BTAF_BRUSU
ID BTAF_BRUSU Reviewed; 278 AA.
AC A0A0H3G4K1;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 21.
DE RecName: Full=Autotransporter adhesin BtaF {ECO:0000305};
DE AltName: Full=Brucella trimeric autotransporter {ECO:0000303|PubMed:24236157};
DE AltName: Full=Type 5 secretion system autotransporter BtaF {ECO:0000305};
DE Flags: Precursor;
GN Name=btaF {ECO:0000303|PubMed:24236157};
GN OrderedLocusNames=BR1846 {ECO:0000312|EMBL:AAN30741.1},
GN BS1330_I1840 {ECO:0000312|EMBL:AEM19158.1};
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
RN [3]
RP FUNCTION AS AN ADHESIN, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=24236157; DOI=10.1371/journal.pone.0079770;
RA Ruiz-Ranwez V., Posadas D.M., Estein S.M., Abdian P.L., Martin F.A.,
RA Zorreguieta A.;
RT "The BtaF trimeric autotransporter of Brucella suis is involved in
RT attachment to various surfaces, resistance to serum and virulence.";
RL PLoS ONE 8:E79770-E79770(2013).
CC -!- FUNCTION: Participates in bacterial attachment to several surfaces,
CC including various extracellular matrix (ECM) components and a
CC hydrophobic abiotic surface. Involved in adhesion to host epithelial
CC cells and is required for full virulence in mice. Also implicated in
CC the resistance to porcine serum. {ECO:0000269|PubMed:24236157}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P0C2W0}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:24236157}. Cell
CC outer membrane {ECO:0000250|UniProtKB:P0C2W0}. Note=The C-terminal
CC translocator domain is localized in the outer membrane and the
CC passenger domain is at the cell surface (By similarity). Localizes at
CC the new cell pole generated after cell division (PubMed:24236157).
CC {ECO:0000250|UniProtKB:P0C2W0, ECO:0000269|PubMed:24236157}.
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. {ECO:0000250|UniProtKB:P0C2W0}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant shows a significant decrease in
CC the attachment to an abiotic surface and in the ability to bind
CC collagen, hyaluronic acid and fetuin. Deletion leads to decreased
CC adhesion to host cells, but it does not affect later stages of cellular
CC infection. Splenic infection is significantly reduced in mice.
CC {ECO:0000269|PubMed:24236157}.
CC -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014291; AAN30741.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM19158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H3G4K1; -.
DR SMR; A0A0H3G4K1; -.
DR EnsemblBacteria; AEM19158; AEM19158; BS1330_I1840.
DR KEGG; bms:BR1846; -.
DR KEGG; bsi:BS1330_I1840; -.
DR HOGENOM; CLU_062782_0_0_5; -.
DR OMA; DTNAKGV; -.
DR Proteomes; UP000007104; Chromosome I.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR005594; YadA_C.
DR Pfam; PF03895; YadA_anchor; 1.
DR SUPFAM; SSF54523; SSF54523; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell outer membrane; Membrane; Protein transport; Signal;
KW Transmembrane; Transmembrane beta strand; Transport; Virulence.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..278
FT /note="Autotransporter adhesin BtaF"
FT /id="PRO_0000438298"
FT REGION 30..182
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 186..224
FT /note="Outer membrane translocation of the passenger
FT domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 225..278
FT /note="Translocator domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
SQ SEQUENCE 278 AA; 28553 MW; 7DC70067A8F86211 CRC64;
MKLPPVFVFE LVENQGLANI ALIRPRVIAP DNNLRPGGIV SGIAGLLTLG QENRNLISEN
RQVINNNTTA IGQNSDRIDA NAKGVADNRA AIGQNSGRID ANAKGVADNK AAIGRNSGRI
DANAKGVADN KTAIGRNSGR IDTNAKGVAD NRAAISQNRG RINANAAGVA SNRAAIRQNS
AAISALGQRV DGLQGQINSA RKEARAGAAN AAALSGLRYD NRPGKVSIAT GVGGFKGSTA
LAAGIGYTSK NENARYNVSV AYNEAGTSWN AGASFTLN
