VACA_HELPJ
ID VACA_HELPJ Reviewed; 1288 AA.
AC Q9ZKW5;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 119.
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; OrderedLocusNames=jhp_0819;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD06400.1; -; Genomic_DNA.
DR PIR; E71884; E71884.
DR RefSeq; WP_000405515.1; NC_000921.1.
DR AlphaFoldDB; Q9ZKW5; -.
DR SMR; Q9ZKW5; -.
DR STRING; 85963.jhp_0819; -.
DR EnsemblBacteria; AAD06400; AAD06400; jhp_0819.
DR KEGG; hpj:jhp_0819; -.
DR OMA; NQGTINY; -.
DR Proteomes; UP000000804; Chromosome.
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..1288
FT /note="Vacuolating cytotoxin autotransporter"
FT /id="PRO_0000387585"
FT CHAIN 34..?
FT /note="Vacuolating cytotoxin"
FT /id="PRO_0000022649"
FT CHAIN ?..1288
FT /note="Vacuolating cytotoxin translocator"
FT /evidence="ECO:0000255"
FT /id="PRO_0000022650"
FT DOMAIN 1015..1288
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT REGION 326..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1288 AA; 139132 MW; 244B159DFC5F32B9 CRC64;
MEIQQTHRKI NRPLVSLVLA GALISAIPQE SHAAFFTTVI IPAIVGGIAT GTAVGTVSGL
LSWGLKQAEE ANKTPDKPDK VWRIQAGKGF NEFPNKEYDL YKSLLSSKID GGWDWGNAAR
HYWVKGGQWN KLEVDMKDAV GTYKLSGLRN FTGGDLDVNM QKATLRLGQF NGNSFTSYKD
SADRTTRVNF NAKNISIDNF VEINNRVGSG AGRKASSTVL TLQASEGITS SKNAEISLYD
GATLNLASNS VKLNGNVWMG RLQYVGAYLA PSYSTINTSK VQGEVDFNHL TVGDQNAAQA
GIIASNKTHI GTLDLWQSAG LNIIAPPEGG YKDKPNSTTS QSGTKNDKKE ISQNNNSNTE
VINPPNNTQK TETEPTQVID GPFAGGKDTV VNIFHLNTKA DGTIKVGGFK ASLTTNAAHL
NIGKGGVNLS NQASGRTLLV ENLTGNITVD GPLRVNNQVG GYALAGSSAN FEFKAGVDTK
NGTATFNNDI SLGRFVNLKV DAHTANFKGI DTGNGGFNTL DFSGVTDKVN INKLITASTN
VAVKNFNINE LIVKTNGISV GEYTHFSEDI GSQSRINTVR LETGTRSIFS GGVKFKSGEK
LVINDFYYSP WNYFDARNVK NVEITRKFAS STPENPWGTS KLMFNNLTLG QNAVMDYSQF
SNLTIQGDFI NNQGTINYLV RGGKVATLNV GNAAAMMFNN DIDSATGFYK PLIKINSAQD
LIKNTEHVLL KAKIIGYGNV STGTNGISNV NLEEQFKERL ALYNNNNRMD TCVVRNTDDI
KACGMAIGNQ SMVNNPDNYK YLIGKAWRNI GISKTANGSK ISVYYLGNST PTENGGNTTN
LPTNTTNNAH SANYALVKNA PFAHSATPNL VAINQHDFGT IESVFELANR SKDIDTLYTH
SGAQGRDLLQ TLLIDSHDAG YARQMIDNTS TGEITKQLNA ATDALNNVAS LEHKQSGLQT
LSLSNAMILN SRLVNLSRKH TNHINSFAQR LQALKGQEFA SLESAAEVLY QFAPKYEKPT
NVWANAIGGA SLNSGSNASL YGTSAGVDAF LNGNVEAIVG GFGSYGYSSF SNQANSLNSG
ANNANFGVYS RFFANQHEFD FEAQGALGSD QSSLNFKSTL LQDLNQSYNY LAYSATARAS
YGYDFAFFRN ALVLKPSVGV SYNHLGSTNF KSNSQSQVAL KNGASSQHLF NANANVEARY
YYGDTSYFYL HAGVLQEFAH FGSNDVASLN TFKINAARSP LSTYARAMMG GELQLAKEVF
LNLGVVYLHN LISNASHFAS NLGMRYSF
