BTAE_BRUSU
ID BTAE_BRUSU Reviewed; 740 AA.
AC A0A0H3G586;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Autotransporter adhesin BtaE {ECO:0000305};
DE AltName: Full=Brucella trimeric autotransporter {ECO:0000303|PubMed:23319562};
DE AltName: Full=Type 5 secretion system autotransporter BtaE {ECO:0000305};
DE Flags: Precursor;
GN Name=btaE {ECO:0000303|PubMed:23319562};
GN OrderedLocusNames=BR0072 {ECO:0000312|EMBL:AAN29029.1},
GN BS1330_I0072 {ECO:0000312|EMBL:AEM17441.1};
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=23319562; DOI=10.1128/iai.01241-12;
RA Ruiz-Ranwez V., Posadas D.M., Van der Henst C., Estein S.M., Arocena G.M.,
RA Abdian P.L., Martin F.A., Sieira R., De Bolle X., Zorreguieta A.;
RT "BtaE, an adhesin that belongs to the trimeric autotransporter family, is
RT required for full virulence and defines a specific adhesive pole of
RT Brucella suis.";
RL Infect. Immun. 81:996-1007(2013).
CC -!- FUNCTION: Binds to hyaluronic acid and epithelial cells, and is
CC required for full virulence in the mouse model.
CC {ECO:0000269|PubMed:23319562}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P0C2W0}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:23319562}. 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:23319562).
CC {ECO:0000250|UniProtKB:P0C2W0, ECO:0000269|PubMed:23319562}.
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 exhibits a reduction in the
CC adhesion to HeLa and A549 epithelial cells compared with the wild-type
CC strain. Shows an attenuated phenotype in the mouse model.
CC {ECO:0000269|PubMed:23319562}.
CC -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC {ECO:0000305}.
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DR EMBL; AE014291; AAN29029.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM17441.1; -; Genomic_DNA.
DR RefSeq; WP_006191142.1; NZ_KN046804.1.
DR AlphaFoldDB; A0A0H3G586; -.
DR SMR; A0A0H3G586; -.
DR EnsemblBacteria; AEM17441; AEM17441; BS1330_I0072.
DR GeneID; 45051226; -.
DR KEGG; bms:BR0072; -.
DR KEGG; bsi:BS1330_I0072; -.
DR HOGENOM; CLU_007476_0_0_5; -.
DR OMA; KRDDQAN; -.
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 Gene3D; 2.150.10.10; -; 2.
DR InterPro; IPR008640; Adhesin_Head_dom.
DR InterPro; IPR008635; Coiled_stalk_dom.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR InterPro; IPR005594; YadA_C.
DR Pfam; PF03895; YadA_anchor; 1.
DR Pfam; PF05658; YadA_head; 4.
DR Pfam; PF05662; YadA_stalk; 4.
DR SUPFAM; SSF101967; SSF101967; 4.
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..11
FT /evidence="ECO:0000255"
FT CHAIN 12..740
FT /note="Autotransporter adhesin BtaE"
FT /id="PRO_0000438297"
FT TRANSMEM 686..696
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 700..710
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 719..725
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 728..739
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT REGION 12..647
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 648..686
FT /note="Outer membrane translocation of the passenger
FT domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 687..740
FT /note="Translocator domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
SQ SEQUENCE 740 AA; 75453 MW; 63EF0705F5794631 CRC64;
MFGLSVNHAY AGPGIFINDG TDDGCIWTFD KEDYSPIGDY FGNTAPADKD SAGRNSPASV
KYHIPSIQQL GGAATLKCLS KDRDTQTDRV LFYGNSKEQG SISLTLGGEL FVNNGNLGLG
GGTDTKAMRI GSMATLTGPS GLRSLAIGAG EIATVASGDD AIAIGTAAQA AHVGSIALGL
QSTTELPSLV KDVTINGIKL SAFAGSNPAS VLSIGNDTLK RSITNVGAGR VSKDSTDAVN
GRQLFAVSEQ AASGWSLTVN GMDKSRVGPG DTVDLSNSDG NLVLSKKGKD VTFNLASDLK
VTSLVAGNTF LDTNGLVITG GPSMTVSGID AGQLKISHVA DGAVTVTSTD AVNGSQLHRV
AHTIAEHLGG DAHVNADGSV IGPQYTVQKK RYKTIYDAFG GVDENLANIN DILHDIESGG
GIKYFHANSI GADSRALGTN SIAVGSDSVA SGEGSISVGN GAQASAHGSV ALGENAAAPD
ANSVALGAGS KTSEVVATKG TTINGQYYDF AGDAPSGTVS VGDKGAERTI TNVAAGRISV
ESTDAVNGSQ LNAVNQAIEN LAAGVTENDK FSVKYDRHSD GTKKNSMTLQ GWDSATPVVL
ANVADGVHKN DAVNVSQLKA GLSTTLGEAK AYTDQTALQT LDQANAYTDK KFGKLNEDIV
ATRIEARQAA AIGLAAASLR YDDRPGKISA AIGGGFWRGE GAVALGLGHT SEDQRMRSNL
SAATSGGNWG MGAGFSYTFN
