EIBE_ECOLX
ID EIBE_ECOLX Reviewed; 487 AA.
AC Q9LA53;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=Immunoglobulin-binding protein EibE {ECO:0000303|PubMed:10722621};
DE AltName: Full=Trimeric autotransporter adhesin EibE;
DE Short=TAA EibE {ECO:0000305};
DE AltName: Full=Type 5 secretion system autotransporter EibE;
DE Flags: Precursor;
GN Name=eibE {ECO:0000303|PubMed:10722621};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1] {ECO:0000312|EMBL:AAF63045.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BINDING TO HUMAN IGG, SUBUNIT,
RP 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).
CC -!- FUNCTION: Binds (in a non-immune fashion) to the Fc portion of human
CC IgG and very weakly to IgA; binding occurs on the cell surface. Confers
CC the ability to survive exposure to human serum exposure.
CC {ECO:0000269|PubMed:10722621}.
CC -!- SUBUNIT: Homotrimer; can probably form mixed heterotrimers in vivo (By
CC similarity). In denaturing gels runs as a band of about 180 kDa
CC (PubMed:10722621). {ECO:0000250|UniProtKB:Q9MCI8,
CC ECO:0000269|PubMed:10722621}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000305|PubMed:10722621}. Cell
CC outer membrane {ECO:0000305|PubMed:10722621}. Note=The C-terminal
CC translocator domain is localized in the outer membrane and the
CC passenger domain is at the cell surface. {ECO:0000305|PubMed:10722621}.
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 -!- 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; AF151676; AAF63045.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9LA53; -.
DR SMR; Q9LA53; -.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
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; 1.
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..487
FT /note="Immunoglobulin-binding protein EibE"
FT /id="PRO_0000450749"
FT TOPO_DOM 27..436
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8,
FT ECO:0000305|PubMed:10722621"
FT TRANSMEM 437..447
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT TRANSMEM 450..461
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT TRANSMEM 464..473
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT TRANSMEM 477..487
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 27..396
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000250|UniProtKB:P0C2W0"
FT REGION 154..278
FT /note="Head domain"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 279..294
FT /note="Neck"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 295..332
FT /note="Right-handed coiled-coil (RHcc)"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 333..358
FT /note="Saddle domain"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 359..417
FT /note="Left-handed coiled-coil (LHcc)"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 394..436
FT /note="Outer membrane translocation of the passenger
FT domain"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT REGION 437..487
FT /note="Translocator domain"
FT /evidence="ECO:0000250|UniProtKB:Q9MCI8"
FT COILED 379..422
FT /evidence="ECO:0000255"
SQ SEQUENCE 487 AA; 51605 MW; D959C67EF7C21CF3 CRC64;
MSKKFTMTLL SSSLAGLLVM SGGVSAQEEK YTVPYAIGEG KWGNTYEVVK TGGNGNFRYE
VKEKNGKKRS LFTFDSKGDV IINGSGITYT IHDGALNDFA QTAEKKKNGQ SQSHRMTDSV
VRDVYNKVYS LQRTKITGFS VEDGENGKVS LGSDAKASGE FSVAVGNGAK ATEKASTSVG
SWSAALGRQS VALGVGTYAY ANASTAAGTA AYVDGSAIYG TAIGNYAKVD KNATEGVALG
AKAISAHKNS VALGANSRTT RDNEVYIGYE EASGKAYKTR TLGGLTDGTR PSDAATVRQV
DRVKDSVEQL AQDTNTRLVV EAKKSREYTD SRTTVGVNPD GKLTRAEGAT KTIAVNDGLV
ALSGRTDRID YAVGSVDRRV TKNTQAIQSN TRQLQEHNAR LNSQQRQIRE NHEEMKRAAA
QSAALAGLFQ PYSVGKFNAT AALGGYSDKQ AVAVGVGYRF NEQTAAKAGI AASDGDVSYN
MGVNFEF
