PPQQE_HELPY
ID PPQQE_HELPY Reviewed; 444 AA.
AC O25656;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Zinc protease PqqE {ECO:0000303|PubMed:33970782};
DE EC=3.4.24.- {ECO:0000269|PubMed:33970782};
DE Flags: Precursor;
GN Name=pqqE {ECO:0000303|PubMed:33970782};
GN OrderedLocusNames=HP_1012 {ECO:0000312|EMBL:AAD08056.1};
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 43504 / NCTC 11637 / JCM 7653 / RPH 13487;
RX PubMed=17533641; DOI=10.1002/pmic.200600875;
RA Smith T.G., Lim J.M., Weinberg M.V., Wells L., Hoover T.R.;
RT "Direct analysis of the extracellular proteome from two strains of
RT Helicobacter pylori.";
RL Proteomics 7:2240-2245(2007).
RN [3]
RP FUNCTION AS A PROTEASE, CATALYTIC ACTIVITY, ACTIVITY REGULATION, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 78-HIS--HIS-82.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=33970782; DOI=10.1080/19490976.2021.1921928;
RA Marques M.S., Costa A.C., Osorio H., Pinto M.L., Relvas S.,
RA Dinis-Ribeiro M., Carneiro F., Leite M., Figueiredo C.;
RT "Helicobacter pylori PqqE is a new virulence factor that cleaves junctional
RT adhesion molecule A and disrupts gastric epithelial integrity.";
RL Gut Microbes 13:1-21(2021).
CC -!- FUNCTION: Virulence factor that cleaves the cytoplasmic domain of the
CC human junctional adhesion molecule A (JAM-A), compromising gastric
CC epithelial barrier function and cell-cell adhesion (PubMed:33970782).
CC Cleavage of JAM-A occurs after Ala-285 or, to a lesser extent, before
CC Ala-285 (PubMed:33970782). {ECO:0000269|PubMed:33970782}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P10507};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P10507};
CC -!- ACTIVITY REGULATION: Can function alone, but full activity requires the
CC presence of the non-peptidase homolog YmxG.
CC {ECO:0000269|PubMed:33970782}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17533641}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted.
CC {ECO:0000269|PubMed:33970782}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR EMBL; AE000511; AAD08056.1; -; Genomic_DNA.
DR PIR; D64646; D64646.
DR RefSeq; NP_207802.1; NC_000915.1.
DR RefSeq; WP_000680224.1; NC_018939.1.
DR AlphaFoldDB; O25656; -.
DR SMR; O25656; -.
DR DIP; DIP-3200N; -.
DR IntAct; O25656; 7.
DR MINT; O25656; -.
DR STRING; 85962.C694_05240; -.
DR PaxDb; O25656; -.
DR DNASU; 899547; -.
DR EnsemblBacteria; AAD08056; AAD08056; HP_1012.
DR KEGG; hpy:HP_1012; -.
DR PATRIC; fig|85962.47.peg.1091; -.
DR eggNOG; COG0612; Bacteria.
DR OMA; FFEHLLF; -.
DR PhylomeDB; O25656; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 2.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Secreted; Signal; Virulence; Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..444
FT /note="Zinc protease PqqE"
FT /evidence="ECO:0000255"
FT /id="PRO_5004157810"
FT ACT_SITE 81
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT MUTAGEN 78..82
FT /note="HMLEH->QMLQL: Exhibits very low activity."
FT /evidence="ECO:0000269|PubMed:33970782"
FT MUTAGEN 78..82
FT /note="Missing: Loss of activity."
FT /evidence="ECO:0000269|PubMed:33970782"
SQ SEQUENCE 444 AA; 50331 MW; 3A6092EF0792EAB2 CRC64;
MKHFSVKRLL GLSSVLLVTL GASMHAQSYL PKHESVTLKN GLQVVSVPLE NKTGVIEVDV
LYKVGSRNET MGKSGIAHML EHLNFKSTKN LKAGEFDKIV KRFGGVSNAS TSFDITRYFI
KTSQANLDKS LELFAETMGS LNLKEDEFLP ERQVVAEERR WRTDNSPIGM LYFRFFNTAY
VYHPYHWTPI GFMDDIQNWT LKDIKKFHSL YYQPKNAIVL VVGDVNSQKV FELSKKHFES
LKNLDEKAIP TPYMKEPKQD GARTAVVHKD GVHLEWVALG YKVPAFKHKD QVALDALSRL
LGEGKSSWLQ SELVDKKRLA SQAFSHNMQL QDESVFLFIA GGNPNVKAEA LQKEIVALLE
KLKKGEITQA ELDKLKINQK ADFISNLESS SDVAGLFADY LVQNDIQGLT DYQRQFLDLK
VSDLVRVANE YFKDTQSTTV FLKP
