EIBC_ECOLX
ID EIBC_ECOLX Reviewed; 504 AA.
AC Q9LA56;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=Immunoglobulin-binding protein EibC {ECO:0000303|PubMed:10722621};
DE AltName: Full=Trimeric autotransporter adhesin EibC;
DE Short=TAA EibC {ECO:0000305};
DE AltName: Full=Type 5 secretion system autotransporter EibC;
DE Flags: Precursor;
GN Name=eibC {ECO:0000303|PubMed:10722621};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1] {ECO:0000312|EMBL:AAF63035.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], BINDING TO HUMAN IGG AND IGA, AND
RP SUBCELLULAR LOCATION.
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 IGA AND 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, 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 and less well to IgA; binding occurs on the cell surface. Confers
CC the ability to survive exposure to human serum exposure
CC (PubMed:10722621). Binds to the Fc portion of human IgG and IgA and to
CC whole mouse antibodies also via Fc (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 (PubMed:22155776). In denaturing gels runs as a
CC band of about 200 kDa (PubMed:10722621). Binds the Fc portion of
CC immunoglobulins; binds more than 1 Fc per subunit (PubMed:19303642).
CC {ECO:0000269|PubMed:10722621, ECO:0000269|PubMed:19303642,
CC 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 ECO:0000305|PubMed:19303642}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:22155776}. Note=The C-terminal translocator domain
CC is localized in the outer membrane and the passenger domain is at the
CC cell surface. {ECO:0000269|PubMed:22155776,
CC ECO:0000305|PubMed:10722621, ECO:0000305|PubMed:19303642}.
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 a prophage region of strain ECOR 9, upon UV
CC 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; AF151674; AAF63035.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9LA56; -.
DR SMR; Q9LA56; -.
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 Gene3D; 2.150.10.10; -; 1.
DR InterPro; IPR008640; Adhesin_Head_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; 2.
DR SUPFAM; SSF101967; SSF101967; 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.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..504
FT /note="Immunoglobulin-binding protein EibC"
FT /id="PRO_0000450747"
FT TOPO_DOM 27..453
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22155776"
FT TRANSMEM 454..464
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT TRANSMEM 467..478
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT TRANSMEM 481..490
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT TRANSMEM 494..504
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 27..413
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 154..280
FT /note="Head domain"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 281..296
FT /note="Neck"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 297..342
FT /note="Right-handed coiled-coil (RHcc)"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 343..368
FT /note="Saddle domain"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 369..434
FT /note="Left-handed coiled-coil (LHcc)"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 411..453
FT /note="Outer membrane translocation of the passenger
FT domain"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 454..504
FT /note="Translocator domain"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT COILED 411..438
FT /evidence="ECO:0000255"
SQ SEQUENCE 504 AA; 53159 MW; 6B5E192DD4B2771B CRC64;
MSKKFTMTLL SSSLAGLLVM SGGVSAQEEK YTVPYAIGEG KWGNTYEVVK TGGNGNFRYE
VKEKNGKKRS LFTFDSKGDV IINGSGITYT IHDGALNDFA QTAEKKKNGQ SQSHRMTDSV
VRDVYNKVYS LQRTKITGFS VEDGENGKVS LGSDAKASGE FSVAVGTGAR ADKKFATAVG
SWAAADGKQS TALGVGAYAY ANASTAAGTA AYVDGSAIYG TAIGNYAKVD ENATEGTALG
AKATVTNKNS VALGANSVTT RDNEVYIGYK TGTESDKTYG TRVLGGLSDG TRNSDAATVG
QLNRKVGGVY DDVKARITVE SEKQKKYTDQ KTSEVNEKVE ARTTVGVDSD GKLTRAEGAT
KTIAVNDGLV ALSGRTDRID YAVGAIDGRV TRNTQSIEKN SKAIAANTRT LQQHSARLDS
QQRQINENHK EMKRAAAQSA ALTGLFQPYS VGKFNATAAV GGYSDQQALA VGVGYRFNEQ
TAAKAGVAFS DGDASWNVGV NFEF
