ProGP497 (Putative secretion protein)
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ProGP ID | ProGP497 (Putative secretion protein) |
Validation Status | Uncharacterized |
Organism Information | |
Organism Name | Acinetobacter nosocomialis |
Domain | Bacteria |
Classification | Phylum : Proteobacteria Class : Gammaproteobacteria Orders : Pseudomonadales Family : Moraxellaceae Genus : Acinetobacter Species : nosocomialis |
Taxonomic ID (NCBI) | 106654 |
Genome Information | |
GenBank | CR543861 |
EMBL | CR543861 |
Organism Additional Information | Non-pathogenic species |
Protein Information | |
Protein Name | Putative secretion protein |
UniProtKB/SwissProt ID | Q6F814 |
NCBI RefSeq | WP_004924397.1 |
EMBL-CDS | CAG69801.1 |
UniProtKB Sequence | >tr|Q6F814|Q6F814_ACIAD Putative secretion protein (HlyD family) OS=Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1) GN=ACIAD3109 PE=3 SV=1 MPKIKPSRIVIIAISIVVIALLAWFFFKPKQQQPQYITETANYGNLENTVLATGTLDATK LISVGAQVSGQVKKMYVQLGDEVKQGQLIAQIDSTTQENSLKTADANIRNLEAQRLQQEA NLNEAQLAYRRQQQMFAQDATSKAELESAEATYKTAQAQIKAINAQIESAKVTRSTAQTN IGYTRIVAPTDGTVVAIVTEEGQTVNANQSAPTIVKIAKLQNMTIKAQVSEADIMKVEKG QQVYFTTLGDDKKRYATLRQIEPAPDSISSESTTSSTSSSSSSSTAIYYNALFDVPNEDG KLRIDMTAQVYIVLDSVNHALLVPSSALSTRSANSQGQSSSSKNTAASSVAATHKKDKTD GPKLERLNLTAEQKQAVEAGKATLSVVRVLNADGTAQPKQVLIGINNRVSAQVLAGLKAG DQVVIADSSDTAASTANSTNRRRNGPPMGM |
Sequence length | 450 AA |
Subcellular Location | Membrane |
Glycosylation Status | |
Glycosylation Type | O- (Ser/Thr) linked |
Technique(s) used for Glycosylation Detection | ZIC-HILIC for glycopeptide enrichment, multiple MS/MS fragmentation |
Glycan Information | |
Glycan Annotation | Pentasaccharide (HexNAc - HexNAc -HexNAc-HexNAc-HexNAc) |
Protein Glycosylation linked (PGL) gene(s) | |
OST Gene Name | PglLADP1 |
OST ProGT ID | ProGT83 |
Literature | |
Year of Identification | 2015 |
Year of Identification Month Wise | 2015.4.6 |
Reference | Harding, C.M., Nasr, M.A., Kinsella, R.L., Scott, N.E., Foster, L.J., Weber, B.S., Fiester, S.E., Actis, L.A., Tracy, E.N., Munson Jr, R.S. and Feldman, M.F., 2015. A cinetobacter strains carry two functional oligosaccharyltransferases, one devoted exclusively to type IV pilin, and the other one dedicated to O‐glycosylation of multiple proteins. Molecular microbiology, 96(5), pp.1023-1041. |
Corresponding Author | Mario F Feldman |
Contact | Department of Biological Sciences, University of Alberta, Edmonton, AB, T6G 2G2, Canada. |