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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

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)DescriptionActionsGraphical viewLength
Transmembranei1003 – 1014Beta strandedSequence analysisAdd BLAST12
Topological domaini1015 – 1028ExtracellularSequence analysisAdd BLAST14
Transmembranei1029 – 1039Beta strandedSequence analysisAdd BLAST11
Topological domaini1040 – 1042PeriplasmicSequence analysis3
Transmembranei1043 – 1055Beta strandedSequence analysisAdd BLAST13
Topological domaini1056 – 1094ExtracellularSequence analysisAdd BLAST39
Transmembranei1095 – 1106Beta strandedSequence analysisAdd BLAST12
Topological domaini1107PeriplasmicSequence analysis1
Transmembranei1108 – 1118Beta strandedSequence analysisAdd BLAST11
Topological domaini1119 – 1129ExtracellularSequence analysisAdd BLAST11
Transmembranei1130 – 1140Beta strandedSequence analysisAdd BLAST11
Topological domaini1141 – 1147PeriplasmicSequence analysis7
Transmembranei1148 – 1159Beta strandedSequence analysisAdd BLAST12
Topological domaini1160 – 1181ExtracellularSequence analysisAdd BLAST22
Transmembranei1182 – 1193Beta strandedSequence analysisAdd BLAST12
Transmembranei1194 – 1204Beta strandedSequence analysisAdd BLAST11
Topological domaini1205 – 1209ExtracellularSequence analysis5
Transmembranei1210 – 1221Beta strandedSequence analysisAdd BLAST12
Topological domaini1222PeriplasmicSequence analysis1
Transmembranei1223 – 1234Beta strandedSequence analysisAdd BLAST12
Topological domaini1235 – 1244ExtracellularSequence analysis10
Transmembranei1245 – 1256Beta strandedSequence analysisAdd BLAST12
Transmembranei1257 – 1268Beta strandedSequence analysisAdd BLAST12
Topological domaini1269 – 1274ExtracellularSequence analysis6
Transmembranei1275 – 1286Beta strandedSequence analysisAdd BLAST12

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane, Periplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 491 PublicationAdd BLAST49
ChainiPRO_000038757350 – 1286AIDA-I autotransporterAdd BLAST1237
ChainiPRO_000000269850 – 846Adhesin AIDA-IAdd BLAST797
ChainiPRO_0000002699847 – 1286AIDA-I translocatorAdd BLAST440

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)DescriptionActionsGraphical viewLength
Sitei846 – 847Cleavage; by autolysis2

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

11286
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi966 – 979Combined sources14
Beta strandi1005 – 1017Combined sources13
Beta strandi1021 – 1039Combined sources19
Turni1044 – 1046Combined sources3
Beta strandi1047 – 1066Combined sources20
Turni1067 – 1069Combined sources3
Beta strandi1072 – 1091Combined sources20
Beta strandi1095 – 1115Combined sources21
Beta strandi1120 – 1144Combined sources25
Beta strandi1150 – 1168Combined sources19
Beta strandi1178 – 1182Combined sources5
Beta strandi1187 – 1200Combined sources14
Beta strandi1214 – 1224Combined sources11
Beta strandi1227 – 1230Combined sources4
Beta strandi1235 – 1237Combined sources3
Beta strandi1241 – 1253Combined sources13
Beta strandi1255 – 1268Combined sources14
Beta strandi1274 – 1284Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MEEX-ray3.00A840-1286[»]
ProteinModelPortaliQ03155.
SMRiQ03155.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini998 – 1286AutotransporterPROSITE-ProRule annotationAdd BLAST289

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)DescriptionActionsGraphical viewLength
Sequence conflicti115I → V AA sequence (PubMed:15950405).Curated1
Sequence conflicti339I → L AA sequence (PubMed:15950405).Curated1
Sequence conflicti348Y → S AA sequence (PubMed:15950405).Curated1
Sequence conflicti351I → L AA sequence (PubMed:15950405).Curated1
Sequence conflicti388R → B AA sequence (PubMed:15950405).Curated1
Sequence conflicti396 – 397RG → BE AA sequence (PubMed:15950405).Curated2
Sequence conflicti399I → L AA sequence (PubMed:15950405).Curated1
Sequence conflicti410N → D AA sequence (PubMed:15950405).Curated1
Sequence conflicti528I → L AA sequence (PubMed:15950405).Curated1
Sequence conflicti683R → M AA sequence (PubMed:15950405).Curated1
Sequence conflicti692 – 693IN → VD AA sequence (PubMed:15950405).Curated2
Sequence conflicti695T → S AA sequence (PubMed:15950405).Curated1
Sequence conflicti698I → L AA sequence (PubMed:15950405).Curated1
Sequence conflicti829N → D AA sequence (PubMed:15950405).Curated1
Sequence conflicti850 – 851TL → VV AA sequence (PubMed:15950405).Curated2
Sequence conflicti854S → V AA sequence (PubMed:15950405).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MEEX-ray3.00A840-1286[»]
ProteinModelPortaliQ03155.
SMRiQ03155.
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...

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 2, 2016
This is version 96 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.