ProGP75

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ProGP ID ProGP75
Validation Status Uncharacterized
Organism Information
Organism NamePaenibacillus (Bacillus) alvei CCM 2051
Domain Bacteria
Classification Family: Paenibacillaceae
Order: Bacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI) 44250
Genome Sequence(s)
GenBank FJ751775
EMBL FJ751775
Gene Information
Gene NamespaA
Protein Information
Protein NameS-layer glycoprotein
UniProtKB/SwissProt ID C1JZ07
EMBL-CDSACN92046.1
UniProtKB Sequence >tr|C1JZ07|C1JZ07_PAEAL Surface (S-) layer glycoprotein OS=Paenibacillus alvei GN=spaA PE=4 SV=1 MKKRLALLLSVAMAFSMFANVAFGADAAKTTQEKFDALKEAGVFSGYPGTTDAKLGQDMT RAEFAKVLVKLFGLKEIHGQYSYKDKNYDAKNWAAPFIEAVTAEGLMQGKDLTKKIFDFN GKITVEEASKTLVTALKLEPVKDAQNKATDWAKGYFEAAVNAGLFSKDANPKANATRAQL VEAAFAADEMSKGPKVTSYKVIDSKTVEFTMSDKEVQKVTLDKALEPNKETEVTFTYKNK EGKEFKITTKVTYTITAAQKIESVTAENLKEVVVKFDGSLDKKSAEKADNYEVKDAKVDS AKLIDKNTVYVLLKEEDSSTMKNQKEIELKVKGVQNEDKSKTFDEKVKFTPMDVKTPEAK EVVGLGTKAFKVVFSEPVKKSGVFTTSNYKVDGKTVSASVKYVYPNIAIVSTDLSVGEHK LTVSNVEDFSGLKIAPVEKTFTIAEDTTAPKVVSAKAKDPMELEIEFNETVKSISKIYHG NSSNTGEVKIKDNIVTVKFEKSKALYLGENTVYIEGATDYSNNKANREVKVNPSLDAERP EVEKVELKNSDHQIILTFNKELDAASATNRDNYFLKDKDGKFFKHDAVNKNDGKILTTPT YKKDKKTVTIDLIKPLDEGDYILEVNGVKDNAYVSNTMLPFSKKITADAKSGPARAWTNY DANQDYIYIQFPKAVKTDGDGDATIKAKYTVFGKSLNDDYETPVLVQPDTIRIDAKRGTL LTTDGEVKNPYSPDVGATLIKDIDGDWFEGGENYKVEVKELGDAKVTWAEKATVKDRNEL KVKLTGKLNNVDVSDFKVTTVDGPKVPNSYQQDGNTLTLKFNDSNKLPVDLFGAQLVAVN DNSTDTFGNRIQKFTVDVNGELRPEATSVVVNKATVTGATYEAVVSVNSVVYTDFADTAQ FIKFFGVEVDSQKADIVKIEAATDGKAEQKSFKILFNLPTSVKEVKSDTRFRVELQDKGT SVVRDRQGNVIQDFYLPGTYSGK
Sequence length 983 AA
Subcellular LocationSurface
Function Structural component of the surface layer.
Glycosylation Status
Glycosylation Type O- (Tyr) linked
Technique(s) used for Glycosylation DetectionCarbohydrate determination
Glycan Information
Glycan Annotation β-D-Galp-(1→O)-Tyr glycosidic linkage unit. The glycan chains consist on average of twenty branched trisaccharide repeating units with the structure [→3)-β-D-Galp-(1→4)-[α-D-Glcp-(1→6)-]-β-D-ManpNAc-(1→]n. This O-antigen-like domain of the polysaccharide is connected with the S-layer polypeptide through the ‘‘core’’ structure →3)[GroA-(2→O)-PO2-(O→4)-β-D-ManpNAc-(1→4)]-α-L-Rhap-(1→3)-α-L-Rhap-(1→3)-α-L-Rhap-(1→3)-β-D-Galp-(1→O)-Tyr. Except for the substitution in position 4 of the nonreducing rhamnose with the modified glyceric acid phosphate residue GroA-2→OPO2→4-β-D-ManpNAc-(1→, this core is identical to the core of the Tyr-linked glycan from the S-layer glycoprotein of Tb. thermohydrosulfuricus L111-69.
BCSDB ID23154
Literature
Year of Identification1991
Year of Identification Month Wise1991.02
ReferenceMessner, P., Steiner, K., Zarschler, K. and Schaffer, C. (2008) S-layer nanoglycobiology of bacteria. Carbohydr Res, 343, 1934-1951. [PubMed: 18336801]
Author Messner, P., Steiner, K., Zarschler, K. Schaffer, C.
Research GroupUniversity of Natural Resources and Applied Life Sciences, Vienna, Center for NanoBiotechnology A-1180 Vienna, Gregor-Mendel-Strasse 33, Austria.
Corresponding Author Schaffer, C.
ContactUniversity of Natural Resources and Applied Life Sciences, Vienna, Center for NanoBiotechnology A-1180 Vienna, Gregor-Mendel-Strasse 33, Austria.
ReferenceMessner, P., Christian, R., Neuninger, C. and Schulz, G. (1995) Similarity of "core" structures in two different glycans of tyrosine-linked eubacterial S-layer glycoproteins. J Bacteriol, 177, 2188-2193. [PubMed: 7721708]
AuthorMessner, P., Christian, R., Neuninger, C. Schulz, G.
Research GroupCenter for Ultrastructure Research, University of Natural Resources and Applied Life Sciences, Vienna, Austria.
Corresponding Author Schulz, G.
ContactCenter for Ultrastructure Research, University of Natural Resources and Applied Life Sciences, Vienna, Austria.
ReferenceAltman, E., Brisson, J.R., Messner, P. and Sleytr, U.B. (1991) Structure of the glycan chain from the surface layer glycoprotein of Bacillus alvei CCM 2051. Biochem Cell Biol, 69, 72-78.
AuthorAltman, E., Brisson, J.R., Messner, P. Sleytr, U.B.
Research GroupDivision of Biological Sciences, National Research Council, Ottawa, Canada.
Corresponding Author Sleytr, U.B.
ContactDivision of Biological Sciences, National Research Council, Ottawa, Canada.