CAGE_HELPY
ID CAGE_HELPY Reviewed; 983 AA.
AC Q48252; P94836; Q9JMX3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Type IV secretion system protein CagE {ECO:0000305};
DE EC=7.4.2.8 {ECO:0000269|PubMed:26565397};
DE AltName: Full=CAG pathogenicity island protein 23;
DE AltName: Full=Protein PicB;
GN Name=cagE {ECO:0000303|PubMed:8962108};
GN Synonyms=cag23, picB {ECO:0000303|PubMed:8825091};
GN OrderedLocusNames=HP_0544;
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 [GENOMIC DNA], AND FUNCTION IN VIRULENCE.
RC STRAIN=ATCC 53726 / 84-183;
RX PubMed=8825091; DOI=10.1111/j.1365-2958.1995.18050867.x;
RA Tummuru M.K.R., Sharma S.A., Blaser M.J.;
RT "Helicobacter pylori picB, a homologue of the Bordetella pertussis toxin
RT secretion protein, is required for induction of IL-8 in gastric epithelial
RT cells.";
RL Mol. Microbiol. 18:867-876(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN VIRULENCE.
RC STRAIN=DSM 4867 / CCUG 17874 / NCTC 11638;
RX PubMed=8962108; DOI=10.1073/pnas.93.25.14648;
RA Censini S., Lange C., Xiang Z., Crabtree J., Ghiara P., Borodovsky M.,
RA Rappuoli R., Covacci A.;
RT "cag, a pathogenicity island of Helicobacter pylori, encodes type I-
RT specific and disease-associated virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14648-14653(1996).
RN [3]
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 [4]
RP FUNCTION, ATPASE ACTIVITY, CATALYTIC ACTIVITY, INTERACTION WITH CAGV AND
RP CAGBETA, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=26565397; DOI=10.1371/journal.pone.0142606;
RA Shariq M., Kumar N., Kumari R., Kumar A., Subbarao N., Mukhopadhyay G.;
RT "Biochemical analysis of CagE: a VirB4 homologue of Helicobacter pylori
RT Cag-T4SS.";
RL PLoS ONE 10:e0142606-e0142606(2015).
RN [5]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, AND CRYOELECTRON TOMOGRAPHY.
RX PubMed=31088930; DOI=10.1128/mbio.00849-19;
RA Hu B., Khara P., Song L., Lin A.S., Frick-Cheng A.E., Harvey M.L.,
RA Cover T.L., Christie P.J.;
RT "In situ molecular architecture of the Helicobacter pylori Cag type IV
RT secretion system.";
RL MBio 10:e00849-e00849(2019).
CC -!- FUNCTION: ATPase component of the type IV secretion system Cag (Cag-
CC T4SS) (PubMed:26565397). Acts as a molecular motor to provide the
CC energy that is required for the export of proteins (Probable). Required
CC for CagA translocation and induction of IL-8 in host gastric epithelial
CC cells (PubMed:26565397, PubMed:8825091, PubMed:8962108). Plays a key
CC role in Cag-T4SS pilus biogenesis, especially in the localization and
CC stabilization of the pilus-associated components CagI, CagL and the
CC surface protein CagH (PubMed:26565397). Is also critical for assembly
CC of the entire cytoplasmic portion of the Cag inner membrane complex
CC (IMC) (PubMed:31088930). {ECO:0000269|PubMed:26565397,
CC ECO:0000269|PubMed:31088930, ECO:0000269|PubMed:8825091,
CC ECO:0000269|PubMed:8962108, ECO:0000305|PubMed:26565397}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8;
CC Evidence={ECO:0000269|PubMed:26565397};
CC -!- SUBUNIT: Component of the Cag type IV secretion system, which is
CC composed of a wheel-shaped outer membrane complex (OMC) and an inner
CC membrane complex (IMC) (PubMed:31088930). Interacts with CagV and
CC CagBeta (PubMed:26565397). {ECO:0000269|PubMed:26565397,
CC ECO:0000269|PubMed:31088930}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:26565397}; Peripheral membrane protein
CC {ECO:0000269|PubMed:26565397}; Cytoplasmic side
CC {ECO:0000269|PubMed:26565397}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene affects pilus synthesis.
CC Mutant is unable to translocate CagA and is unable to induce IL-8
CC secretion by gastric epithelial cells (PubMed:26565397). Deletion has
CC no effect on assembly of the Cag outer membrane complex, but the mutant
CC machine completely lacks the entire cytoplasmic complex
CC (PubMed:31088930). {ECO:0000269|PubMed:26565397,
CC ECO:0000269|PubMed:31088930}.
CC -!- SIMILARITY: Belongs to the TrbE/VirB4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF80209.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U28133; AAB63389.1; -; Genomic_DNA.
DR EMBL; AF282853; AAF80209.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE000511; AAD07610.1; -; Genomic_DNA.
DR PIR; H64587; H64587.
DR RefSeq; NP_207340.1; NC_000915.1.
DR RefSeq; WP_000495985.1; NC_018939.1.
DR AlphaFoldDB; Q48252; -.
DR SMR; Q48252; -.
DR DIP; DIP-3373N; -.
DR IntAct; Q48252; 1.
DR MINT; Q48252; -.
DR STRING; 85962.C694_02805; -.
DR TCDB; 3.A.7.12.1; the type iv (conjugal dna-protein transfer or virb) secretory pathway (ivsp) family.
DR PaxDb; Q48252; -.
DR PRIDE; Q48252; -.
DR EnsemblBacteria; AAD07610; AAD07610; HP_0544.
DR KEGG; hpy:HP_0544; -.
DR PATRIC; fig|85962.47.peg.587; -.
DR eggNOG; COG3451; Bacteria.
DR OMA; MFMDEFW; -.
DR PhylomeDB; Q48252; -.
DR PHI-base; PHI:3143; -.
DR PHI-base; PHI:7342; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR004346; CagE_TrbE_VirB.
DR InterPro; IPR018145; CagE_TrbE_VirB_cntrl_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR043964; P-loop_TraG.
DR Pfam; PF03135; CagE_TrbE_VirB; 1.
DR Pfam; PF19044; P-loop_TraG; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR00929; VirB4_CagE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Virulence.
FT CHAIN 1..983
FT /note="Type IV secretion system protein CagE"
FT /id="PRO_0000089281"
FT BINDING 597..604
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 15
FT /note="V -> I (in Ref. 2; AAF80209)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="K -> Q (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="A -> T (in Ref. 1; AAB63389)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="V -> I (in Ref. 1; AAB63389)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="V -> I (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 242
FT /note="S -> G (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="Y -> F (in Ref. 2; AAF80209)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="I -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="V -> I (in Ref. 1; AAB63389)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="C -> S (in Ref. 1; AAB63389)"
FT /evidence="ECO:0000305"
FT CONFLICT 556
FT /note="E -> D (in Ref. 1; AAB63389)"
FT /evidence="ECO:0000305"
FT CONFLICT 618..631
FT /note="VHNFPANVSKDKQK -> AIIFLLMSAKTNKS (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 618..619
FT /note="VH -> AY (in Ref. 2; AAF80209)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="N -> D (in Ref. 1; AAB63389)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="I -> V (in Ref. 1; AAB63389)"
FT /evidence="ECO:0000305"
FT CONFLICT 733
FT /note="D -> N (in Ref. 2; AAF80209)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="G -> S (in Ref. 1; AAB63389)"
FT /evidence="ECO:0000305"
FT CONFLICT 855..983
FT /note="RNAIVRLATQSITDLLACPIADTIREQCPTKIFLRNDGGNLSDYQRLANVTE
FT KEFEIITKGLDRKILYKQDGSPSVIASFNLRGIPKEYLKILSTDTVFVKEIDKIIQNHS
FT IIDKYQALRQMYQQIKEY -> ETLLLDLQPKASLIFWLALLLIRLENNALQRFF (in
FT Ref. 1; AAB63389)"
FT /evidence="ECO:0000305"
FT CONFLICT 981
FT /note="K -> E (in Ref. 2; AAF80209)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 983 AA; 112021 MW; 844D8A653DFFE8E5 CRC64;
MFVASKQADE QKKLVIEQEV QKRQFKKIEE LKADMQKGVN PFFKVLFDGG NRLFGFPETF
IYSSIFILFV TIVLSVILFQ AYEPVLIVAI VIVLVALGFK KDYRLYQRME RAMKFKKPFL
FKGVKNKAFM SIFSMKPSKE MANDIHLNPN REDRLVSAAN SYLANNYECF LDDGVILTNN
YSLLGTIKLG GIDFLTTSKK DLIELHASIY SVFRNFVTPE FKFYFHTVKK KIVIDETNRD
YSLIFSNDFM RAYNEKQKRE SFYDISFYLT IEQDLLDTLN EPVMNKKHFA DNNFEEFQRI
IRAKLENFKD RIELIEELLS KYHPIRLKEY TKDGVIYSKQ CEFYNFLVGM NEAPFICNRK
DLYLKEKMHG GVKEVYFANK HGKILNDDLS EKYFSAIEIS EYAPKSQSDL FDKINALDSE
FIFMHAYSPK NSQVLKDKLA FTSRRIIISG GSKEQGMTLG CLSELVGNGD ITLGSYGNSL
VLFADSFEKM KQSVKECVSS LNAKGFLANA ATFSMENYFF AKHCSFITLP FIFDVTSNNF
ADFIAMRAMS FDGNQENNAW GNSVMTLKSE INSPFYLNFH MPTDFGSASA GHTLILGSTG
SGKTVFMSMT LNAMGQFVHN FPANVSKDKQ KLTMVYMDKD YGAYGNIVAM GGEYVKIELG
TDTGLNPFAW AACVQKTNAT MEQKQTAISV VKELVKNLAT KSDEKDENGN SISFSLADSN
TLAAAVTNLI TGDMNLDYPI TQLINAFGKD HNDPNGLVAR LAPFCKSTNG EFQWLFDNKA
TDRLDFSKTI IGVDGSSFLD NNDVSPFICF YLFARIQEAM DGRRFVLDID EAWKYLGDPK
VAYFVRDMLK TARKRNAIVR LATQSITDLL ACPIADTIRE QCPTKIFLRN DGGNLSDYQR
LANVTEKEFE IITKGLDRKI LYKQDGSPSV IASFNLRGIP KEYLKILSTD TVFVKEIDKI
IQNHSIIDKY QALRQMYQQI KEY
