ID   VACA4_HELPX             Reviewed;        1291 AA.
AC   Q48258;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Vacuolating cytotoxin autotransporter;
DE   Contains:
DE     RecName: Full=Vacuolating cytotoxin;
DE   Contains:
DE     RecName: Full=Vacuolating cytotoxin translocator;
DE   Flags: Precursor;
GN   Name=vacA;
OS   Helicobacter pylori (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=210;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=185-44;
RX   PubMed=8057855; DOI=10.1111/j.1365-2958.1994.tb01019.x;
RA   Haas R., Schmitt W.;
RT   "Genetic analysis of the Helicobacter pylori vacuolating cytotoxin:
RT   structural similarities with the IgA protease type of exported protein.";
RL   Mol. Microbiol. 12:307-319(1994).
CC   -!- FUNCTION: Induces vacuolation of eukaryotic cells. Causes ulceration
CC       and gastric lesions.
CC   -!- SUBCELLULAR LOCATION: [Vacuolating cytotoxin autotransporter]:
CC       Periplasm {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Vacuolating cytotoxin]: Secreted. Cell surface.
CC   -!- SUBCELLULAR LOCATION: [Vacuolating cytotoxin translocator]: Cell outer
CC       membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CC       Note=The cleaved C-terminal fragment (autotransporter domain) is
CC       localized in the outer membrane. {ECO:0000250}.
CC   -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC       autotransporter protein to the periplasmic space. Then, insertion of
CC       the C-terminal translocator domain in the outer membrane forms a
CC       hydrophilic pore for the translocation of the passenger domain to the
CC       bacterial cell surface, with subsequent cleavage (By similarity).
CC       {ECO:0000250}.
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DR   EMBL; Z26883; CAA81528.1; -; Genomic_DNA.
DR   PIR; S44983; S44983.
DR   AlphaFoldDB; Q48258; -.
DR   SMR; Q48258; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.130; -; 1.
DR   InterPro; IPR005546; Autotransporte_beta.
DR   InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR   InterPro; IPR006315; OM_autotransptr_brl.
DR   InterPro; IPR003842; Vacuolating_cytotoxin.
DR   Pfam; PF02691; VacA; 1.
DR   PRINTS; PR01656; VACCYTOTOXIN.
DR   SMART; SM00869; Autotransporter; 1.
DR   SUPFAM; SSF103515; SSF103515; 1.
DR   TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR   PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE   3: Inferred from homology;
KW   Cell outer membrane; Membrane; Periplasm; Secreted; Signal; Toxin;
KW   Transmembrane; Transmembrane beta strand; Virulence.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..1291
FT                   /note="Vacuolating cytotoxin autotransporter"
FT                   /id="PRO_0000387590"
FT   CHAIN           34..?
FT                   /note="Vacuolating cytotoxin"
FT                   /id="PRO_0000002720"
FT   CHAIN           ?..1291
FT                   /note="Vacuolating cytotoxin translocator"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000002721"
FT   DOMAIN          1018..1291
FT                   /note="Autotransporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT   REGION          326..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1291 AA;  139636 MW;  ECA56A61CAE36669 CRC64;
     MEIQQTHRKI NRPLVSLALV GALVSITPQQ SHAAFFTTVI IPAIVGGIAT GAAVGTVSGL
     LGWGLKQAEE ANKTPDKPDK VWRIQAGKGF NEFPNKEYDL YKSLLSSKID GGWDWGNAAR
     HYWVKDGQWN KLEVDMQNAV GTYNLSGLIN FTGGDLDVNM QKATLRLGQF NGNSFTSYKD
     SADRTTRVDF NAKNILIDNF LEINNRVGSG AGRKASSTVL TLQASEGITS RENAEISLYD
     GATLNLASNS VKLMGNVWMG RLQYVGAYLA PSYSTINTSK VTGEVNFNHL TVGDHNAAQA
     GIIASNKTHI GTLDLWQSAG LNIIAPPEGG YKDKPNDKPS NTTQNNAKND KQESSQNNSN
     TQVINPPNSA QKTEIQPTQV IDGPFAGGKN TVVNINRINT NADGTIRVGG FKASLTTNAA
     HLHIGKGGIN LSNQASGRSL LVENLTGNIT VDGPLRVNNQ VGGYALAGSS ANFEFKAGTD
     TKNGTATFNN DISLGRFVNL KVDAHTANFK GIDTGNGGFN TLDFSGVTNK VNINKLITAS
     TNVAVKNFNI NELVVKTNGV SVGEYTHFSE DIGSQSRINT VRLETGTRSI YSGGVKFKGG
     EKLVINDFYY APWNYFDARN IKNVEITNKL AFGPQGSPWG TAKLMFNNLT LGQNAVMDYS
     QFSNLTIQGD FVNNQGTINY LVRGGQVATL NVGNAAAMFF SNNVDSATGF YQPLMKINSA
     QDLIKNKEHV LLKAKIIGYG NVSAGTDSIA NVNLIEQFKE RLALYNNNNR MDICVVRNTD
     DIKACGTAIG NQSMVNNPEN YKYLEGKAWK NIGISKTANG SKISVHYLGN STPTENGGNT
     TNLPTNTTNK VRFASYALIK NAPFARYSAT PNLVAINQHD FGTIESVFEL ANRSNDIDTL
     YANSGAQGRD LLQTLLIDSH DAGYARTMID ATSANEITKQ LNTATTTLNN IASLEHKTSG
     LQTLSLSNAM ILNSRLVNLS RRHTNHIDSF AKRLQALKDQ RFASLESAAE VLYQFAPKYE
     KPTNVWANAI GGTSLNSGGN ASLYGTSAGV DAYLNGEVEA IVGGFGSYGY SSFSNQANSL
     NSGANNTNFG VYSRIFANQH EFDFEAQGAL GSDQSSLNFK SALLRDLNQS YNYLAYSAAT
     RASYGYDFAF FRNALVLKPS VGVSYNHLGS TNFKSNSNQK VALKNGASSQ HLFNASANVE
     ARYYYGDTSY FYMNAGVLQE FANFGSSNAV SLNTFKVNAT RNPLNTHARV MMGGELKLAK
     EVFLNLGFVY LHNLISNIGH FASNLGMRYS F