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Protein

AIDA-I autotransporter

Gene

aidA-I

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Potent bacterial adhesin that mediates bacterial attachment to a broad variety of human and other mammalian cells. AIDA possesses additional virulence properties, as it is capable of mediating bacterial autoaggregation via intercellular self-recognition and it is a highly efficient initiator of biofilm formation.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Virulence

Protein family/group databases

MEROPSiU69.001.
TCDBi1.B.12.1.1. the autotransporter-1 (at-1) family.

Names & Taxonomyi

Protein namesi
Recommended name:
AIDA-I autotransporter
Short name:
AIDA
Cleaved into the following 2 chains:
Alternative name(s):
AIDAc
Gene namesi
Name:aidA-I
Encoded oniPlasmid pIB60 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

Adhesin AIDA-I :
  • Secreted
  • Cell surface

  • Note: The N-terminal passenger domain containing the adhesin moity gains access to the surface.
AIDA-I translocator :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1003 – 101412Beta strandedSequence analysisAdd
BLAST
Topological domaini1015 – 102814ExtracellularSequence analysisAdd
BLAST
Transmembranei1029 – 103911Beta strandedSequence analysisAdd
BLAST
Topological domaini1040 – 10423PeriplasmicSequence analysis
Transmembranei1043 – 105513Beta strandedSequence analysisAdd
BLAST
Topological domaini1056 – 109439ExtracellularSequence analysisAdd
BLAST
Transmembranei1095 – 110612Beta strandedSequence analysisAdd
BLAST
Topological domaini1107 – 11071PeriplasmicSequence analysis
Transmembranei1108 – 111811Beta strandedSequence analysisAdd
BLAST
Topological domaini1119 – 112911ExtracellularSequence analysisAdd
BLAST
Transmembranei1130 – 114011Beta strandedSequence analysisAdd
BLAST
Topological domaini1141 – 11477PeriplasmicSequence analysis
Transmembranei1148 – 115912Beta strandedSequence analysisAdd
BLAST
Topological domaini1160 – 118122ExtracellularSequence analysisAdd
BLAST
Transmembranei1182 – 119312Beta strandedSequence analysisAdd
BLAST
Transmembranei1194 – 120411Beta strandedSequence analysisAdd
BLAST
Topological domaini1205 – 12095ExtracellularSequence analysis
Transmembranei1210 – 122112Beta strandedSequence analysisAdd
BLAST
Topological domaini1222 – 12221PeriplasmicSequence analysis
Transmembranei1223 – 123412Beta strandedSequence analysisAdd
BLAST
Topological domaini1235 – 124410ExtracellularSequence analysis
Transmembranei1245 – 125612Beta strandedSequence analysisAdd
BLAST
Transmembranei1257 – 126812Beta strandedSequence analysisAdd
BLAST
Topological domaini1269 – 12746ExtracellularSequence analysis
Transmembranei1275 – 128612Beta strandedSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane, Periplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 49491 PublicationAdd
BLAST
Chaini50 – 12861237AIDA-I autotransporterPRO_0000387573Add
BLAST
Chaini50 – 846797Adhesin AIDA-IPRO_0000002698Add
BLAST
Chaini847 – 1286440AIDA-I translocatorPRO_0000002699Add
BLAST

Post-translational modificationi

Glycosylated with an average of 19 heptose residues. Only the glycosylated form binds to mammalilan cells. But glycosylation of AIDA is not required for AIDA-mediated cell-cell aggregation, interaction with Ag43, and induction of biofilm formation.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei846 – 8472Cleavage; by autolysis

Keywords - PTMi

Autocatalytic cleavage, Glycoprotein

Proteomic databases

PRIDEiQ03155.

Miscellaneous databases

PMAP-CutDBQ03155.

Interactioni

Subunit structurei

Intercellular AIDA-AIDA interaction is responsible for bacterial autoaggregation. AIDA can also interact with antigen 43 (Ag43), and the resultant intercellular AIDA-Ag43 interaction causes cell aggregation.

Structurei

Secondary structure

1
1286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi966 – 97914Combined sources
Beta strandi1005 – 101713Combined sources
Beta strandi1021 – 103919Combined sources
Turni1044 – 10463Combined sources
Beta strandi1047 – 106620Combined sources
Turni1067 – 10693Combined sources
Beta strandi1072 – 109120Combined sources
Beta strandi1095 – 111521Combined sources
Beta strandi1120 – 114425Combined sources
Beta strandi1150 – 116819Combined sources
Beta strandi1178 – 11825Combined sources
Beta strandi1187 – 120014Combined sources
Beta strandi1214 – 122411Combined sources
Beta strandi1227 – 12304Combined sources
Beta strandi1235 – 12373Combined sources
Beta strandi1241 – 125313Combined sources
Beta strandi1255 – 126814Combined sources
Beta strandi1274 – 128411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MEEX-ray3.00A840-1286[»]
ProteinModelPortaliQ03155.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini998 – 1286289AutotransporterPROSITE-ProRule annotationAdd
BLAST

Domaini

The signal peptide, cleaved at the inner membrane, guides the polyprotein to the periplasmic space. Then, insertion of the C-terminal translocator domain (or beta-domain) in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface, with subsequent autocatalytic cleavage. Finally, the mature AIDA protein remains in contact with the cell surface via non-covalent interactions with the translocator pore.

Sequence similaritiesi

Contains 1 autotransporter (TC 1.B.12) domain. [View classification]PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Family and domain databases

Gene3Di2.160.20.20. 2 hits.
2.40.128.130. 1 hit.
InterProiIPR030930. AIDA.
IPR005546. Autotransporte_beta.
IPR024973. ESPR.
IPR006315. OM_autotransptr_brl.
IPR012332. P22_tailspike_C-like.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF16168. AIDA. 5 hits.
PF03797. Autotransporter. 1 hit.
PF13018. ESPR. 1 hit.
[Graphical view]
SMARTiSM00869. Autotransporter. 1 hit.
[Graphical view]
SUPFAMiSSF103515. SSF103515. 1 hit.
SSF51126. SSF51126. 2 hits.
TIGRFAMsiTIGR01414. autotrans_barl. 1 hit.
TIGR04415. O_hepto_targRPT. 13 hits.
PROSITEiPS51208. AUTOTRANSPORTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q03155-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKAYSIIWS HSRQAWIVAS ELARGHGFVL AKNTLLVLAV VSTIGNAFAV
60 70 80 90 100
NISGTVSSGG TVSSGETQIV YSGRGNSNAT VNSGGTQIVN NGGKTTATTV
110 120 130 140 150
NSSGSQNVGT SGATISTIVN SGGIQRVSSG GVASATNLSG GAQNIYNLGH
160 170 180 190 200
ASNTVIFSGG NQTIFSGGIT DSTNISSGGQ QRVSSGGVAS NTTINSSGAQ
210 220 230 240 250
NILSEEGAIS THISSGGNQY ISAGANATET IVNSGGFQRV NSGAVATGTV
260 270 280 290 300
LSGGTQNVSS GGSAISTSVY NSGVQTVFAG ATVTDTTVNS GGNQNISSGG
310 320 330 340 350
IVSETTVNVS GTQNIYSGGS ALSANIKGSQ IVNSEGTAIN TLVSDGGYQH
360 370 380 390 400
IRNGGIASGT IVNQSGYVNI SSGGYAESTI INSGGTLRVL SDGYARGTIL
410 420 430 440 450
NNSGRENVSN GGVSYNAMIN TGGNQYIYSD GEATAAIVNT SGFQRINSGG
460 470 480 490 500
TAPVQNSVVV TRTVSSAAKP FDAEVYSGGK QTVYLWRGIW YSNFLTAVWS
510 520 530 540 550
MFPGTASGAN VNLSGRLNAF AGNVVGTILN QEGRQYVYSG ATATSTVGNN
560 570 580 590 600
EGREYVLSGG ITDGTVLNSG GLQAVSSGGK ASATVINEGG AQFVYDGGQV
610 620 630 640 650
TGTNIKNGGT IRVDSGASAL NIALSSGGNL FTSTGATLPE LTTMAALSVS
660 670 680 690 700
QNHASNIVLE NGGLLRVTSG GTATDTTVNS AGRLRIDDGG TINGTTTINA
710 720 730 740 750
DGIVAGTNIQ NDGNFILNLA ENYDFETELS GSGVLVKDNT GIMTYAGTLT
760 770 780 790 800
QAQGVNVKNG GIIFDSAVVN ADMAVNQNAY INISDQATIN GSVNNNGSIV
810 820 830 840 850
INNSIINGNI TNDADLSFGT AKLLSATVNG SLVNNKNIIL NPTKESAGNT
860 870 880 890 900
LTVSNYTGTP GSVISLGGVL EGDNSLTDRL VVKGNTSGQS DIVYVNEDGS
910 920 930 940 950
GGQTRDGINI ISVEGNSDAE FSLKNRVVAG AYDYTLQKGN ESGTDNKGWY
960 970 980 990 1000
LTSHLPTSDT RQYRPENGSY ATNMALANSL FLMDLNERKQ FRAMSDNTQP
1010 1020 1030 1040 1050
ESASVWMKIT GGISSGKLND GQNKTTTNQF INQLGGDIYK FHAEQLGDFT
1060 1070 1080 1090 1100
LGIMGGYANA KGKTINYTSN KAARNTLDGY SVGVYGTWYQ NGENATGLFA
1110 1120 1130 1140 1150
ETWMQYNWFN ASVKGDGLEE EKYNLNGLTA SAGGGYNLNV HTWTSPEGIT
1160 1170 1180 1190 1200
GEFWLQPHLQ AVWMGVTPDT HQEDNGTVVQ GAGKNNIQTK AGIRASWKVK
1210 1220 1230 1240 1250
STLDKDTGRR FRPYIEANWI HNTHEFGVKM SDDSQLLSGS RNQGEIKTGI
1260 1270 1280
EGVITQNLSV NGGVAYQAGG HGSNAISGAL GIKYSF
Length:1,286
Mass (Da):132,272
Last modified:June 1, 1994 - v1
Checksum:iB2A00F72AC05FB34
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti115 – 1151I → V AA sequence (PubMed:15950405).Curated
Sequence conflicti339 – 3391I → L AA sequence (PubMed:15950405).Curated
Sequence conflicti348 – 3481Y → S AA sequence (PubMed:15950405).Curated
Sequence conflicti351 – 3511I → L AA sequence (PubMed:15950405).Curated
Sequence conflicti388 – 3881R → B AA sequence (PubMed:15950405).Curated
Sequence conflicti396 – 3972RG → BE AA sequence (PubMed:15950405).Curated
Sequence conflicti399 – 3991I → L AA sequence (PubMed:15950405).Curated
Sequence conflicti410 – 4101N → D AA sequence (PubMed:15950405).Curated
Sequence conflicti528 – 5281I → L AA sequence (PubMed:15950405).Curated
Sequence conflicti683 – 6831R → M AA sequence (PubMed:15950405).Curated
Sequence conflicti692 – 6932IN → VD AA sequence (PubMed:15950405).Curated
Sequence conflicti695 – 6951T → S AA sequence (PubMed:15950405).Curated
Sequence conflicti698 – 6981I → L AA sequence (PubMed:15950405).Curated
Sequence conflicti829 – 8291N → D AA sequence (PubMed:15950405).Curated
Sequence conflicti850 – 8512TL → VV AA sequence (PubMed:15950405).Curated
Sequence conflicti854 – 8541S → V AA sequence (PubMed:15950405).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65022 Genomic DNA. Translation: CAA46156.1.
PIRiS28634.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65022 Genomic DNA. Translation: CAA46156.1.
PIRiS28634.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4MEEX-ray3.00A840-1286[»]
ProteinModelPortaliQ03155.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiU69.001.
TCDBi1.B.12.1.1. the autotransporter-1 (at-1) family.

Proteomic databases

PRIDEiQ03155.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

PMAP-CutDBQ03155.

Family and domain databases

Gene3Di2.160.20.20. 2 hits.
2.40.128.130. 1 hit.
InterProiIPR030930. AIDA.
IPR005546. Autotransporte_beta.
IPR024973. ESPR.
IPR006315. OM_autotransptr_brl.
IPR012332. P22_tailspike_C-like.
IPR011050. Pectin_lyase_fold/virulence.
[Graphical view]
PfamiPF16168. AIDA. 5 hits.
PF03797. Autotransporter. 1 hit.
PF13018. ESPR. 1 hit.
[Graphical view]
SMARTiSM00869. Autotransporter. 1 hit.
[Graphical view]
SUPFAMiSSF103515. SSF103515. 1 hit.
SSF51126. SSF51126. 2 hits.
TIGRFAMsiTIGR01414. autotrans_barl. 1 hit.
TIGR04415. O_hepto_targRPT. 13 hits.
PROSITEiPS51208. AUTOTRANSPORTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "AIDA-I, the adhesin involved in diffuse adherence of the diarrhoeagenic Escherichia coli strain 2787 (O126:H27), is synthesized via a precursor molecule."
    Benz I., Schmidt M.A.
    Mol. Microbiol. 6:1539-1546(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 50-56.
    Strain: O126:H27 / 2787 / DAEC.
  2. "Characterization and immuno-detection of AIDA-I adhesin isolated from porcine Escherichia coli."
    Fang Y., Ngeleka M., Middleton D.M., Simko E.
    Vet. Microbiol. 109:65-73(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 112-117; 338-352; 388-393; 396-405; 408-414; 473-480; 520-530; 679-685; 691-698; 797-804; 822-836 AND 847-855.
    Strain: PD20 and PD58.
  3. "Processing of the AIDA-I precursor: removal of AIDAc and evidence for the outer membrane anchoring as a beta-barrel structure."
    Suhr M., Benz I., Schmidt M.A.
    Mol. Microbiol. 22:31-42(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 847-856; 927-934 AND 948-964.
    Strain: O126:H27 / 2787 / DAEC.
  4. "Characterization of the essential transport function of the AIDA-I autotransporter and evidence supporting structural predictions."
    Maurer J., Jose J., Meyer T.F.
    J. Bacteriol. 181:7014-7020(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY OF THE TRANSLOCATOR DOMAIN.
  5. "Novel roles for the AIDA adhesin from diarrheagenic Escherichia coli: cell aggregation and biofilm formation."
    Sherlock O., Schembri M.A., Reisner A., Klemm P.
    J. Bacteriol. 186:8058-8065(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GLYCOSYLATION.

Entry informationi

Entry nameiAIDA_ECOLX
AccessioniPrimary (citable) accession number: Q03155
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 11, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.