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Database: UniProt
Entry: J0RZZ9_HELPX
LinkDB: J0RZZ9_HELPX
Original site: J0RZZ9_HELPX 
ID   J0RZZ9_HELPX            Unreviewed;       444 AA.
AC   J0RZZ9;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Peptidase M16 inactive domain protein {ECO:0000313|EMBL:EJC28766.1};
GN   ORFNames=HPHPH5B_0541 {ECO:0000313|EMBL:EJC28766.1};
OS   Helicobacter pylori Hp H-5b.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=992092 {ECO:0000313|EMBL:EJC28766.1, ECO:0000313|Proteomes:UP000003365};
RN   [1] {ECO:0000313|EMBL:EJC28766.1, ECO:0000313|Proteomes:UP000003365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hp H-5b {ECO:0000313|EMBL:EJC28766.1,
RC   ECO:0000313|Proteomes:UP000003365};
RX   PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA   Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA   Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA   Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT   "Genome sequences of 65 Helicobacter pylori strains isolated from
RT   asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT   disease, or gastritis.";
RL   Pathog. Dis. 68:39-43(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:EJC28766.1}.
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DR   EMBL; AKQF01000002; EJC28766.1; -; Genomic_DNA.
DR   RefSeq; WP_000680253.1; NZ_AKQF01000002.1.
DR   AlphaFoldDB; J0RZZ9; -.
DR   PATRIC; fig|992092.3.peg.524; -.
DR   Proteomes; UP000003365; Unassembled WGS sequence.
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:InterPro.
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   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_5003738787"
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;  50400 MW;  10C3021E54C2226E CRC64;
     MKHFSVKRLL RLSSVLLVTL GASMHAQSYL PKHESVTLKN GLQVVSVPLE NKTGVIEVDV
     LYKVGSRNEV MGKSGIAHML EHLNFKSTKN LKAGEFDKIV KRFGGVSNAS TSFDITRYFI
     KTSQANLDKS LELFAETMGS LNLKEDEFLP ERQVVAEERR WRTDNSPIGM LYFRFFNTAY
     VYHPYHWTPI GFMDDIQNWT LKDIKKFHSL YYQPKNAIIL VVGDVNSQKV FELSKKHFES
     LKNLDEKAIP TPYMKEPKQD GARTAVVHKD GVHLEWVALG YKVPAFKHKD QVALDALSKL
     LGEGKSSWLQ SELVDKKRLA SQAFSHNMQL QDESVFLFIA GGNPNIKAEA LQKEIVALLE
     KLKKGEITQA ELDKIKINQK ADFISNLESS SDVAGLFADY LVQNDLQGLT DYQQQFLDLK
     VSDLVRVANE YFKDTQSTTV FLKP
//
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