VACA2_HELPX
ID VACA2_HELPX Reviewed; 1287 AA.
AC Q48245; Q9R5K9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 97.
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=ATCC 49503 / 60190;
RX PubMed=8144644; DOI=10.1016/s0021-9258(17)34097-8;
RA Cover T.L., Tummuru M.K., Cao P., Thompson S.A., Blaser M.J.;
RT "Divergence of genetic sequences for the vacuolating cytotoxin among
RT Helicobacter pylori strains.";
RL J. Biol. Chem. 269:10566-10573(1994).
RN [2]
RP PROTEIN SEQUENCE OF 34-56, AND CHARACTERIZATION.
RC STRAIN=ATCC 49503 / 60190;
RX PubMed=1587837; DOI=10.1016/s0021-9258(19)50054-0;
RA Cover T.L., Blaser M.J.;
RT "Purification and characterization of the vacuolating toxin from
RT Helicobacter pylori.";
RL J. Biol. Chem. 267:10570-10575(1992).
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; U05676; AAA17657.1; -; Unassigned_DNA.
DR PIR; B53739; B53739.
DR PDB; 2QV3; X-ray; 2.40 A; A=388-844.
DR PDB; 6NYF; EM; 3.20 A; A/B/C/D/E/F=34-854.
DR PDB; 6NYG; EM; 3.90 A; A/B/C/D/E/F/G/H/I/J/K/L=34-854.
DR PDB; 6NYJ; EM; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L=34-854.
DR PDB; 6NYL; EM; 3.70 A; A/B/C/D/E/F/G/H/I/J/K/L=34-854.
DR PDB; 6NYM; EM; 3.60 A; A/B/C/D/E/F/G/H/I/J/K/L=34-854.
DR PDB; 6NYN; EM; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L=34-854.
DR PDB; 6ODY; EM; 3.80 A; A/B/C/D/E/F=373-844.
DR PDBsum; 2QV3; -.
DR PDBsum; 6NYF; -.
DR PDBsum; 6NYG; -.
DR PDBsum; 6NYJ; -.
DR PDBsum; 6NYL; -.
DR PDBsum; 6NYM; -.
DR PDBsum; 6NYN; -.
DR PDBsum; 6ODY; -.
DR AlphaFoldDB; Q48245; -.
DR SMR; Q48245; -.
DR DIP; DIP-46228N; -.
DR TCDB; 1.B.12.6.1; the autotransporter-1 (at-1) family.
DR ABCD; Q48245; 6 sequenced antibodies.
DR EvolutionaryTrace; Q48245; -.
DR PHI-base; PHI:3141; -.
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 DisProt; DP03034; -.
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 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing; Membrane;
KW Periplasm; Secreted; Signal; Toxin; Transmembrane;
KW Transmembrane beta strand; Virulence.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:1587837"
FT CHAIN 34..1287
FT /note="Vacuolating cytotoxin"
FT /id="PRO_0000387588"
FT CHAIN 34..?
FT /note="Vacuolating cytotoxin autotransporter"
FT /id="PRO_0000002716"
FT CHAIN ?..1287
FT /note="Vacuolating cytotoxin translocator"
FT /evidence="ECO:0000255"
FT /id="PRO_0000002717"
FT DOMAIN 1014..1287
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT REGION 326..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:6NYF"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:6NYF"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:6NYF"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:6NYJ"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:6NYN"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:6NYJ"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 390..396
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 416..428
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 430..435
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 437..448
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:6NYJ"
FT STRAND 468..475
FT /evidence="ECO:0007829|PDB:2QV3"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 482..485
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 495..510
FT /evidence="ECO:0007829|PDB:2QV3"
FT TURN 512..514
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 515..541
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 543..552
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 563..568
FT /evidence="ECO:0007829|PDB:2QV3"
FT TURN 570..572
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 573..580
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 585..587
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 592..607
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 612..631
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 639..648
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 653..656
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 660..666
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 668..672
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 674..678
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 680..682
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 687..697
FT /evidence="ECO:0007829|PDB:2QV3"
FT TURN 703..705
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 711..715
FT /evidence="ECO:0007829|PDB:2QV3"
FT HELIX 717..719
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 722..730
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 732..738
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 742..745
FT /evidence="ECO:0007829|PDB:2QV3"
FT HELIX 751..756
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 759..763
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 769..775
FT /evidence="ECO:0007829|PDB:2QV3"
FT HELIX 776..786
FT /evidence="ECO:0007829|PDB:2QV3"
FT HELIX 789..793
FT /evidence="ECO:0007829|PDB:2QV3"
FT HELIX 795..801
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 804..807
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 811..815
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 817..824
FT /evidence="ECO:0007829|PDB:2QV3"
FT STRAND 832..835
FT /evidence="ECO:0007829|PDB:6NYF"
FT STRAND 837..839
FT /evidence="ECO:0007829|PDB:2QV3"
SQ SEQUENCE 1287 AA; 139041 MW; 0007370062FCB71F CRC64;
MEIQQTHRKI NRPLVSLALV GALVSITPQQ SHAAFFTTVI IPAIVGGIAT GTAVGTVSGL
LGWGLKQAEE ANKTPDKPDK VWRIQAGKGF NEFPNKEYDL YKSLLSSKID GGWDWGNAAT
HYWIKGGQWN KLEVDMKDAV GTYKLSGLRN FTGGDLDVNM QKATLRLGQF NGNSFTSYKD
SADRTTRVDF NAKNILIDNF LEINNRVGSG AGRKASSTVL TLQASEGITS SKNAEISLYD
GATLNLASNS VKLNGNVWMG RLQYVGAYLA PSYSTINTSK VTGEVNFNHL TVGDHNAAQA
GIIASNKTHI GTLDLWQSAG LNIIAPPEGG YKDKPNNTPS QSGAKNDKQE SSQNNSNTQV
INPPNSTQKT EVQPTQVIDG PFAGGKDTVV NIDRINTKAD GTIKVGGFKA SLTTNAAHLN
IGKGGVNLSN QASGRTLLVE NLTGNITVDG PLRVNNQVGG YALAGSSANF EFKAGVDTKN
GTATFNNDIS LGRFVNLKVD AHTANFKGID TGNGGFNTLD FSGVTNKVNI NKLITASTNV
AVKNFNINEL IVKTNGVSVG EYTHFSEDIG SQSRINTVRL ETGTRSIFSG GVKFKSGEKL
VIDEFYYSPW NYFDARNIKN VEITRKFASS TPENPWGTSK LMFNNLTLGQ NAVMDYSQFS
NLTIQGDFIN NQGTINYLVR GGKVATLNVG NAAAMMFNND IDSATGFYKP LIKINSAQDL
IKNTEHVLLK AKIIGYGNVS TGTNGISNVN LEEQFKERLA LYNNNNRMDT CVVRNTDDIK
ACGMAIGNQS MVNNPDNYKY LIGKAWKNIG ISKTANGSKI SVYYLGNSTP TENGGNTTNL
PTNTTNNARF ASYALIKNAP FAHSATPNLV AINQHDFGTI ESVFELANRS KDIDTLYANS
GAQGRDLLQT LLIDSHDAGY ARTMIDATSA NEITKQLNTA TTTLNNIASL EHKTSSLQTL
SLSNAMILNS RLVNLSRRHT NNIDSFAKRL QALKDQRFAS LESAAEVLYQ FAPKYEKPTN
VWANAIGGAS LNNGGNASLY GTSAGVDAYL NGQVEAIVGG FGSYGYSSFN NQANSLNSGA
NNTNFGVYSR IFANQHEFDF EAQGALGSDQ SSLNFKSALL RDLNQSYNYL AYSAATRASY
GYDFAFFRNA LVLKPSVGVS YNHLGSTNFK SNSTNKVALS NGSSSQHLFN ASANVEARYY
YGDTSYFYMN AGVLQEFANF GSSNAVSLNT FKVNATRNPL NTHARVMMGG ELKLAKEVFL
NLGVVYLHNL ISNIGHFASN LGMRYSF
