ProGP202

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ProGP ID ProGP202
Validation Status Characterized
Organism Information
Organism NameEscherichia coli 2787 (O126:H27)
Domain Bacteria
Classification Family: Enterobacteriaceae
Order: "Enterobacteriales"
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 562
Genome Sequence(s)
GenBank GU810159
EMBL GU810159
Organism Additional Information Escherichia coli (Gram-negative) is the predominant facultative organism in the human intestine. It is responsible for a number of diseases like urinary tract infections, gastroenteritis (diarrhoea), meningitis, traveler's diarrhea and hemorrhagic colitis. There are a myriad of serotypes of pathogenic E. coli. Adhesion to the host cells is an important step in its pathogenesis. However, most strains are harmless and normal flora residing in the gut.
Gene Information
Gene NameaidA (plasmid encoded)
Protein Information
Protein NameDiffuse Adherence Adhesin (AIDA-I)
UniProtKB/SwissProt ID D7PPP4
EMBL-CDSADH10230.1
UniProtKB Sequence >tr|D7PPP4|D7PPP4_ECOLX Diffuse adherence adhesin OS=Escherichia coli GN=aidA PE=4 SV=1 MNKAYSIIWSHSRQAWIVASELARGHGFVLAKNTLLVLAVVSTIGNAFAVNISGTVSSGG TVSSGETQIVYSGGETSNATVNSGGTQIVNNGGKTTATTVNSSGSQNVGTSGATISTIVN SGGIQRVSSGGVASATNLSGGAQNIYNLGHASNTVIFSGGNQTIFSGGITDSTNISSGGQ QRVSSGGVASNTTINSSGAQNILSGGSAISTHISSGGNQYISAGANATETIVNSGGFQRV NSGAVATGTVLSGGTQNVSSGGSAISTSVYNSGVQTVFAGATVTDTTVNSGGNQNISSGG IVSETTVNVSGTQNIYSGGSALSANIKGSQIVNSEGTAINTLVSDGGYQHIRNGGIASGT IVNQSGYVNISSGGYAESTIINSGGTLRVLSDGYARGTILNNSGRENVSNGGVSYNAMIN TGGNQYIYSDGEATAAIVNTSGFQRINSGGTASGTKLSGGNQNVSSGGKAIDAEVYSGGK QTVYSGGEVSGTQIFNGGMVNVSGGTASGANVNLSGRLNAFAGNVVGTILNQEGRQYVYS GATATSTVGNNEGREYVLSGGITDGTVLNSGGLQAVSSGGKASATVINEGGAQFVYDGGQ VTGTNIKNGGTIRVDSGASALNIALSSGGNLFTSTGATVTGTNHYGSFSVSQNHASNIVL ENGGLLAVTSGGTATDTTVNSAGRLRIDDGGTINGTTTINADGIVAGTNIQNDGNFILNL AENYDFETELSGSGVLVKDNTGIMTYAGTLTQAQGVNVKNGGIIFDSAVVNADMAVNQNA YINISDQATINGSVNNNGSIVINNSIINGNITNDADLSFGTAKLLSATVNGSLVNNKNII LNPTKESAGNTLTVSNYTGTPGSVISLGGVLEGDNSLTDRLVVKGNTSGQSDIVYVNEDG SGGQTRDGINIISVEGNSDAEFSLKNRVVAGAYDYTLQKGNESGTDNKGWYLTSHLPTSD TRQYRPENGSYATNMALANSLFLMDLNERKQFRAMSDNTQPESASVWMKITGGRSSGKLN DGQNKTTTNQFINQLGGDIYKFHAEQLGDFTLGIMGGYANAKGKTINYTSNKAARNTLDG YSVGVYGTWYQNGENATGLFAETWMQYNWFNASVKGDGLEEEKYNLNGLTASAGGGYNLN VHTWTSPEGITGEFWLQPHLQAVWMGVTPDTHQEDNGTVVQGAGKNNIQTKAGIRASWKV KSTLDKDTGREFRPYIEANWIHNTHEFGVKMSDDSQLLSGSRNQGEIKTGIEGVITQNLS VNGGVAYQAGGHGSNAISGALGIKYSF
Sequence length 1287 AA
Subcellular LocationPeriplasm (Extracellular membrane associated)
Function Self-associating autotransporters (SAAT). Adhesin involved in diffuse adherence. Able to confer a pattern of diffuse adherence on the surface of cultured epithelial cells.
Glycosylation Status
Glycosylation Type O- (Ser) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS102, S111, S116, S242, S252, S334, S391, S409, S540, S546, S559, S570, S577, S578, S583, T154
Experimentally Validated Glycosite(s ) in Mature ProteinS102, S111, S116, S242, S252, S334, S391, S409, S540, S546, S559, S570, S577, S578, S583, T154
Glycosite(s) Annotated Protein Sequence >tr|D7PPP4|D7PPP4_ECOLX Diffuse adherence adhesin OS=Escherichia coli GN=aidA PE=4 SV=1 MNKAYSIIWSHSRQAWIVASELARGHGFVLAKNTLLVLAVVSTIGNAFAVNISGTVSSGG TVSSGETQIVYSGGETSNATVNSGGTQIVNNGGKTTATTVNS*(102)SGSQNVGTS*(111)GATIS*(116)TIVN SGGIQRVSSGGVASATNLSGGAQNIYNLGHASNT*(154)VIFSGGNQTIFSGGITDSTNISSGGQ QRVSSGGVASNTTINSSGAQNILSGGSAISTHISSGGNQYISAGANATETIVNSGGFQRV NS*(242)GAVATGTVLS*(252)GGTQNVSSGGSAISTSVYNSGVQTVFAGATVTDTTVNSGGNQNISSGG IVSETTVNVSGTQNIYSGGSALSANIKGSQIVNS*(334)EGTAINTLVSDGGYQHIRNGGIASGT IVNQSGYVNISSGGYAESTIINSGGTLRVLS*(391)DGYARGTILNNSGRENVS*(409)NGGVSYNAMIN TGGNQYIYSDGEATAAIVNTSGFQRINSGGTASGTKLSGGNQNVSSGGKAIDAEVYSGGK QTVYSGGEVSGTQIFNGGMVNVSGGTASGANVNLSGRLNAFAGNVVGTILNQEGRQYVYS*(540)GATATS*(546)TVGNNEGREYVLS*(559)GGITDGTVLNS*(570) GGLQAVS*(577)S*(578) GGKAS*(583)ATVINEGGAQFVYDGGQ VTGTNIKNGGTIRVDSGASALNIALSSGGNLFTSTGATVTGTNHYGSFSVSQNHASNIVL ENGGLLAVTSGGTATDTTVNSAGRLRIDDGGTINGTTTINADGIVAGTNIQNDGNFILNL AENYDFETELSGSGVLVKDNTGIMTYAGTLTQAQGVNVKNGGIIFDSAVVNADMAVNQNA YINISDQATINGSVNNNGSIVINNSIINGNITNDADLSFGTAKLLSATVNGSLVNNKNII LNPTKESAGNTLTVSNYTGTPGSVISLGGVLEGDNSLTDRLVVKGNTSGQSDIVYVNEDG SGGQTRDGINIISVEGNSDAEFSLKNRVVAGAYDYTLQKGNESGTDNKGWYLTSHLPTSD TRQYRPENGSYATNMALANSLFLMDLNERKQFRAMSDNTQPESASVWMKITGGRSSGKLN DGQNKTTTNQFINQLGGDIYKFHAEQLGDFTLGIMGGYANAKGKTINYTSNKAARNTLDG YSVGVYGTWYQNGENATGLFAETWMQYNWFNASVKGDGLEEEKYNLNGLTASAGGGYNLN VHTWTSPEGITGEFWLQPHLQAVWMGVTPDTHQEDNGTVVQGAGKNNIQTKAGIRASWKV KSTLDKDTGREFRPYIEANWIHNTHEFGVKMSDDSQLLSGSRNQGEIKTGIEGVITQNLS VNGGVAYQAGGHGSNAISGALGIKYSF
Sequence Around Glycosites (21 AA) GGKTTATTVNSSGSQNVGTSG
NSSGSQNVGTSGATISTIVNS
QNVGTSGATISTIVNSGGIQR
VNSGGFQRVNSGAVATGTVLS
SGAVATGTVLSGGTQNVSSGG
ANIKGSQIVNSEGTAINTLVS
INSGGTLRVLSDGYARGTILN
ILNNSGRENVSNGGVSYNAMI
LNQEGRQYVYSGATATSTVGN
QYVYSGATATSTVGNNEGREY
GNNEGREYVLSGGITDGTVLN
GGITDGTVLNSGGLQAVSSGG
VLNSGGLQAVSSGGKASATVI
LNSGGLQAVSSGGKASATVIN
LQAVSSGGKASATVINEGGAQ
NIYNLGHASNTVIFSGGNQTI
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionAberrant mobility on SDS-polyacrylamide gel, labelling with digoxigenin (DIG) hydrazide after periodate oxidation. The glycan was not detectable by common lectins and could not be deglycosylated by a broad spectrum of glycosidases.
Technique(s) used for Glycosylated Residue(s) Detection MS-MS (tandem mass spectrometry) and N-terminal sequencing of AIDA-I peptides
Protein Glycosylation- Implication Glycosylation is required to ensure a normal conformation of AIDA-I. Glycans could be involved in receptor recognition making it essential for adhesion but not for autoaggregation or biofilm formation. It also provides increased resistance to degradation. Only the glycosylated form binds to cultured epithelial cells. Further unglycosylated AIDA-I is expressed in smaller amounts than its relatively thermostable glycosylated form. Unglycosylated AIDA-I is more sensitive to proteases and induces important extracytoplasmic stress.
Glycan Information
Glycan Annotation Heterogenous multiple heptose residues (atleast 19 per protein molecule).
Technique(s) used for Glycan Identification Gas chromatography and mass spectrometry after methanolysis and carbohydrate labelling.
Protein Glycosylation linked (PGL) gene(s)
OST Gene NameAah is the heptosyltransferase. Tib C (E. coli (ETEC) strain H10407) has sequence similarity with Aah gene and it can substitute function of Aah.
OST ProGT IDProGT7
Additional CommentAIDA- I is primarily associated with pathogenic E. coli strains involved in neonatal and postweaning diarrhea in piglets.
The glycosylated peptides were identified in a region of the protein composed of imperfect 19-amino-acid repeats.
Glycosylation by heptoses represents a novel protein modification in eubacteria.
Sequon features: The N-terminal repeats of AIDA-I that contain multiple copies of the consensus sequence VXNSGG, might serve as acceptor sites for the AAH heptosyltransferase.
UniProtKB information is provided according to Ref. no. 1 in which glycosites have been confirmed.
Literature
Year of Identification2001
Year of Identification Month Wise2001.6.1
Year of Validation 2007
ReferenceCharbonneau, M.E., Girard, V., Nikolakakis, A., Campos, M., Berthiaume, F., Dumas, F., Lepine, F. and Mourez, M. (2007) O-linked glycosylation ensures the normal conformation of the autotransporter adhesin involved in diffuse adherence. J Bacteriol, 189, 8880-8889. [PubMed: 17951390]
AuthorCharbonneau, M.E., Girard, V., Nikolakakis, A., Campos, M., Berthiaume, F., Dumas, F., Lepine, F. and Mourez, M.
Research GroupUniversity of Montreal, Faculty of Veterinary Medicine, 3200 Sicotte, St.-Hyacinthe, Quebec J2S 7C6, Canada.
Corresponding Author Mourez, M.
ContactUniversity of Montreal, Faculty of Veterinary Medicine, 3200 Sicotte, St.-Hyacinthe, Quebec J2S 7C6, Canada.
Reference Sherlock, O., Schembri, M.A., Reisner, A. and Klemm, P. (2004) Novel roles for the AIDA adhesin from diarrheagenic Escherichia coli: cell aggregation and biofilm formation. J Bacteriol, 186, 8058-8065. [PubMed: 15547278]
Author Sherlock, O., Schembri, M.A., Reisner, A. Klemm, P.
Research GroupCentre for Biomedical Microbiology, BioCentrum-DTU, Bldg. 301, Technical University of Denmark, DK-2800 Lyngby, Denmark.
Corresponding Author Klemm, P.
ContactCentre for Biomedical Microbiology, BioCentrum-DTU, Bldg. 301, Technical University of Denmark, DK-2800 Lyngby, Denmark.
Reference Sherlock, O., Schembri, M.A., Reisner, A. and Klemm, P. (2004) Novel roles for the AIDA adhesin from diarrheagenic Escherichia coli: cell aggregation and biofilm formation. J Bacteriol, 186, 8058-8065. [PubMed: 15547278]
Author Sherlock, O., Schembri, M.A., Reisner, A. Klemm, P.
Research GroupCentre for Biomedical Microbiology, BioCentrum-DTU, Technical University of Denmark, DK-2800 Lyngby, Denmark.
Corresponding Author Klemm, P.
ContactCentre for Biomedical Microbiology, BioCentrum-DTU, Technical University of Denmark, DK-2800 Lyngby, Denmark.
Reference Moormann, C., Benz, I. and Schmidt, M.A. (2002) Functional substitution of the TibC protein of enterotoxigenic Escherichia coli strains for the autotransporter adhesin heptosyltransferase of the AIDA system. Infect Immun, 70, 2264-2270. [PubMed: 11953358]
Author Moormann, C., Benz, I. Schmidt, M.A.
Research GroupInstitute of Infectiology, Center for Molecular Biology of Inflammation, Westfälische Wilhelms-University Münster, D-48149 Münster, Germany.
ContactInstitute of Infectiology, Center for Molecular Biology of Inflammation, Westfälische Wilhelms-University Münster, D-48149 Münster, Germany.
Reference Benz, I. and Schmidt, M.A. (2001) Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA-I adhesin. Mol Microbiol, 40, 1403-1413. [PubMed: 11442838]
Author Benz, I. Schmidt, M.A.
Research Groupnstitute of Infectiology - Center for Molecular Biology of Inflammation (ZMBE), University Hospital Münster, Germany.
Corresponding Author Schmidt, M.A.
Contactnstitute of Infectiology - Center for Molecular Biology of Inflammation (ZMBE), University Hospital Münster, Germany.