ProGP344 (SlaA (S-layer protein))

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ProGP ID ProGP344 (SlaA (S-layer protein))
Validation Status Characterized
Organism Information
Organism NameSulfolobus acidocaldarius (DSM 639)
Domain Archaea
Classification Phylum : Crenarchaeota
Class : Thermoprotei
Orders : sulfolobales
Family : Sulfolobaceae
Genus : Sulfolobus
Species : acidocaldarius
Strain : DSM 639
Taxonomic ID (NCBI) 2285
Genome Information
GenBank CP000077.1
EMBL CP000077
Gene Information
Gene NameslaA (Saci_2355) or slp1
NCBI Gene ID 3472789
GenBank Gene Sequence NC_007181
Protein Information
Protein NameSlaA (S-layer protein)
UniProtKB/SwissProt ID Q4J6E5
NCBI RefSeq WP_011279138.1
EMBL-CDSAAY81636.1
UniProtKB Sequence >tr|Q4J6E5|Q4J6E5_SULAC Conserved protein OS=Sulfolobus acidocaldarius GN=Saci_2355 PE=4 SV=1 MNKLVGLLVSSLFLASILIGIAPAITTTALTPPVSAGGIQAYLLTGSGAPASGLVLFVVN VSNIQVSSSNVTNVISTVVSNIQINAKTENAQTGATTGSVTVRFPTSGYNAYYDSVDKVV FVVVSFLYPYTTTSVNIPLSYLSKYLPGLLTAQPYDETGAQVTSVSSTPFGSLIDTSTGQ QILGTNPVLTSYNSYTTQANTNMQEGVVSGTLTSFTLGGQSFSGSTVPVILYAPFIFSNS PYQAGLYNPMQVNGNLGSLSSEAYYHPVIWGRALINTTLIDTYASGSVPFTFQLNYSVPG PLTINMAQLAWIASINNLPTSFTYLSYKFSNGYESFLGIISNSTQLTAGALTINPSGNFT INGKKFYVYLLVVGSTNSTTPVEYVTKLVVEYPSSTNFLPQGVTVTTSSNKYTLPVYEIG GPAGTTITLTGNWYSTPYTVQITVGSTPTLTNYVSQILLKAVAYEGINVSTTQSPYYSTA ILSTPPSEISITGSSTITAQGKLTATSASATVNLLTNATLTYENIPLTQYSFNGIIVTPG YAAINGTTAMAYVIGALYNKTSDYVLSFAGSQEPMQVMNNNLTEVTTLAPFGLTLLAPSV PATETGTSPLQLEFFTVPSTSYIALVDFGLWGNLTSVTVSAYDTVNNKLSVNLGYFYGIV IPPSISTAPYNYQNFICPNNYVTVTIYDPDAVLDPYPSGSFTTSSLPLKYGNMNITGAVI FPGSSVYNPSGVFGYSNFNKGAAVTTFTYTAQSGPFSPVALTGNTNYLSQYADNNPTDNY YFIQTVNGMPVLMGGLSIVASPVSASLPSSTSSPGFMYLLPSAAQVPSPLPGMATPNYNL NIYITYKIDGATVGNNMINGLYVASQNTLIYVVPNGSFVGSNIKLTYTTTDYAVLHYFYS TGQYKVFKTVSVPNVTANLYFPSSTTPLYQLSVPLYLSEPYYGSPLPTYIGLGTNGTSLW NSPNYVLFGVSAVQQYLGFIKSISVTLSNGTTVVIPLTTSNMQTLFPQLVGQELQACNGT FQFGISITGLEKLLNLNVQQLNNSILSVTYHDYVTGETLTATTKLVALSTLSLVAKGAGV VEFLLTAYPYTGNITFAPPWFIAENVVKQPFMTYSDLQFAKTNPSAILSLSTVNITVVGL GGKASVYYNSTSGQTVITNIYGQTVATLSGNVLPTLTELAAGNGTFTGSLQFTIVPNNTV VQIPSSLTKTSFAVYTNGSLAIVLNGKAYSLGPAGLFLLPFVTYTGSAIGANATAIITVS DGVGTSTTQVPITAENFTPIRLAPFQVPAQVPLPNAPKLKYEYNGSIVITPQQQVLKIYV TSILPYPQEFQIQAFVYEASQFNVHTGSPTAAPVYFSYSAVRAYPALGIGTSVPNLLVYV QLQGISNLPAGKYVIVLSAVPFAGGPVLSEYPAQLIFTNVTLTQ
Sequence length 1424 AA
Subcellular LocationSurface
Function The S-layer has to maintain the cell integrity and stabilize as well as to protect the cell against mechanical and osmotic stresses or extreme pH conditions. It is also predicted that the S-layer has to maintain or even determine the cell shape. It is also responsible for cell-cell interaction.
Glycosylation Status
Glycosylation Type N- (Asn) linked
Experimentally Validated Glycosite(s) in Full Length Protein(Signal peptide : 1-29) N1042, N1093, N1134, N1197, N1217, N1252, N1276, N1304, N1419
Experimentally Validated Glycosite(s ) in Mature ProteinN1013, N1064, N1105, N1168, N1188, N1223, N1247, N1275, N1390
Glycosite(s) Annotated Protein Sequence >tr|Q4J6E5|Q4J6E5_SULAC Conserved protein OS=Sulfolobus acidocaldarius GN=Saci_2355 PE=4 SV=1 MNKLVGLLVSSLFLASILIGIAPAITTTALTPPVSAGGIQAYLLTGSGAPASGLVLFVVN VSNIQVSSSNVTNVISTVVSNIQINAKTENAQTGATTGSVTVRFPTSGYNAYYDSVDKVV FVVVSFLYPYTTTSVNIPLSYLSKYLPGLLTAQPYDETGAQVTSVSSTPFGSLIDTSTGQ QILGTNPVLTSYNSYTTQANTNMQEGVVSGTLTSFTLGGQSFSGSTVPVILYAPFIFSNS PYQAGLYNPMQVNGNLGSLSSEAYYHPVIWGRALINTTLIDTYASGSVPFTFQLNYSVPG PLTINMAQLAWIASINNLPTSFTYLSYKFSNGYESFLGIISNSTQLTAGALTINPSGNFT INGKKFYVYLLVVGSTNSTTPVEYVTKLVVEYPSSTNFLPQGVTVTTSSNKYTLPVYEIG GPAGTTITLTGNWYSTPYTVQITVGSTPTLTNYVSQILLKAVAYEGINVSTTQSPYYSTA ILSTPPSEISITGSSTITAQGKLTATSASATVNLLTNATLTYENIPLTQYSFNGIIVTPG YAAINGTTAMAYVIGALYNKTSDYVLSFAGSQEPMQVMNNNLTEVTTLAPFGLTLLAPSV PATETGTSPLQLEFFTVPSTSYIALVDFGLWGNLTSVTVSAYDTVNNKLSVNLGYFYGIV IPPSISTAPYNYQNFICPNNYVTVTIYDPDAVLDPYPSGSFTTSSLPLKYGNMNITGAVI FPGSSVYNPSGVFGYSNFNKGAAVTTFTYTAQSGPFSPVALTGNTNYLSQYADNNPTDNY YFIQTVNGMPVLMGGLSIVASPVSASLPSSTSSPGFMYLLPSAAQVPSPLPGMATPNYNL NIYITYKIDGATVGNNMINGLYVASQNTLIYVVPNGSFVGSNIKLTYTTTDYAVLHYFYS TGQYKVFKTVSVPNVTANLYFPSSTTPLYQLSVPLYLSEPYYGSPLPTYIGLGTNGTSLW NSPNYVLFGVSAVQQYLGFIKSISVTLSNGTTVVIPLTTSNMQTLFPQLVGQELQACNGT FQFGISITGLEKLLNLNVQQLN*(1042)NSILSVTYHDYVTGETLTATTKLVALSTLSLVAKGAGV VEFLLTAYPYTGN*(1093)ITFAPPWFIAENVVKQPFMTYSDLQFAKTNPSAILSLSTVN*(1134)ITVVGL GGKASVYYNSTSGQTVITNIYGQTVATLSGNVLPTLTELAAGNGTFTGSLQFTIVPN*(1197)NTV VQIPSSLTKTSFAVYTN*(1217)GSLAIVLNGKAYSLGPAGLFLLPFVTYTGSAIGAN*(1252)ATAIITVS DGVGTSTTQVPITAEN*(1276)FTPIRLAPFQVPAQVPLPNAPKLKYEYN*(1304)GSIVITPQQQVLKIYV TSILPYPQEFQIQAFVYEASQFNVHTGSPTAAPVYFSYSAVRAYPALGIGTSVPNLLVYV QLQGISNLPAGKYVIVLSAVPFAGGPVLSEYPAQLIFTN*(1419)VTLTQ
Sequence Around Glycosites (21 AA) KLLNLNVQQLNNSILSVTYHD
FLLTAYPYTGNITFAPPWFIA
PSAILSLSTVNITVVGLGGKA
TGSLQFTIVPNNTVVQIPSSL
LTKTSFAVYTNGSLAIVLNGK
VTYTGSAIGANATAIITVSDG
STTQVPITAENFTPIRLAPFQ
PNAPKLKYEYNGSIVITPQQQ
SEYPAQLIFTNVTLTQ
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Technique(s) used for Glycosylation DetectionGlycan identification by nano-LC-MS/MS
Technique(s) used for Glycosylated Residue(s) Detection In-gel tryptic digestion and nano-LC-ES-MS/MS (nano-liquid chromatography-electrospray tandem mass spectrometry)
Protein Glycosylation- Implication Glycosylation of S layer protein might contribute towards increased stability and half life of S layer structural proteins in extreme thermoacidic enviornments.
Glycan Information
Glycan Annotation Linkage:β-GlcNAc-Asn.
N-linked hexasaccharide units - two residues each of Man and GlcNAc (one trisubstituted) and one residue each of Glc and 6-deoxy-6-sulfoglucose (6-sulfoquinovose, QuiS - a rare acidic sugar).β-D-Glcp-(1→4)-β-D-Quip(6--SO3-)-(1→3)-[α-D-Manp(1→4), α-D-Manp(1→6)]β-D-GlcpNAc-(1→4)-β-D-GlcpNAc-(1→Asn....
Microheterogeneity is observed as a family of glycans modify each of the glycosylation sites. The glycans are linked via a chitobiose core.
BCSDB ID 5950
GlyTouCan G92308TW
Technique(s) used for Glycan Identification GC-MS of trimethylsilyl (TMS) methyl glycoside derivatives and nano-LC-ESMS analysis
Protein Glycosylation linked (PGL) gene(s)
OST Gene NameConserved membrane protein
OST ProGT IDProGT51
Additional CommentSimilar to eukaryotes and unlike other archaea, the tribranched glycan is linked via chitobiose core (GlcNAcβ1-4GlcNAc) to the Asn in S. acidocaldarius glycoproteins. Hence sulfolobus has been suggested as closest eukaryotic model for N glycosylation studies among archaeal speceis.
The glycosylation density at C terminus of the protein averages around 1 site per 30-40 residues.
Similarity found in glycan sequence in SlaA and cytochrome b558/566 subunit A strengthen the existing understanding of conservation of N glycosylation in a given species in archaea.
The glycosylation was detected in other strains by thymol-sulfuric acid staining and DIG-glycan detection by 1996 (Ref. no. 3).
Literature
Year of Identification2010
Year of Identification Month Wise2010.07
Year of Validation 2010
ReferencePeyfoon, E., Meyer, B., Hitchen, P.G., Panico, M., Morris, H.R., Haslam, S.M., Albers, S.V. and Dell, A., 2010. The S-layer glycoprotein of the crenarchaeote Sulfolobus acidocaldarius is glycosylated at multiple sites with chitobiose-linked N-glycans. Archaea, 2010.
Corresponding Author Anne Dell
ContactDivision of Molecular Biosciences, Faculty of Natural Sciences, Imperial College London, London SW7 2AZ, UK
ReferenceVeith, A., Klingl, A., Zolghadr, B., Lauber, K., Mentele, R., Lottspeich, F., Rachel, R., Albers, S.V. and Kletzin, A., 2009. Acidianus, Sulfolobus and Metallosphaera surface layers: structure, composition and gene expression. Molecular microbiology, 73(1), pp.58-72.
Corresponding Author Arnulf Kletzin
ContactInstitute of Microbiology and Genetics, Technische Universität Darmstadt, Schnittspahnstrasse 10, 64287 Darmstadt, Germany.
ReferenceGrogan, D.W., 1996. Organization and interactions of cell envelope proteins of the extreme thermoacidophile Sulfolobus acidocaldarius. Canadian journal of microbiology, 42(11), pp.1163-1171.
Corresponding Author DENNIS W.GROGAN
ContactMax Planck Institute for Biochemistry, Martinsried Germany
ReferenceGrogan, D.W., 1989. Phenotypic characterization of the archaebacterial genus Sulfolobus: comparison of five wild-type strains. Journal of Bacteriology, 171(12), pp.6710-6719.
Corresponding Author DENNIS W.GROGAN
ContactMax Planck Institute for Biochemistry, Martinsried Germany
Referencevan Wolferen, M., Shajahan, A., Heinrich, K., Brenzinger, S., Black, I.M., Wagner, A., Briegel, A., Azadi, P. and Albers, S.V., 2020. Species-specific recognition of Sulfolobales mediated by UV-inducible pili and S-layer glycosylation patterns. MBio, 11(2), pp.e03014-19.
Corresponding Author Sonja-Verena Albers
ContactAlexander Wagner, Biozentrum, University of Basel, Basel, Switzerland