ProGP75 (S-layer glycoprotein)
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| ProGP ID | ProGP75 (S-layer glycoprotein) |
| Validation Status | Uncharacterized |
| Organism Information | |
| Organism Name | Paenibacillus (Bacillus) alvei CCM 2051T |
| Domain | Bacteria |
| Classification | Phylum : Firmicutes Class : Bacilli Orders : Bacillales Family : Paenibacillaceae Genus : Paenibacillus Species : alvei Strain : CCM 2051T |
| Taxonomic ID (NCBI) | 44250 |
| Genome Information | |
| GenBank | FJ751775 |
| EMBL | FJ751775 |
| Gene Information | |
| Gene Name | spaA |
| Protein Information | |
| Protein Name | S-layer glycoprotein |
| UniProtKB/SwissProt ID | C1JZ07 |
| EMBL-CDS | ACN92046.1 |
| 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 Location | Surface |
| Function | Structural component of the surface layer. |
| Glycosylation Status | |
| Glycosylation Type | O- (Tyr) linked |
| Technique(s) used for Glycosylation Detection | Carbohydrate 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 ID | 23154 |
| Literature | |
| Year of Identification | 1991 |
| Year of Identification Month Wise | 1991.02 |
| Reference | Messner, P., Steiner, K., Zarschler, K. and Schäffer, C., 2008. S-layer nanoglycobiology of bacteria. Carbohydrate Research, 343(12), pp.1934-1951. |
| Corresponding Author | Christina Schaffer Paul Messner |
| Contact | Center for NanoBiotechnology, University of Natural Resources and Applied Life Sciences Vienna, A-1190 Vienna, Austria. University of Natural Resources and Life Sciences Vienna, Center for NanoBiotechnology A-1180 Vienna, Gregor-Mendel-Strasse 33, Austria. |
| Reference | Messner, P., Christian, R., Neuninger, C. and Schulz, G., 1995. Similarity of" core" structures in two different glycans of tyrosine-linked eubacterial S-layer glycoproteins. Journal of Bacteriology, 177(8), pp.2188-2193. |
| Corresponding Author | Paul Messner |
| Contact | Center for NanoBiotechnology, University of Applied Life Sciences and Natural Resources, A-1180 Vienna, Austria. |
| Reference | Altman, 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. Biochemistry and Cell Biology, 69(1), pp.72-78. |
| Corresponding Author | Eleonora Altman |
| Contact | Division of Biological Sciences, National Research Council, Ottawa, Canada. |