ProGP55

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ProGP ID ProGP55
Validation Status Characterized
Organism Information
Organism NameAcetogenium kivui (Thermoanaerobacter kivui)
Domain Bacteria
Classification Family: Thermoanaerobacteraceae
Order: Thermoanaerobacterales
Class: Clostridia
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI) 2325
Genome Sequence(s)
EMBL M31069
Protein Information
Protein NameCell surface protein/ S-layer protein
UniProtKB/SwissProt ID P22258
EMBL-CDSAAA21930.1
UniProtKB Sequence >sp|P22258|SLAP_ACEKI Cell surface protein OS=Acetogenium kivui PE=1 SV=1 MKNLKKLIAVVSTFALVFSAMAVGFAATTPFTDVKDDAPYASAVARLYALNITNGVGDPK FGVDQPVTRAQMITFVNRMLGYEDLAEMAKSEKSAFKDVPQNHWAVGQINLAYKLGLAQG VGNGKFDPNSELRYAQALAFVLRALGFKDLDWPYGYLAKAQDLGLVHGLNLAYNGVIKRG DLALILDRALEVPMVKYVDGKEVLGEPLISKVATKAEYTVIATNAQDRSVEEGKVAVLDK DGKLTTINAGLVDFSEYLGKKVIVYSERFGDPVYVAEGDNDVVSFTEGQDSVGTTVYKND DNKTAIKVDDNAYVLYNGYLTKVSKVTVKEGAEVTIINNNYLIVNGSYDNSTIVYNDVQS GDKYLNRDSNYELKGTVTVTGAVSKVTDIKANDYIYYGKQYDVNGNVVGTVIYVVRNQVT GTVTEKSVSGSTYKASIDNVSYTVADNNVWNQLEPGKKVTVILNKDNVIVGISSTTTTTA VNYAIFKEKSDPFTAWFAKVKLILPDAAEKVFDAVYSDVYDKVNLAEGTIVTYTVDANGK LNDIQRANDQPFSSASYKADAKVLTEGSTTYYITDNTVLLNNTSDGYKALKLTDLKDATN LNVKIVADNYNVAKVVVFNNASFVSTTTSTVYAYVTGTADVYVNGSTFTRLTVLENGQTK TYDANAQLATNYTHKAVVLTLTNAKIANIALPTVASGVKLTNIDQANLRITDTTNKGYLL DPNFIVVDTNGNLKGLSDITKDTGVNLYTNDVGKVFVIEIVQ
Sequence length 762 AA
Subcellular LocationSurface
Function The S-layer is a paracrystalline mono-layered assembly of proteins which coat the surface of bacteria. This bacterium is covered by a S-layer with hexagonal symmetry.
Glycosylation Status
Glycosylation Type O (Tyr) linked
Experimentally Validated Glycosite(s) in Full Length ProteinY297, Y516, Y520, Y632
Experimentally Validated Glycosite(s ) in Mature ProteinY297, Y516, Y520, Y632
Glycosite(s) Annotated Protein Sequence >sp|P22258|SLAP_ACEKI Cell surface protein OS=Acetogenium kivui PE=1 SV=1 MKNLKKLIAVVSTFALVFSAMAVGFAATTPFTDVKDDAPYASAVARLYALNITNGVGDPK FGVDQPVTRAQMITFVNRMLGYEDLAEMAKSEKSAFKDVPQNHWAVGQINLAYKLGLAQG VGNGKFDPNSELRYAQALAFVLRALGFKDLDWPYGYLAKAQDLGLVHGLNLAYNGVIKRG DLALILDRALEVPMVKYVDGKEVLGEPLISKVATKAEYTVIATNAQDRSVEEGKVAVLDK DGKLTTINAGLVDFSEYLGKKVIVYSERFGDPVYVAEGDNDVVSFTEGQDSVGTTVY*(297)KND DNKTAIKVDDNAYVLYNGYLTKVSKVTVKEGAEVTIINNNYLIVNGSYDNSTIVYNDVQS GDKYLNRDSNYELKGTVTVTGAVSKVTDIKANDYIYYGKQYDVNGNVVGTVIYVVRNQVT GTVTEKSVSGSTYKASIDNVSYTVADNNVWNQLEPGKKVTVILNKDNVIVGISSTTTTTA VNYAIFKEKSDPFTAWFAKVKLILPDAAEKVFDAVY*(516)SDVY*(520)DKVNLAEGTIVTYTVDANGK LNDIQRANDQPFSSASYKADAKVLTEGSTTYYITDNTVLLNNTSDGYKALKLTDLKDATN LNVKIVADNYNVAKVVVFNNASFVSTTTSTVY*(632)AYVTGTADVYVNGSTFTRLTVLENGQTK TYDANAQLATNYTHKAVVLTLTNAKIANIALPTVASGVKLTNIDQANLRITDTTNKGYLL DPNFIVVDTNGNLKGLSDITKDTGVNLYTNDVGKVFVIEIVQ
Sequence Around Glycosites (21 AA) EGQDSVGTTVYKNDDNKTAIK
DAAEKVFDAVYSDVYDKVNLA
KVFDAVYSDVYDKVNLAEGTI
SFVSTTTSTVYAYVTGTADVY
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionDeglycosylation (trifluoromethanesulfonic acid), aberrant migration on SDS-PAGE.
Technique(s) used for Glycosylated Residue(s) Detection Protease digestion and glycopeptide separation by molecular sieve chromatography and reversed-phase HPLC. Deglycosylated and undeglycosylated peptides were run on 2D PAGE and subjected to N-terminal sequencing post blotting.
Protein Glycosylation- Implication An N terminal SLH sequence of A. kivui S layer glycoprotein is suggested to fold independently and present itself in a modular way that may serve as an anchor to the peptidoglycan. Glycosylated residues are surface exposed and implicated in protease K resistance.
Glycan Information
Glycan Annotation Carbohydrate content 8% corresponding to 40 to 50 sugar molecules per protein monomer. Acidic, repetitive heterogenous glycans of varying length containing N-acetylglucosamine, 1,6 linked glucose, 1,4 linked galactosamine and/or unidentified sugar-related component.
Technique(s) used for Glycan Identification Hydrazinolysis followed by amino-acid analysis as well as two-dimensional NMR spectroscopy
Literature
Additional CommentA new recognition sequence for tyrosine linked glycosylation in A. kivui is suggested based on the fact that all glycosylated tyrosine in the sequence are preceded by valine.
Year of Identification1989
Year of Identification Month Wise1989.11.01
Year of Validation 1992
Reference Peters, J., Rudolf, S., Oschkinat, H., Mengele, R., Sumper, M., Kellermann, J., Lottspeich, F. and Baumeister, W. (1992) Evidence for tyrosine-linked glycosaminoglycan in a bacterial surface protein. Biol Chem Hoppe Seyler, 373, 171-176. [PubMed: 1596358]
Author Peters, J., Rudolf, S., Oschkinat, H., Mengele, R., Sumper, M., Kellermann, J., Lottspeich, F. Baumeister, W.
Research GroupMax-Planck-Institut für Biochemie, Martinsried bei München.
Corresponding Author Baumeister, W.
ContactMax-Planck-Institut für Biochemie, Martinsried bei München.
Reference Peters, J., Rudolf, S., Oschkinat, H., Mengele, R., Sumper, M., Kellermann, J., Lottspeich, F. and Baumeister, W. (1992) Evidence for tyrosine-linked glycosaminoglycan in a bacterial surface protein. Biol Chem Hoppe Seyler, 373, 171-176. [PubMed: 1596358]
Author Peters, J., Rudolf, S., Oschkinat, H., Mengele, R., Sumper, M., Kellermann, J., Lottspeich, F. and Baumeister, W.
Research GroupMax-Planck-Institut für Biochemie, Martinsried bei München.
Corresponding Author Baumeister, W.
ContactMax-Planck-Institut für Biochemie, Martinsried bei München.
Reference1) Lupas, A., Engelhardt, H., Peters, J., Santarius, U., Volker, S. and Baumeister, W. (1994) Domain structure of the Acetogenium kivui surface layer revealed by electron crystallography and sequence analysis. J Bacteriol, 176, 1224-1233. [PubMed: 8113161]
Author Lupas, A., Engelhardt, H., Peters, J., Santarius, U., Volker, S. and Baumeister, W.
Research GroupMax-Planck-Institut für Biochemie, Martinsried, Germany
Corresponding Author Baumeister, W.
ContactMax-Planck-Institut für Biochemie, Martinsried, Germany
Reference Peters, J., Peters, M., Lottspeich, F., Baumeister, W.(1989) S-layer protein gene of Acetogenium kivui: cloning and expression in Escherichia coli and determination of the nucleotide sequence. J Bacteriol, 171, 6307-6315. [PubMed: 2681162]
AuthorBaumeister, W
Research GroupMax-Planck-Institut für Biochemie, Martinsried, Federal Republic of Germany.
Corresponding Author Peters, J., Peters, M., Lottspeich, F. Baumeister, W
ContactMax-Planck-Institut für Biochemie, Martinsried, Federal Republic of Germany.