EIBA_ECOLX
ID EIBA_ECOLX Reviewed; 392 AA.
AC Q9LA60;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 35.
DE RecName: Full=Immunoglobulin-binding protein EibA {ECO:0000303|PubMed:10722621};
DE AltName: Full=Trimeric autotransporter adhesin EibA;
DE Short=TAA EibA {ECO:0000305};
DE AltName: Full=Type 5 secretion system autotransporter EibA;
DE Flags: Precursor;
GN Name=eibA {ECO:0000303|PubMed:10722621};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BINDING TO HUMAN IGA AND IGG,
RP SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 35328 / ECOR 9;
RX PubMed=10722621; DOI=10.1128/iai.68.4.2205-2214.2000;
RA Sandt C.H., Hill C.W.;
RT "Four different genes responsible for nonimmune immunoglobulin-binding
RT activities within a single strain of Escherichia coli.";
RL Infect. Immun. 68:2205-2214(2000).
RN [2]
RP FUNCTION, BINDING TO HUMAN IGG, AND SUBUNIT.
RX PubMed=19303642; DOI=10.1016/j.molimm.2009.02.024;
RA Leo J.C., Goldman A.;
RT "The immunoglobulin-binding Eib proteins from Escherichia coli are
RT receptors for IgG Fc.";
RL Mol. Immunol. 46:1860-1866(2009).
RN [3]
RP BINDING TO FC, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND TOPOLOGY.
RX PubMed=22155776; DOI=10.1128/jb.05322-11;
RA Mikula K.M., Leo J.C., Lyskowski A., Kedracka-Krok S., Pirog A.,
RA Goldman A.;
RT "The translocation domain in trimeric autotransporter adhesins is necessary
RT and sufficient for trimerization and autotransportation.";
RL J. Bacteriol. 194:827-838(2012).
CC -!- FUNCTION: Binds (in a non-immune fashion) to the Fc portion of human
CC IgG but not IgA; binding occurs on the cell surface. Confers the
CC ability to survive exposure to human serum exposure (PubMed:10722621).
CC Binds to the Fc portion of human IgG and to whole mouse antibodies also
CC via Fc, binds more than 1 Fc or IgG (PubMed:19303642).
CC {ECO:0000269|PubMed:10722621, ECO:0000269|PubMed:19303642}.
CC -!- SUBUNIT: Homotrimer; can probably form mixed heterotrimers in vivo
CC (PubMed:22155776). Will form mixed heterotrimers with EibD; these are
CC correctly located in the outer membrane and bind IgG Fc, although less
CC well than homotrimers. Does not form trimers with distantly related
CC YadA from Y.enterocolitica; coexpression was lethal and one of the
CC genes is eliminated in vivo. If the full translocator domain (299-392)
CC is exchanged with that of YadA ('368-455'), will form heterotrimers
CC with YadA and vice-versa (PubMed:22155776). In denaturing gels runs as
CC 2 bands of about 121 and 131 kDa; extracting the sample with 88% phenol
CC at 70 degrees Celsius reduces part of the signal to about 45 kDa
CC (PubMed:10722621). Binds the Fc portion of IgG; binds more than 1 Fc
CC per subunit (PubMed:19303642). {ECO:0000269|PubMed:10722621,
CC ECO:0000269|PubMed:19303642, ECO:0000269|PubMed:22155776}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:22155776,
CC ECO:0000305|PubMed:10722621, ECO:0000305|PubMed:19303642}. Cell outer
CC membrane {ECO:0000269|PubMed:22155776, ECO:0000305|PubMed:10722621}.
CC Note=The C-terminal translocator domain is localized in the outer
CC membrane and the passenger domain is at the cell surface.
CC {ECO:0000269|PubMed:22155776, ECO:0000305|PubMed:10722621,
CC ECO:0000305|PubMed:19303642}.
CC -!- INDUCTION: In strain ECOR 9 expression is greater at 37 than 27 degrees
CC Celsius and increases upon entry into stationary phase (at protein
CC level). Upon expression from a plasmid in strain AB1157 (with its own
CC leader sequence) more protein is seen at 37 than 27 degrees Celsius (at
CC protein level). {ECO:0000269|PubMed:10722621}.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space (By similarity). Then,
CC trimerization and insertion of the C-terminal translocator domain in
CC the outer membrane forms a hydrophilic pore for the translocation of
CC the passenger domain to the bacterial cell surface (PubMed:22155776).
CC Trimerizes to make a lollipop-shaped form which consists of three
CC domains: a C-terminal membrane-anchor domain, an extended coiled-coil
CC stalk domain which binds IgG Fc, and an N-terminal head domain (By
CC similarity). {ECO:0000250|UniProtKB:P0C2W0,
CC ECO:0000250|UniProtKB:Q9MCI8, ECO:0000269|PubMed:22155776}.
CC -!- MISCELLANEOUS: Encoded in an Atlas prophage region of strain ECOR 9,
CC upon UV treatment bacteriophage containing this gene can be isolated.
CC {ECO:0000269|PubMed:10722621}.
CC -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC Eib subfamily. {ECO:0000305}.
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DR EMBL; AF151091; AAF63234.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9LA60; -.
DR SMR; Q9LA60; -.
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:0046819; P:protein secretion by the type V secretion system; IMP:UniProtKB.
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 outer membrane; Coiled coil; Membrane; Protein transport; Signal;
KW Transmembrane; Transmembrane beta strand; Transport; Virulence.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..392
FT /note="Immunoglobulin-binding protein EibA"
FT /id="PRO_0000450746"
FT TOPO_DOM 28..341
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22155776"
FT TRANSMEM 342..352
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT TRANSMEM 355..366
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT TRANSMEM 369..378
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT TRANSMEM 382..392
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 28..301
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 187..230
FT /note="Right-handed coiled-coil (RHcc)"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 231..256
FT /note="Saddle domain"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 257..322
FT /note="Left-handed coiled-coil (LHcc)"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 299..341
FT /note="Outer membrane translocation of the passenger
FT domain"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 342..392
FT /note="Translocator domain"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT COILED 174..215
FT /evidence="ECO:0000255"
SQ SEQUENCE 392 AA; 41950 MW; 21A764E71D0948AF CRC64;
MSKKFTKAVL SAAMAGVLFG VSFDIMAAEQ SYSALNAQNG AGSIYKVYYN PDNKTAHIDW
GGLGDVEKER NKPIPLLSKI DGNGNVTITS ADGSTTFTVY DKEVHDFMKA AASGKTDDIK
TNLLTEQNIR DLYNRVSAIQ QMETNVGLDE YGNVAVTPNE IKERVSLQRY LAWESANSTI
VANELEAQKG KLDAQKGELE AQKKNLGELT TRTDKIDAAA AATAAKVESR TLVGVSSDGT
LTRAEGAKNT ISVNDGLVAL SGRTDRIDAA VGAIDGRVTR NTQSIEKNSK AIAANTRTLQ
QHSARLDSQQ RQINENHKEM KRAAAQSAAL TGLFQPYSVG KFNASAAVGG YSDEQALAVG
VGYRFNEQTA AKAGVAFSDG DASWNVGVNF EF
