VIRBB_BARHE
ID VIRBB_BARHE Reviewed; 356 AA.
AC Q9RNC7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Type IV secretion system protein VirB11;
GN Name=virB11; OrderedLocusNames=BH13350;
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=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 [2]
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 [3]
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 [4]
RP INTERACTION WITH VIRB9.
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 [5]
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 [6]
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 VirB4, 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 VirB9. {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 GSP E family. {ECO:0000305}.
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DR EMBL; AF182718; AAF00949.1; -; Genomic_DNA.
DR EMBL; BX897699; CAF28108.1; -; Genomic_DNA.
DR RefSeq; WP_011181136.1; NZ_LRIJ02000001.1.
DR AlphaFoldDB; Q9RNC7; -.
DR SMR; Q9RNC7; -.
DR STRING; 283166.BH13350; -.
DR PaxDb; Q9RNC7; -.
DR EnsemblBacteria; CAF28108; CAF28108; BH13350.
DR GeneID; 64157505; -.
DR KEGG; bhe:BH13350; -.
DR eggNOG; COG0630; Bacteria.
DR OMA; GDEIVTM; -.
DR Proteomes; UP000000421; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043684; C:type IV secretion system complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0044097; P:secretion by the type IV secretion system; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001482; T2SS/T4SS.
DR InterPro; IPR014155; VirB11.
DR Pfam; PF00437; T2SSE; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02788; VirB11; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Transport; Virulence.
FT CHAIN 1..356
FT /note="Type IV secretion system protein VirB11"
FT /id="PRO_0000273533"
FT BINDING 187..194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 356 AA; 39721 MW; 92FBAA74CE4775A7 CRC64;
MNQNLHTLSD ETVAIVLTKL EPISTFLKDE NLFEIVINRP YQVMTEGVEG WKTIETPALS
FNELMGIAKV VASYSKQNIS EKNPILSATL PGNERIQIVI PPAVEKNTIS MTIRKPSSRS
FSLEDLANKG LFSVCEQVSF TPLNNYLSHL SELKHIDHDL VRAYAKKDFV FFLNQAVQCQ
KNILIAGKTG SGKTTLSKAL IAKIPDDERI ITIEDTPELV VPQPNYVSMI YSKDGQGLAS
VGPKELLESA LRMRPDRILL QELRDGTAFY YIRNVNSGHP GSITTVHAST ALAAFEQMTL
LVKESEGGGD LERDDIRGLL ISMIDIIIQC KRIEGKFKVT EIYYDPFKQR NIFGGN
