207741"
FT DOMAIN 57..159
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 198..377
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 444 AA; 50358 MW; 2DD63190B35CAE61 CRC64;
MKHFSVKRLL RLSSVLLVTL GASMHAQSYL PKHESITLKN GLQVVSVPLE NKTGVIEVDV
LYKVGSRNEV MGKSGIAHML EHLNFKSTKN LKAGEFDKIV KRFGGVSNAS TSFDITRYFI
KTSQANLDKS LELFAETMGS LNLKEDEFLP ERQVVAEERR WRTDNSPIGM LYFRFFNTAY
VYHPYHWTPI GFMDDIQNWT LKDIKKFHSL YYQPKNAIIL VVGDVNSQKV FELSKKHFES
LKNLDGKTIP TPYMKEPKQD GARTAVVHKD GVHLEWVALG YKVPAFKHKD QVALDALSKL
LGEGKSSWLQ SELVDKKRLA SQAFSHNMQL QDESVFLFIA GGNPNVKAEA LQKEIVALLE
KLKKGEITQA ELDKIKINQK ADFISNLESS SDVAGLFADY LVQNDIQGLT DYQQQFLDLK
VSDLVRVANE YFKDTQSTTV FLKP
//
