ID T2SKG0_HELPX Unreviewed; 444 AA.
AC T2SKG0;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Protease {ECO:0000313|EMBL:EQD92740.1};
GN ORFNames=L932_06015 {ECO:0000313|EMBL:EQD92740.1};
OS Helicobacter pylori PZ5026.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1337392 {ECO:0000313|EMBL:EQD92740.1, ECO:0000313|Proteomes:UP000015722};
RN [1] {ECO:0000313|EMBL:EQD92740.1, ECO:0000313|Proteomes:UP000015722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PZ5026 {ECO:0000313|EMBL:EQD92740.1,
RC ECO:0000313|Proteomes:UP000015722};
RX PubMed=24051318;
RA Sheh A., Piazuelo M.B., Wilson K.T., Correa P., Fox J.G.;
RT "Draft Genome Sequences of Helicobacter pylori Strains Isolated from
RT Regions of Low and High Gastric Cancer Risk in Colombia.";
RL Genome Announc. 1:e00736-13(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:EQD92740.1}.
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DR EMBL; ASYT01000145; EQD92740.1; -; Genomic_DNA.
DR RefSeq; WP_021173337.1; NZ_ASYT01000145.1.
DR AlphaFoldDB; T2SKG0; -.
DR PATRIC; fig|1337392.3.peg.738; -.
DR Proteomes; UP000015722; 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: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:EQD92740.1};
KW Protease {ECO:0000313|EMBL:EQD92740.1}; 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_5004604937"
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; 50295 MW; 921E6026E4B35D77 CRC64;
MRYFSVKRLL GLSSVLLVTL GASMHAQSYL PKHESVTLKN GLQVVSVPLE NKTGVIEVDV
LYKVGSRNEV MGKSGIAHML EHLNFKSTKN LKAGEFDKIV KRFGGVSNAS TSFDITRYFI
KTSQANLDKS LELFAETMGS LNLKEDEFLP ERQVVAEERR WRTDNSPIGM LYFRFFNTAY
VYHPYHWTPI GFMDDIQNWT LKDIKKFHSL YYQPKNAIVL VVGDVNSQKV FELTKKHFES
LKNLDEKAIP TPYMKEPKQD GARTAVVHKD GVHLEWVALG YKVPAFKHKD QVALDALSKL
LGEGKSSWLQ SELVDKKRLA SQAFSHNMQL QDESVFLFIA GGNPNIKAEA LQKEIVALLE
KLKKGEITQA ELDKIKINQK ADFISNLESS GDVAGLFADY LVQNDLQGLT DYQQQFLDLK
VSDLVRVANE YFKDAQSTTV FLKP
//
