ID   VACA3_HELPX             Reviewed;        1310 AA.
AC   Q48253;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=TX30A;
RX   PubMed=7629077; DOI=10.1074/jbc.270.30.17771;
RA   Atherton J.C., Cao P., Peek R.M. Jr., Tummuru M.K., Blaser M.J.,
RA   Cover T.L.;
RT   "Mosaicism in vacuolating cytotoxin alleles of Helicobacter pylori.
RT   Association of specific vacA types with cytotoxin production and peptic
RT   ulceration.";
RL   J. Biol. Chem. 270:17771-17777(1995).
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; U29401; AAA86834.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q48253; -.
DR   SMR; Q48253; -.
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; IPR003842; Vacuolating_cytotoxin.
DR   Pfam; PF03797; Autotransporter; 1.
DR   Pfam; PF02691; VacA; 1.
DR   PRINTS; PR01656; VACCYTOTOXIN.
DR   SMART; SM00869; Autotransporter; 1.
DR   SUPFAM; SSF103515; SSF103515; 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..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..1310
FT                   /note="Vacuolating cytotoxin autotransporter"
FT                   /id="PRO_0000387589"
FT   CHAIN           31..?
FT                   /note="Vacuolating cytotoxin"
FT                   /id="PRO_0000002718"
FT   CHAIN           ?..1310
FT                   /note="Vacuolating cytotoxin translocator"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000002719"
FT   DOMAIN          1038..1310
FT                   /note="Autotransporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT   REGION          339..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1310 AA;  141989 MW;  1BC21FE3D435F981 CRC64;
     MEIQQTHRKI NRPIISLALV GVLMGTELGA NTPNDPIHSE SRAFFTTVII PAIVGGIATG
     AAVGTVSGLL SWGLKQAEQA NKAPDKPDKV WRIQAGRGFD NFPHKQYDLY KSLLSSKIDG
     GWDWGNAARH YWVKDGQWNK LEVDMQNAVG TYNLSGLINF TGGDLDVNMQ KATLRLGQFN
     GNSFTSFKDG ANRTTRVNFD AKNILIDNFV EINNRVGSGA GRKASSTVLT LKSSEKITSR
     ENAEISLYDG ATLNLVSSSN QSVDLYGKVW MGRLQYVGAY LAPSYSTIDT SKVQGEMNFR
     HLAVGDQNAA QAGIIANKKT NIGTLDLWQS AGLSIITPPE GGYESKTKDN PQNNPKNDAQ
     KTEIQPTQVI DGPFAGGKDT VVNIFHLNTK ADGTLRAGGF KASLSTNAAH LHIGEGGVNL
     SNQASGRTLL VENLTGNITV EGTLRVNNQV GGAAIAGSSA NFEFKAGEDT NNATATFNND
     IHLGKAVNLR VDAHTANFNG NIYLGKSTNL RVNGHTAHFK NIDATKSDNG LNTSTLDFSG
     VTDKVNINKL TTAATNVNIK NFDIKELVVT TRVQSFGQYT IFGENIGDKS RIGVVSLQTG
     YSPAYSGGVT FKGGKKLVID EIYHAPWNYF DARNVTDVEI NKRILFGAPG NIAGKTGLMF
     NNLTLNSNAS MDYGKDLDLT IQGHFTNNQG TMNLFVQDGR VATLNAGHQA SMIFNNLVDS
     TTGFYKPLIK INNAQNLTKN KEHVLVKARN IDYNLVGVQG ASYDNISASN TNLQEQFKER
     LALYNNNNRM DTCVVRKDNL NDIKACGMAI GNQSMVNNPE NYKYLEGKAW KNTGINKTAN
     NTTIAVNLGN NSTPTNSTTD TTNLPTNTTN NARFASYALI KNAPFAHSAT PNLVAINQHD
     FGTIESVFEL ANRSSDIDTL YANSGAQGRD LLQTLLIDSH DAGYARTMID ATSANEITQQ
     LNAATTTLNN IASLEHKTSG LQTLSLSNAM ILNSRLVNLS RKHTNHIDSF AKRLQALKDQ
     RFASLESAAE VLYQFAPKYE KPTNVWANAI GGTSLNNGSN ASLYGTSAGV DAYLNGEVEA
     IVGGFGSYGY SSFSNQANSL NSGANNTNFG VYSRIFANQH EFDFEAQGAL GSDQSSLNFK
     SALLQDLNQS YHYLAYSATT RASYGYDFAF FRNALVLKPS VGVSYNHLGS TNFKSNSNQV
     ALSNGSSSQH LFNANANVEA RYYYGDTSYF YMNAGVLQEF ARFGSNNAVS LNTFKVNATR
     NPLNTHARVM MGGELQLAKE VFLNLGVVYL HNLISNASHF ASNLGMRYSF