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| | Organism Information | | Organism Name | Escherichia coli K12 | | Domain | Bacteria | | Classification | Family: Enterobacteriaceae
Order: "Enterobacteriales"
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria" | | Taxonomic ID (NCBI) | | | | | | | Genome Sequence(s) | | GenBank | | | EMBL | | | 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 Name | flu | | NCBI Gene ID | | | GenBank Gene Sequence | | | | | | | Protein Information | | Protein Name | Ag43α (Antigen 43 passenger domain) | | UniProtKB/SwissProt ID | | | NCBI RefSeq | | | EMBL-CDS | | | UniProtKB Sequence | | | Sequence length | 1039 AA | | Subcellular Location | Secreted | | Function | Self-associating autotransporters (SAAT). It is the extracellular passenger domain of the E. coli autotransporter which represents a branch of the type V secretion pathway. Mediates bacterial autoaggregation (Ag43 interacts with Ag43 intercellularly) and biofilm formation as well as adhesion to and invasion of mammalian cells. It causes frizzy colony morphology and cell settling. | | | | | | Protein Structure | | Homology Model | | | Homology Model File | | | | | | | Glycosylation Status | | Glycosylation Type | O (Ser) linked | | Experimentally Validated Glycosite(s) in Full Length Protein | (Signal pepide: 1-52; sequence beyond 551 is cleaved during secretion) T87, T113, S117, S135, T149, T150, T229, T232, T287/T288, S317, S332, S396, S406, S422, T487, S491, S503 | | Experimentally Validated Glycosite(s ) in Mature Protein | T35, T61, S65, S83, T97, T98, T177, T180, T235/T236, S265, S280, S344, S354, S370, T435, S439, S451 | | Glycosite(s) Annotated Protein Sequence | >sp|P39180|AG43_ECOLI Antigen 43 OS=Escherichia coli (strain K12) GN=flu PE=1 SV
=3
MKRHLNTCYRLVWNHMTGAFVVASELARARGKRGGVAVALSLAAVTSLPVLAADIVVHPG
ETVNGGTLAN
HDNQIVFGTTNGMTIST*(87)GLEYGPDNEANTGGQWVQDGGTANKT*(113)TVTS*(117)GGL
Q
RVNPGGSVSDTVIS*(135)AGGGQSLQGRAVNT*(149)T(150)LNGGEQWMHEGAIATGTVINDKGW
QVVKPG
TVATDTVVNTGAEGGPDAENGDTGQFVRGDAVRTTINKNGRQIVRAEGT*(229)ANT*(232)
TVVYAGGD
QTVHGHALDTTLNGGYQYVHNGGTASDTVVNSDGWQIVKNGGVAGNT*(287)T*(288)VNQK
GRLQVDAG
GTATNVTLKQGGALVTS*(317)TAATVTGINRLGAFS*(332)VVEGKADNVVLENGGRLD
VLTGHTATNT
RVDDGGTLDVRNGGTATTVSMGNGGVLLADSGAAVS*(396)GTRSDGKAFS*(406)IG
GGQADALMLEKG
SS*(422)FTLNAGDTATDTTVNGGLFTARGGTLAGTTTLNNGAILTLSGKTVNNDTLTI
REGDAL
LQGGSLT*(487)GNGS*(491)VEKSGSGTLTVS*(503)NTTLTQKAVNLNEGTLTLNDS
TVTTDVIAQRGTALKL
TGSTVLNGAIDPTNVTLASGATWNIPDNATVQSVVDDLSHAGQIHFTSTRTGKFVPAT
LK
VKNLNGQNGTISLRVRPDMAQNNADRLVIDGGRATGKTILNLVNAGNSASGLATSGKGIQ
VVEAINGATT
EEGAFVQGNRLQAGAFNYSLNRDSDESWYLRSENAYRAEVPLYASMLTQA
MDYDRIVAGSRSHQTGVNGENNSV
RLSIQGGHLGHDNNGGIARGATPESSGSYGFVRLEG
DLMRTEVAGMSVTAGVYGAAGHSSVDVKDDDGSRAGTV
RDDAGSLGGYLNLVHTSSGLWA
DIVAQGTRHSMKASSDNNDFRARGWGWLGSLETGLPFSITDNLMLEPQLQYT
WQGLSLDD
GKDNAGYVKFGHGSAQHVRAGFRLGSHNDMTFGEGTSSRAPLRDSAKHSVSELPVNWWVQ
PSVI
RTFSSRGDMRVGTSTAGSGMTFSPSQNGTSLDLQAGLEARVRENITLGVQAGYAHS
VSGSSAEGYNGQATLNVTF
| | Sequence Around Glycosites (21 AA) | FGTTNGMTISTGLEYGPDNEA
WVQDGGTANKTTVTSGGLQRV
GGTANKTTVTSGGLQRVNPGG
PGGSVSDTVISAGGGQSLQGR
GQSLQGRAVNTTLNGGEQWMH
QSLQGRAVNTTLNGGEQWMHE
NGRQIVRAEGTANTTVVYAGG
QIVRAEGTANTTVVYAGGDQT
IVKNGGVAGNTTVNQKGRLQV
VKNGGVAGNTTVNQKGRLQVD
TLKQGGALVTSTAATVTGINR
VTGINRLGAFSVVEGKADNVV
VLLADSGAAVSGTRSDGKAFS
SGTRSDGKAFSIGGGQADALM
ADALMLEKGSSFTLNAGDTAT
GDALLQGGSLTGNGSVEKSGS
LQGGSLTGNGSVEKSGSGTLT
EKSGSGTLTVSNTTLTQKAVN | | Glycosite Sequence Logo | | | Glycosite Sequence Logo | | | Technique(s) used for Glycosylation Detection | Labelling with digoxigenin (DIG)-conjugated hydrazide. Subsequently, the DIG-labelled structures were detected with peroxidase-conjugated anti-DIG antibodies.. | | Technique(s) used for Glycosylated Residue(s) Detection | Automated LC-ESI–MS/MS (liquid chromatography electrospray ionization tandem mass spectrometry) with CID (collision induced dissociation) and ETD (electron transfer dissociation) after β-elimination. | | Protein Glycosylation- Implication | Glycosylation protects Ag43α against native-state proteolysis and stabilizes it against thermal and chemical denaturation, and also increases its refolding rate. It reduces the stabilizing effect of Ca2+ ions, prevents Ca2+ to promote cell adhesion and inhibits the bacterial amyloid-forming ability of Ag43α. | | | | | | Glycan Information | | Glycan Annotation | Multiple heptose residues. | | | | | | Protein Glycosylation linked (PGL) gene(s) | | OST Gene Name | aah (autotransporter-adhesin-heptosyltransferase) charcaterized based on gene deletion studies | | OST Protein Name | Aah is the heptosyltransferase. Tib C (E. coli (ETEC) strain H10407) has sequence similarity with Aah gene and it can substitute function of Aah. | | | | | | Literature | | Reference(s) | 1) Knudsen, S.K., Stensballe, A., Franzmann, M., Westergaard, U.B. and Otzen, D.E. (2008) Effect of glycosylation on the extracellular domain of the Ag43 bacterial autotransporter: enhanced stability and reduced cellular aggregation. Biochem J, 412, 563-577. [PubMed: 18341480]
2) Sherlock, O., Dobrindt, U., Jensen, J.B., Munk Vejborg, R. and Klemm, P. (2006) Glycosylation of the self-recognizing Escherichia coli Ag43 autotransporter protein. J Bacteriol, 188, 1798-1807. [PubMed: 16484190] | | Additional Comments | Ag43 protein is involved in phase variable biofilm formation.
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. | | Year of Identification | 2006 | | Year of Validation | 2008 | | | | |
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