ID   VIRB4_BARHE             Reviewed;         784 AA.
AC   Q9R2W4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Type IV secretion system protein virB4;
GN   Name=virB4; OrderedLocusNames=BH13280;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS   (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=10749166; DOI=10.1089/104454900314528;
RA   Schmiederer M., Anderson B.E.;
RT   "Cloning, sequencing, and expression of three Bartonella henselae genes
RT   homologous to the Agrobacterium tumefaciens VirB region.";
RL   DNA Cell Biol. 19:141-147(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=10882236; DOI=10.1089/10445490050043344;
RA   Padmalayam I., Karem K., Baumstark B.R., Massung R.;
RT   "The gene encoding the 17-kDa antigen of Bartonella henselae is located
RT   within a cluster of genes homologous to the virB virulence operon.";
RL   DNA Cell Biol. 19:377-382(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 732-784.
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=7494028; DOI=10.1128/jcm.33.9.2358-2365.1995;
RA   Anderson B.E., Lu E., Jones D., Regnery R.;
RT   "Characterization of a 17-kilodalton antigen of Bartonella henselae
RT   reactive with sera from patients with cat scratch disease.";
RL   J. Clin. Microbiol. 33:2358-2365(1995).
RN   [5]
RP   INDUCTION.
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=11553594; DOI=10.1128/iai.69.10.6495-6502.2001;
RA   Schmiederer M., Arcenas R., Widen R., Valkov N., Anderson B.E.;
RT   "Intracellular induction of the Bartonella henselae virB operon by human
RT   endothelial cells.";
RL   Infect. Immun. 69:6495-6502(2001).
RN   [6]
RP   INTERACTION WITH VIRB10.
RX   PubMed=15231811; DOI=10.1128/jb.186.14.4796-4801.2004;
RA   Shamaei-Tousi A., Cahill R., Frankel G.;
RT   "Interaction between protein subunits of the type IV secretion system of
RT   Bartonella henselae.";
RL   J. Bacteriol. 186:4796-4801(2004).
RN   [7]
RP   FUNCTION.
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=15049812; DOI=10.1111/j.1365-2958.2003.03964.x;
RA   Schmid M.C., Schulein R., Dehio M., Denecker G., Carena I., Dehio C.;
RT   "The VirB type IV secretion system of Bartonella henselae mediates
RT   invasion, proinflammatory activation and antiapoptotic protection of
RT   endothelial cells.";
RL   Mol. Microbiol. 52:81-92(2004).
RN   [8]
RP   FUNCTION.
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=15642951; DOI=10.1073/pnas.0406796102;
RA   Schulein R., Guye P., Rhomberg T.A., Schmid M.C., Schroeder G.,
RA   Vergunst A.C., Carena I., Dehio C.;
RT   "A bipartite signal mediates the transfer of type IV secretion substrates
RT   of Bartonella henselae into human cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:856-861(2005).
CC   -!- FUNCTION: The type IV secretion system VirB/VirD4 is a major virulence
CC       determinant for subversion of human endothelial cell (HEC) function.
CC       VirB-dependent changes of HEC include massive cytoskeletal
CC       rearrangements, a pro-inflammatory activation by nuclear factor NF-
CC       kappa-B, inhibition of early and late events of apoptosis, leading to
CC       an increased cell survival, and, at high infection doses, a cytostatic
CC       or cytotoxic effect, which interfers with a potent VirB-independent
CC       mitogenic activity. These changes of HEC require the T4S coupling
CC       protein VirD4 and at least one of the effector proteins BepA-G.
CC       Altogether with VirB11, may be implicated in providing the energy, via
CC       hydrolysis of ATP, for the assembly of secretion system and substrate
CC       transport. {ECO:0000269|PubMed:15049812, ECO:0000269|PubMed:15642951}.
CC   -!- SUBUNIT: Interacts with virB10. {ECO:0000269|PubMed:15231811}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}.
CC   -!- INDUCTION: During the interaction with the intracellular environment of
CC       host cells. {ECO:0000269|PubMed:11553594}.
CC   -!- SIMILARITY: Belongs to the TrbE/VirB4 family. {ECO:0000305}.
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DR   EMBL; U23447; AAD48921.1; -; Genomic_DNA.
DR   EMBL; AF182718; AAF00942.1; -; Genomic_DNA.
DR   EMBL; BX897699; CAF28101.1; -; Genomic_DNA.
DR   RefSeq; WP_011181129.1; NZ_LRIJ02000001.1.
DR   AlphaFoldDB; Q9R2W4; -.
DR   SMR; Q9R2W4; -.
DR   STRING; 283166.BH13280; -.
DR   PaxDb; Q9R2W4; -.
DR   PRIDE; Q9R2W4; -.
DR   EnsemblBacteria; CAF28101; CAF28101; BH13280.
DR   KEGG; bhe:BH13280; -.
DR   eggNOG; COG3451; Bacteria.
DR   OMA; HRDLNTL; -.
DR   Proteomes; UP000000421; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 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; Transport; Virulence.
FT   CHAIN           1..784
FT                   /note="Type IV secretion system protein virB4"
FT                   /id="PRO_0000273535"
FT   BINDING         435..442
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   784 AA;  89097 MW;  D352B22827C3BBE9 CRC64;
     MSMMKRESLP EDYIPYIRHI NQHVIALNSR CLMTVMVVEG VNFDTADIDQ LNSLHNQLNT
     LLKNIADERV ALYSHIIRRR ETIYPESQFF SSFAATLDEK YKKKMVSQEL YRNDLFVSLL
     WNPASDKTEQ LASFFQRLAK AKKTQSEPDQ EAIRKIEELS QDLIEGLESY GARLLSVYAH
     GGILFSEQSE FLHQLVGGRR ERIPLTFGTI ASTIYSDRVI FGKETIEIRH ESNERFAGMF
     GWKEYPSKTR PGMTDGLLTA PFEFILTQSF VFKSKAAASV IMGRKQNQMI NAADRASSQI
     EALDEALDDL ESNRFVLGEH HLSLAVFANH PKALAEYLSK ARAHLTNGGA VIAREDLGLE
     AAWWAQLPGN FSYRARSGAI TSRNFAALSP FHSFPIGKLE GNVWGTAVAL LKTQAGSPYY
     FNFHYGDLGN TFVCGPSGSG KTVIVNFLLA QLQKHNPTMV FFDKDQGAEI FVRAGGGKYK
     PLKNGQPTGI APLKGMEYTE KNKVFLRNWV LKLVTAEGQT VTEEERQDIA KAIDALGNLP
     HAQRSLSALQ LFFDNTSKEG IAIRLQRWLK GNDLGWVFDN DQDDLNLDSQ FIGYDMTDFL
     DNEEIRRPLM MYLFNRILDL IDGRRIIIVI DEFWKALEDD SFKAFAQDRL KTIRKQNGMM
     LFATQSPKDA LNSTIAHTII EQCPTQIFFP NQKANYKDYV EDFKLTEREF ELIQSELSRE
     SRRFLIKQGQ SSVVAELNLR GMNDEIAVLS GTTKNIELVN QIISEYGADP DIWLPIFHQR
     RENQ