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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//