ProGP412 (OmpA/MotB)

Home -> ProGPdb -> Search ProGP -> Display data

ProGP ID ProGP412 (OmpA/MotB)
Validation Status Characterized
Organism Information
Organism NameAcinetobacter baumannii ATCC 17978
Domain Bacteria
Classification Family: Moraxellaceae
Order: Pseudomonadales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 400667
Genome Information
GenBank CP000521.1
EMBL CP018664.1
Organism Additional Information Acinetobacter baumannii is an opportunistic nosocomial pathogen infecting immunocompromised patients. It causes pneumonia, septicaemia, urinary tract infections and meningitis. There has been a rise in the multidrug-resistant as well as pandrug-resistant strains of the ?superbug?.
Gene Information
Gene NameA1S_1193
GenBank Gene Sequence CP000521.1
Protein Information
Protein NameOmpA/MotB
NCBI RefSeq ABO11623
EMBL-CDSABO11623.1
UniProtKB Sequence >ABO11623.2 OmpA/MotB [Acinetobacter baumannii ATCC 17978] MSINPIELLKEKVSSTILNNQDGYLGEKTNALSKFYPILLSLLAAKPDLIGQLKNSLAPSLSDLFSHNEQ IKNTVLTHLSGTAPNNEIENTLNSALKPSLNAISDVAGNDQQSIVNYLRQHAETIRSYLPGWAVGLLAPL GIGAGLSSVTSSTAPPLAAATETTGKSRGFLPIIALIILGLLIAWLWRSCQHKEATPAPETKAASGVEAA AAPATLTLSTDDKGAVSQCQAGIGDQGFLATLQTQVKQVFSATKDCDVDTSQTYAAAFTDKDALAGVLGA LKGIPNASLEWVGDKITLKAGDAAALEALTAKVKALVPHTEVVAAAPETAEQSVSNSLSASQTALTAIDP NNVDVNALVKALNLQIINFASGSSDIPADNKAILDQAATLLNKVSGVKLDVGGHTDSTGNAAANKALSQR RAQAVVDYLVSKGVDASKLVAKGHGSEQPVADNTTEEGRFKNRRIEFSVAQ
Sequence length 471 AA
Subcellular LocationOuter Membrane
Function Shows homology with peptidoglycan binding and outer membrane stabilizing proteins
Glycosylation Status
Glycosylation Type O- (Ser/Thr) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS205
Glycosite(s) Annotated Protein Sequence >ABO11623.2 OmpA/MotB [Acinetobacter baumannii ATCC 17978] MSINPIELLKEKVSSTILNNQDGYLGEKTNALSKFYPILLSLLAAKPDLIGQLKNSLAPSLSDLFSHNEQ IKNTVLTHLSGTAPNNEIENTLNSALKPSLNAISDVAGNDQQSIVNYLRQHAETIRSYLPGWAVGLLAPL GIGAGLSSVTSSTAPPLAAATETTGKSRGFLPIIALIILGLLIAWLWRSCQHKEATPAPETKAAS*(205)GVEAA AAPATLTLSTDDKGAVSQCQAGIGDQGFLATLQTQVKQVFSATKDCDVDTSQTYAAAFTDKDALAGVLGA LKGIPNASLEWVGDKITLKAGDAAALEALTAKVKALVPHTEVVAAAPETAEQSVSNSLSASQTALTAIDP NNVDVNALVKALNLQIINFASGSSDIPADNKAILDQAATLLNKVSGVKLDVGGHTDSTGNAAANKALSQR RAQAVVDYLVSKGVDASKLVAKGHGSEQPVADNTTEEGRFKNRRIEFSVAQ
Sequence Around Glycosites (21 AA) ATPAPETKAASGVEAAAAPAT
Technique(s) used for Glycosylation DetectionZIC HILIC and Mass spectrometry (LTQ-Orbitrap Velos)
Technique(s) used for Glycosylated Residue(s) Detection GluC/trypsin cocktail digestion, HILIC-enrichment and LC-MS/UVPD
Glycan Information
Glycan Annotation Pentasaccharide β-GlcNAc3NAcA4OAc-4-(β-GlcNAc-6-)-α-Gal-6-β-Glc-3-β-GalNAc-S/T. β-GlcNAc3NAcA4OAcA is an O-acetylated derivative of glucuronic acid.
BCSDB ID 29567
GlyTouCan G82631BC
Technique(s) used for Glycan Identification 1H:13C HSQC 2D NMR and mass spectrometry
Protein Glycosylation linked (PGL) gene(s)
OST Gene NamePglLAb
OST ProGT IDProGT55 (PglLAb)
Literature
ReferenceIwashkiw, J.A., Seper, A., Weber, B.S., Scott, N.E., Vinogradov, E., Stratilo, C., Reiz, B., Cordwell, S.J., Whittal, R., Schild, S. and Feldman, M.F., 2012. Identification of a general O-linked protein glycosylation system in Acinetobacter baumannii and its role in virulence and biofilm formation. PLoS pathogens, 8(6), p.e1002758.
Corresponding Author Mario F Feldman
ContactAlberta Glycomics Centre, Department of Biological Sciences, University of Alberta, Edmonton, Alberta, Canada
ReferenceIwashkiw JA, Seper A, Weber BS, Scott NE, Vinogradov E, Stratilo C, Reiz B, Cordwell SJ, Whittal R, Schild S, Feldman MF. (2012) Identification of a general O-linked protein glycosylation system in Acinetobacter baumannii and its role in virulence and biofilm formation. PLoS Pathog., 8(6):e1002758. [PubMed: 22685409]
AuthorIwashkiw JA, Seper A, Weber BS, Scott NE, Vinogradov E, Stratilo C, Reiz B, Cordwell SJ, Whittal R, Schild S, Feldman MF.
Research GroupAlberta Glycomics Centre, Department of Biological Sciences, University of Alberta, Edmonton, Alberta, Canada
Corresponding Author Feldman MF.
ContactAlberta Glycomics Centre, Department of Biological Sciences, University of Alberta, Edmonton, Alberta, Canada