EIBD_ECOLX
ID EIBD_ECOLX Reviewed; 511 AA.
AC Q9MCI8;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Immunoglobulin-binding protein EibD {ECO:0000303|PubMed:10722621};
DE AltName: Full=Trimeric autotransporter adhesin EibD {ECO:0000303|PubMed:21742268};
DE Short=TAA EibD {ECO:0000305};
DE AltName: Full=Type 5 secretion system autotransporter EibD {ECO:0000305};
DE Flags: Precursor;
GN Name=eibD {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 FC OF HUMAN IGA AND
RP IGG, 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 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, 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).
RN [4] {ECO:0007744|PDB:2XQH, ECO:0007744|PDB:2XZR}
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 160-418, X-RAY CRYSTALLOGRAPHY
RP (2.80 ANGSTROMS) OF 385-441, BINDING TO FC, FUNCTION IN AGGREGATION AND
RP BIOFILM FORMATION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS
RP OF 332-LYS--TYR-334; 387-ASP-TYR-388 AND 415-THR--THR-417.
RX PubMed=21742268; DOI=10.1016/j.str.2011.03.021;
RA Leo J.C., Lyskowski A., Hattula K., Hartmann M.D., Schwarz H.,
RA Butcher S.J., Linke D., Lupas A.N., Goldman A.;
RT "The structure of E. coli IgG-binding protein D suggests a general model
RT for bending and binding in trimeric autotransporter adhesins.";
RL Structure 19:1021-1030(2011).
CC -!- FUNCTION: Binds (in a non-immune fashion) to the Fc portion of human
CC IgA and IgG; binding occurs on the cell surface. Confers the ability to
CC survive exposure to human serum exposure (PubMed:10722621). Binds to
CC the Fc portion of human IgG, IgA and to whole mouse antibodies also via
CC Fc (PubMed:19303642). Upon overexpression cells acquire an extra cell
CC surface layer that forms a zipper-like contact between cells; cells
CC autoagglutinate and form biofilm more readily, suggesting it may play a
CC role in defense against a host (PubMed:21742268).
CC {ECO:0000269|PubMed:10722621, ECO:0000269|PubMed:19303642,
CC ECO:0000269|PubMed:21742268}.
CC -!- SUBUNIT: Homotrimer; can probably form mixed heterotrimers in vivo
CC (Probable). Will form mixed heterotrimers with EibA or EibC; 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 210 kDa (PubMed:10722621). Binds the Fc portion of
CC immunoglobulins; binds more than 1 Fc per subunit, can be modeled to
CC bind 3 Fc per trimer (PubMed:19303642) (Probable).
CC {ECO:0000269|PubMed:10722621, ECO:0000269|PubMed:19303642,
CC ECO:0000269|PubMed:22155776, ECO:0000305|PubMed:21742268}.
CC -!- INTERACTION:
CC Q9MCI8; Q9MCI8: eibD; NbExp=3; IntAct=EBI-15935491, EBI-15935491;
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:22155776,
CC ECO:0000305|PubMed:10722621, ECO:0000305|PubMed:19303642,
CC ECO:0000305|PubMed:21742268}. Cell outer membrane
CC {ECO:0000269|PubMed:22155776, ECO:0000305|PubMed:10722621,
CC ECO:0000305|PubMed:21742268}; 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 ECO:0000305|PubMed:21742268}.
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 The crystallized passenger domain (residues 161-440) is an entwined,
CC elongated trimer with a head domain, a neck and 2 extended coiled-coil
CC regions of differing handedness separated by a saddle region. There are
CC a number of cavities in the first (right-handed, RHcc) coiled-coil
CC domain that may allow bending of the extended structure. Smaller
CC cavities in the second (left-handed, LHcc) coiled-coil bind 5 Cl(-) and
CC one water molecule. The Fc portion of IgG has been modeled to bind to
CC the LHcc domain just under the saddle; up to 3 Fc can bind to the
CC trimer (PubMed:21742268). {ECO:0000250|UniProtKB:P0C2W0,
CC ECO:0000269|PubMed:21742268, 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; AF151675; AAF63040.1; -; Genomic_DNA.
DR RefSeq; WP_054518649.1; NZ_UFYM01000003.1.
DR PDB; 2XQH; X-ray; 1.99 A; A=160-418.
DR PDB; 2XZR; X-ray; 2.80 A; A=385-441.
DR PDBsum; 2XQH; -.
DR PDBsum; 2XZR; -.
DR AlphaFoldDB; Q9MCI8; -.
DR SMR; Q9MCI8; -.
DR DIP; DIP-59140N; -.
DR EvolutionaryTrace; Q9MCI8; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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 3D-structure; Cell outer membrane; Coiled coil; Membrane;
KW Protein transport; Signal; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..511
FT /note="Immunoglobulin-binding protein EibD"
FT /id="PRO_0000450748"
FT TOPO_DOM 27..460
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:22155776"
FT TRANSMEM 461..471
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:22155776"
FT TRANSMEM 474..485
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:22155776"
FT TRANSMEM 488..497
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:22155776"
FT TRANSMEM 501..511
FT /note="Beta stranded"
FT /evidence="ECO:0000305|PubMed:22155776"
FT REGION 27..417
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000305|PubMed:22155776"
FT REGION 161..287
FT /note="Head domain"
FT /evidence="ECO:0000269|PubMed:21742268"
FT REGION 288..303
FT /note="Neck"
FT /evidence="ECO:0000269|PubMed:21742268"
FT REGION 304..349
FT /note="Right-handed coiled-coil (RHcc)"
FT /evidence="ECO:0000269|PubMed:21742268"
FT REGION 329..344
FT /note="Required to bind IgA"
FT /evidence="ECO:0000269|PubMed:21742268"
FT REGION 350..375
FT /note="Saddle domain"
FT /evidence="ECO:0000269|PubMed:21742268"
FT REGION 376..441
FT /note="Left-handed coiled-coil (LHcc)"
FT /evidence="ECO:0000269|PubMed:21742268"
FT REGION 384..418
FT /note="Required to bind IgG"
FT /evidence="ECO:0000269|PubMed:21742268"
FT REGION 418..460
FT /note="Outer membrane translocation of the passenger
FT domain"
FT /evidence="ECO:0000305|PubMed:22155776"
FT REGION 461..511
FT /note="Translocator domain"
FT /evidence="ECO:0000305|PubMed:22155776"
FT COILED 304..349
FT /evidence="ECO:0000269|PubMed:21742268,
FT ECO:0007744|PDB:2XQH, ECO:0007744|PDB:2XZR"
FT COILED 376..441
FT /evidence="ECO:0000269|PubMed:21742268,
FT ECO:0007744|PDB:2XQH, ECO:0007744|PDB:2XZR"
FT MUTAGEN 332..334
FT /note="KKY->AAA: Loss of IgA binding by fragment 161-418,
FT no change in IgG binding."
FT /evidence="ECO:0000269|PubMed:21742268"
FT MUTAGEN 387..388
FT /note="DY->AA: 2-fold decreased affinity for IgA, at least
FT 5-fold decreased affinity for IgG by fragment 161-418."
FT /evidence="ECO:0000269|PubMed:21742268"
FT MUTAGEN 415..417
FT /note="TRT->AAA: 5-fold decreased affinity for IgA, 4-fold
FT decreased affinity for IgG by fragment 161-418."
FT /evidence="ECO:0000269|PubMed:21742268"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:2XQH"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:2XQH"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:2XQH"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:2XQH"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:2XQH"
FT STRAND 244..247
FT /evidence="ECO:0007829|PDB:2XQH"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:2XQH"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:2XQH"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:2XQH"
FT HELIX 306..349
FT /evidence="ECO:0007829|PDB:2XQH"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:2XQH"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:2XQH"
FT HELIX 372..415
FT /evidence="ECO:0007829|PDB:2XQH"
SQ SEQUENCE 511 AA; 53843 MW; 061ABC75777CEA86 CRC64;
MSKKFTMTLL SSSLAGLLVM SGGVSAQNGT YSVLQDDSQK SGPVKYGSTY EVVKTVDNGN
FRYEVKEKKN DKRTLFKFDS EGNVTVKGKG ITHTLHDPAL KDFARTAEGK KNEQNGNTPP
HKLTDSAVRG VYNKVYGLEK TEITGFSVED GENGKVSLGS DAKASGEFSV AVGNGARATE
KASTAVGSWA AADGKQSTAL GVGTYAYANA STALGSVAFV DNTATYGTAA GNRAKVDKDA
TEGTALGAKA TVTNKNSVAL GANSVTTRDN EVYIGYKTGT ESDKTYGTRV LGGLSDGTRN
SDAATVGQLN RKVGGVYDDV KARITVESEK QKKYTDQKTS EVNEKVEART TVGVDSDGKL
TRAEGATKTI AVNDGLVALS GRTDRIDYAV GAIDGRVTRN TQSIEKNSKA IAANTRTLQQ
HSARLDSQQR QINENHKEMK RAAAQSAALT GLFQPYSVGK FNATAAVGGY SDQQALAVGV
GYRFNEQTAA KAGVAFSDGD ASWNVGVNFE F
