AIDA_ECOLX
ID AIDA_ECOLX Reviewed; 1286 AA.
AC Q03155;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=AIDA-I autotransporter;
DE Short=AIDA;
DE Contains:
DE RecName: Full=Adhesin AIDA-I;
DE Contains:
DE RecName: Full=AIDA-I translocator;
DE AltName: Full=AIDAc;
DE Flags: Precursor;
GN Name=aidA-I;
OS Escherichia coli.
OG Plasmid pIB6.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 50-56.
RC STRAIN=O126:H27 / 2787 / DAEC;
RX PubMed=1625582; DOI=10.1111/j.1365-2958.1992.tb00875.x;
RA Benz I., Schmidt M.A.;
RT "AIDA-I, the adhesin involved in diffuse adherence of the diarrhoeagenic
RT Escherichia coli strain 2787 (O126:H27), is synthesized via a precursor
RT molecule.";
RL Mol. Microbiol. 6:1539-1546(1992).
RN [2]
RP PROTEIN SEQUENCE OF 112-117; 338-352; 388-393; 396-405; 408-414; 473-480;
RP 520-530; 679-685; 691-698; 797-804; 822-836 AND 847-855.
RC STRAIN=PD20, and PD58;
RX PubMed=15950405; DOI=10.1016/j.vetmic.2005.04.018;
RA Fang Y., Ngeleka M., Middleton D.M., Simko E.;
RT "Characterization and immuno-detection of AIDA-I adhesin isolated from
RT porcine Escherichia coli.";
RL Vet. Microbiol. 109:65-73(2005).
RN [3]
RP PROTEIN SEQUENCE OF 847-856; 927-934 AND 948-964.
RC STRAIN=O126:H27 / 2787 / DAEC;
RX PubMed=8899706; DOI=10.1111/j.1365-2958.1996.tb02653.x;
RA Suhr M., Benz I., Schmidt M.A.;
RT "Processing of the AIDA-I precursor: removal of AIDAc and evidence for the
RT outer membrane anchoring as a beta-barrel structure.";
RL Mol. Microbiol. 22:31-42(1996).
RN [4]
RP TOPOLOGY OF THE TRANSLOCATOR DOMAIN.
RX PubMed=10559167; DOI=10.1128/jb.181.22.7014-7020.1999;
RA Maurer J., Jose J., Meyer T.F.;
RT "Characterization of the essential transport function of the AIDA-I
RT autotransporter and evidence supporting structural predictions.";
RL J. Bacteriol. 181:7014-7020(1999).
RN [5]
RP FUNCTION, AND GLYCOSYLATION.
RX PubMed=15547278; DOI=10.1128/jb.186.23.8058-8065.2004;
RA Sherlock O., Schembri M.A., Reisner A., Klemm P.;
RT "Novel roles for the AIDA adhesin from diarrheagenic Escherichia coli: cell
RT aggregation and biofilm formation.";
RL J. Bacteriol. 186:8058-8065(2004).
CC -!- FUNCTION: Potent bacterial adhesin that mediates bacterial attachment
CC to a broad variety of human and other mammalian cells. AIDA possesses
CC additional virulence properties, as it is capable of mediating
CC bacterial autoaggregation via intercellular self-recognition and it is
CC a highly efficient initiator of biofilm formation.
CC {ECO:0000269|PubMed:15547278}.
CC -!- SUBUNIT: Intercellular AIDA-AIDA interaction is responsible for
CC bacterial autoaggregation. AIDA can also interact with antigen 43
CC (Ag43), and the resultant intercellular AIDA-Ag43 interaction causes
CC cell aggregation.
CC -!- SUBCELLULAR LOCATION: [AIDA-I autotransporter]: Periplasm.
CC -!- SUBCELLULAR LOCATION: [Adhesin AIDA-I]: Secreted. Cell surface.
CC Note=The N-terminal passenger domain containing the adhesin moiety
CC gains access to the surface.
CC -!- SUBCELLULAR LOCATION: [AIDA-I translocator]: Cell outer membrane
CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=The
CC cleaved AIDAc containing the translocator domain is localized in the
CC outer membrane.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC polyprotein to the periplasmic space. Then, insertion of the C-terminal
CC translocator domain (or beta-domain) in the outer membrane forms a
CC hydrophilic pore for the translocation of the passenger domain to the
CC bacterial cell surface, with subsequent autocatalytic cleavage.
CC Finally, the mature AIDA protein remains in contact with the cell
CC surface via non-covalent interactions with the translocator pore.
CC -!- PTM: Glycosylated with an average of 19 heptose residues. Only the
CC glycosylated form binds to mammalilan cells. But glycosylation of AIDA
CC is not required for AIDA-mediated cell-cell aggregation, interaction
CC with Ag43, and induction of biofilm formation.
CC {ECO:0000269|PubMed:15547278}.
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DR EMBL; X65022; CAA46156.1; -; Genomic_DNA.
DR PIR; S28634; S28634.
DR PDB; 4MEE; X-ray; 3.00 A; A=840-1286.
DR PDBsum; 4MEE; -.
DR AlphaFoldDB; Q03155; -.
DR SMR; Q03155; -.
DR MEROPS; U69.001; -.
DR TCDB; 1.B.12.1.1; the autotransporter-1 (at-1) family.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd01344; PL2_Passenger_AT; 1.
DR Gene3D; 2.160.20.20; -; 3.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR043990; AC_1.
DR InterPro; IPR030930; AIDA.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR024973; ESPR.
DR InterPro; IPR006315; OM_autotransptr_brl.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF18883; AC_1; 1.
DR Pfam; PF16168; AIDA; 3.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF13018; ESPR; 1.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF51126; SSF51126; 2.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR TIGRFAMs; TIGR04415; O_hepto_targRPT; 13.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autocatalytic cleavage; Cell adhesion; Cell outer membrane;
KW Direct protein sequencing; Glycoprotein; Membrane; Periplasm; Plasmid;
KW Secreted; Signal; Transmembrane; Transmembrane beta strand; Virulence.
FT SIGNAL 1..49
FT /evidence="ECO:0000269|PubMed:1625582"
FT CHAIN 50..1286
FT /note="AIDA-I autotransporter"
FT /id="PRO_0000387573"
FT CHAIN 50..846
FT /note="Adhesin AIDA-I"
FT /id="PRO_0000002698"
FT CHAIN 847..1286
FT /note="AIDA-I translocator"
FT /id="PRO_0000002699"
FT TRANSMEM 1003..1014
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1015..1028
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1029..1039
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1040..1042
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1043..1055
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1056..1094
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1095..1106
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1107
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1108..1118
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1119..1129
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1130..1140
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1141..1147
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1148..1159
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1160..1181
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1182..1193
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 1194..1204
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1205..1209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1210..1221
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1222
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1223..1234
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1235..1244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1245..1256
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TRANSMEM 1257..1268
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1269..1274
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1275..1286
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT DOMAIN 998..1286
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT SITE 846..847
FT /note="Cleavage; by autolysis"
FT CONFLICT 115
FT /note="I -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="Y -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="R -> B (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 396..397
FT /note="RG -> BE (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 410
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="R -> M (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 692..693
FT /note="IN -> VD (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 695
FT /note="T -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="I -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 829
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 850..851
FT /note="TL -> VV (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 854
FT /note="S -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 966..979
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1005..1017
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1021..1039
FT /evidence="ECO:0007829|PDB:4MEE"
FT TURN 1044..1046
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1047..1066
FT /evidence="ECO:0007829|PDB:4MEE"
FT TURN 1067..1069
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1072..1091
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1095..1115
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1120..1144
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1150..1168
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1178..1182
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1187..1200
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1214..1224
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1227..1230
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1235..1237
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1241..1253
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1255..1268
FT /evidence="ECO:0007829|PDB:4MEE"
FT STRAND 1274..1284
FT /evidence="ECO:0007829|PDB:4MEE"
SQ SEQUENCE 1286 AA; 132272 MW; B2A00F72AC05FB34 CRC64;
MNKAYSIIWS HSRQAWIVAS ELARGHGFVL AKNTLLVLAV VSTIGNAFAV NISGTVSSGG
TVSSGETQIV YSGRGNSNAT VNSGGTQIVN NGGKTTATTV NSSGSQNVGT SGATISTIVN
SGGIQRVSSG GVASATNLSG GAQNIYNLGH ASNTVIFSGG NQTIFSGGIT DSTNISSGGQ
QRVSSGGVAS NTTINSSGAQ NILSEEGAIS THISSGGNQY ISAGANATET IVNSGGFQRV
NSGAVATGTV LSGGTQNVSS GGSAISTSVY NSGVQTVFAG ATVTDTTVNS GGNQNISSGG
IVSETTVNVS GTQNIYSGGS ALSANIKGSQ IVNSEGTAIN TLVSDGGYQH IRNGGIASGT
IVNQSGYVNI SSGGYAESTI INSGGTLRVL SDGYARGTIL NNSGRENVSN GGVSYNAMIN
TGGNQYIYSD GEATAAIVNT SGFQRINSGG TAPVQNSVVV TRTVSSAAKP FDAEVYSGGK
QTVYLWRGIW YSNFLTAVWS MFPGTASGAN VNLSGRLNAF AGNVVGTILN QEGRQYVYSG
ATATSTVGNN EGREYVLSGG ITDGTVLNSG GLQAVSSGGK ASATVINEGG AQFVYDGGQV
TGTNIKNGGT IRVDSGASAL NIALSSGGNL FTSTGATLPE LTTMAALSVS QNHASNIVLE
NGGLLRVTSG GTATDTTVNS AGRLRIDDGG TINGTTTINA DGIVAGTNIQ NDGNFILNLA
ENYDFETELS GSGVLVKDNT GIMTYAGTLT QAQGVNVKNG GIIFDSAVVN ADMAVNQNAY
INISDQATIN GSVNNNGSIV INNSIINGNI TNDADLSFGT AKLLSATVNG SLVNNKNIIL
NPTKESAGNT LTVSNYTGTP GSVISLGGVL EGDNSLTDRL VVKGNTSGQS DIVYVNEDGS
GGQTRDGINI ISVEGNSDAE FSLKNRVVAG AYDYTLQKGN ESGTDNKGWY LTSHLPTSDT
RQYRPENGSY ATNMALANSL FLMDLNERKQ FRAMSDNTQP ESASVWMKIT GGISSGKLND
GQNKTTTNQF INQLGGDIYK FHAEQLGDFT LGIMGGYANA KGKTINYTSN KAARNTLDGY
SVGVYGTWYQ NGENATGLFA ETWMQYNWFN ASVKGDGLEE EKYNLNGLTA SAGGGYNLNV
HTWTSPEGIT GEFWLQPHLQ AVWMGVTPDT HQEDNGTVVQ GAGKNNIQTK AGIRASWKVK
STLDKDTGRR FRPYIEANWI HNTHEFGVKM SDDSQLLSGS RNQGEIKTGI EGVITQNLSV
NGGVAYQAGG HGSNAISGAL GIKYSF
