ProGP108

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ProGP ID ProGP108
Validation Status Characterized
Organism Information
Organism NameStaphylothermus marinus F1
Domain Archaea
Classification Family: Desulfurococcaceae
Order: Desulfurococcales
Class: Thermoprotei or Crenarchaeota
Division or phylum: "Crenarchaeota"
Taxonomic ID (NCBI) 2280
Genome Sequence(s)
EMBL U57967
Gene Information
Gene NameSmar_1008
Protein Information
Protein NameTetrabrachion (S layer glycoprotein)
UniProtKB/SwissProt ID Q54436
EMBL-CDSAAC44118.1
UniProtKB Sequence >tr|Q54436|Q54436_STAMA Tetrabrachion OS=Staphylothermus marinus PE=1 SV=1 MNRVLAYSLLAIMTLSLLIIPAPGIAQRITVGVSVKAGTYNFYNITPTTQTVEVTDNGML RVIINRTEATELGTTIRLAFILDTDKYDPNVGGYFLNVSNIGVYAPSDPTQSPYGGVIDI TQNSTLTDGTQVVGNVTVVNGGNNVIILIDLSKLPDLQNVVYITNVYTETSTTANLTNTL LRVKAFDAASWDAVISGNQFKILYIPSLCKYVKINVIHSPAIVGTNVDVIVSFHKYFSLV QSIAGVSLDITVDNKTQLNMTNYYNATENYVLATFINGNLTVGGSEVFSSPTVTVINAST FKYSGQVKDYAPTVADTATPWVRTLNKFEVEFRHEIVNXTHDLIFYIHCDSDTVSYDTWP FLIVNASLDITTTEVAFNSTTINPGDIVNFTAHNVPLQYLTATNYGVLRFQLINPALVVY VPVSNMTLSANTTTGIINGSFVLPDAPYGGLDYLTYLVFNDGKFIANGYITVSPCIETYV LTNTSAYAEDAGSSYIGRFVPGYTSVPGDYIVIKGYGFALSNLTGFTVSINNTDVIILNA TYNASTGKIIILAKLLDTNGTPIPVGAGFIRVGQNGTTNIAYAPFNVTRNSGLEKVLFNP RWFYNGTYYIEHDKLGDPYLYFPVDYPLVNNTFTTEMWPFNTTIEVIGWPTNTFTLKAFN KEFNLSFNLLTLSLTNGYNMTNLYNLTIPFLPYGNYTLLEGTLLSVNNRTVFTVHMGINV DLDSCGNGTLSITVVGAAPNTEYNFTFGYQVHDLNYGITRYISPQWNGTWNISLVTDIYG TGSTSVPLITLYPTSYVINATWDVITWLRLSGSGTLDLLFSVDVSYNGFTDNLTTPITYV FGPSDTTPGSFNIYVNTTYNVSVVRVAVDYLPRTNVVISVPETVLPGDTITVQIFPHHNE VWGFIEPTALFDENQLLGWYLTVRLVDPLSNTVVERVAGYYAGNLIVEDVDGDGDNEVWF VVNLTAPLVLGVDKTYRVDVELFLAVLNPSSNITGVTAVDNECYVQLDLNGTIYWNGLGS GIMLGGDGQIVTVLGVLEGKLDTIKDGIAEINATVNDINTYLKVNVTDLLKTINNSVVMI KNDTATLIIGQAEIKAKLDDLLNLTSQVNDTVTMILACCNNASKVLNRMEGTLNSTYTGV LNVKSDLSTLIDTANNVVIPKFNELYDNVTVEINASRDLIIQKISSVNDSLTTIISAGFN DVEAMISNLNTTLLNRIDELEGTLLFYMTANEQRLEGIINETADDIVYRLTVIIDDRYES LKNLITLRADRLEMIINDNVSTILASIGNVNLTVFNKLNDLEIELGDVNATINAGIFQIQ SNLGNANQLILDTLTSSKVEILNAISSNASAISSEIHNAVNQLSTLVLQVNDTLTLKITG EADNILNFLSSLEGSMNTGFNNVTSTLSAVENNILGKITDTSNLLSSKIDNTLSTLQDLI TSTSNDLKNSISSAKNDIVSSLSSKVDSSTQTLSTKLDDLKSAQESNTNSINNNIMLFGA ASLILLIVTIGLVGYRLIARRRVG
Sequence length 1524 AA
Subcellular LocationSurface (anchored in the membrane at one end)
Function Structural unit of S layer making it stable towards extremely harsh conditions. Encoded as a precursor with 26 AA signal peptide.
Protein Structure
PDB ID 1FE6, 1YBK
Glycosylation Status
Glycosylation Type N (Asn) linked (O Ser/Thr- linked residues not yet identified)
Experimentally Validated Glycosite(s) in Full Length Protein N44, N605, N641, N685, N708, N1279, N1402
Experimentally Validated Glycosite(s ) in Mature Protein N44, N605, N641, N685, N708, N1279, N1402
Glycosite(s) Annotated Protein Sequence >tr|Q54436|Q54436_STAMA Tetrabrachion OS=Staphylothermus marinus PE=1 SV=1 MNRVLAYSLLAIMTLSLLIIPAPGIAQRITVGVSVKAGTYNFYN*(44)ITPTTQTVEVTDNGML RVIINRTEATELGTTIRLAFILDTDKYDPNVGGYFLNVSNIGVYAPSDPTQSPYGGVIDI TQNSTLTDGTQVVGNVTVVNGGNNVIILIDLSKLPDLQNVVYITNVYTETSTTANLTNTL LRVKAFDAASWDAVISGNQFKILYIPSLCKYVKINVIHSPAIVGTNVDVIVSFHKYFSLV QSIAGVSLDITVDNKTQLNMTNYYNATENYVLATFINGNLTVGGSEVFSSPTVTVINAST FKYSGQVKDYAPTVADTATPWVRTLNKFEVEFRHEIVNXTHDLIFYIHCDSDTVSYDTWP FLIVNASLDITTTEVAFNSTTINPGDIVNFTAHNVPLQYLTATNYGVLRFQLINPALVVY VPVSNMTLSANTTTGIINGSFVLPDAPYGGLDYLTYLVFNDGKFIANGYITVSPCIETYV LTNTSAYAEDAGSSYIGRFVPGYTSVPGDYIVIKGYGFALSNLTGFTVSINNTDVIILNA TYNASTGKIIILAKLLDTNGTPIPVGAGFIRVGQNGTTNIAYAPFNVTRNSGLEKVLFNP RWFYN*(605)GTYYIEHDKLGDPYLYFPVDYPLVNNTFTTEMWPFN*(641)TTIEVIGWPTNTFTLKAFN KEFNLSFNLLTLSLTNGYNMTNLYN*(685)LTIPFLPYGNYTLLEGTLLSVNN*(708)RTVFTVHMGINV DLDSCGNGTLSITVVGAAPNTEYNFTFGYQVHDLNYGITRYISPQWNGTWNISLVTDIYG TGSTSVPLITLYPTSYVINATWDVITWLRLSGSGTLDLLFSVDVSYNGFTDNLTTPITYV FGPSDTTPGSFNIYVNTTYNVSVVRVAVDYLPRTNVVISVPETVLPGDTITVQIFPHHNE VWGFIEPTALFDENQLLGWYLTVRLVDPLSNTVVERVAGYYAGNLIVEDVDGDGDNEVWF VVNLTAPLVLGVDKTYRVDVELFLAVLNPSSNITGVTAVDNECYVQLDLNGTIYWNGLGS GIMLGGDGQIVTVLGVLEGKLDTIKDGIAEINATVNDINTYLKVNVTDLLKTINNSVVMI KNDTATLIIGQAEIKAKLDDLLNLTSQVNDTVTMILACCNNASKVLNRMEGTLNSTYTGV LNVKSDLSTLIDTANNVVIPKFNELYDNVTVEINASRDLIIQKISSVNDSLTTIISAGFN DVEAMISNLNTTLLNRIDELEGTLLFYMTANEQRLEGIINETADDIVYRLTVIIDDRYES LKNLITLRADRLEMIINDN*(1279)VSTILASIGNVNLTVFNKLNDLEIELGDVNATINAGIFQIQ SNLGNANQLILDTLTSSKVEILNAISSNASAISSEIHNAVNQLSTLVLQVNDTLTLKITG EADNILNFLSSLEGSMNTGFNN*(1402)VTSTLSAVENNILGKITDTSNLLSSKIDNTLSTLQDLI TSTSNDLKNSISSAKNDIVSSLSSKVDSSTQTLSTKLDDLKSAQESNTNSINNNIMLFGA ASLILLIVTIGLVGYRLIARRRVG
Sequence Around Glycosites (21 AA) SVKAGTYNFYNITPTTQTVEV
KVLFNPRWFYNGTYYIEHDKL
NTFTTEMWPFNTTIEVIGWPT
TNGYNMTNLYNLTIPFLPYGN
LLEGTLLSVNNRTVFTVHMGI
ADRLEMIINDNVSTILASIGN
LEGSMNTGFNNVTSTLSAVEN
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionCarbohydrate analysis using trifluoroacetic acid and GC/MS (gas chromatography/mass spectrometry).
Technique(s) used for Glycosylated Residue(s) Detection Edman degradation
Glycan Information
Glycan Annotation Carbohydrates present: glucose, mannose, and glucosamine. Both N and O linked glycans present.
β-elimination revealed that at least 15 carbohydrate chains are bound to Ser or Thr. Two molecules of 150 KDa proteases are associated with glycosylated tetrabrachion polypeptides (85 KDa & 92KDa) and for this tetrabrachion-protease complex overall carbohydrate content is 38%.
Literature
Year of Identification1995
Year of Identification Month Wise1995.01.01
Year of Validation 1996
Reference Stetefeld, J., Jenny, M., Schulthess, T., Landwehr, R., Engel, J. and Kammerer, R.A. (2000) Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer. Nat Struct Biol, 7, 772-776. [PubMed: 10966648]
Author Stetefeld, J., Jenny, M., Schulthess, T., Landwehr, R., Engel, J. and Kammerer, R.A.
Research GroupDepartment of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. joerg.stetefeld@unibas.ch
Corresponding Author Kammerer, R.A.
ContactDepartment of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. joerg.stetefeld@unibas.ch
Reference Stetefeld, J., Jenny, M., Schulthess, T., Landwehr, R., Engel, J. and Kammerer, R.A. (2000) Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer. Nat Struct Biol, 7, 772-776. [PubMed: 10966648]
Author Stetefeld, J., Jenny, M., Schulthess, T., L wehr, R., Engel, J.
Research GroupDepartment of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. joerg.stetefeld@unibas.ch
Corresponding Author wehr, R., Engel, J.
ContactDepartment of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. joerg.stetefeld@unibas.ch
Reference Peters, J., Nitsch, M., Kuhlmorgen, B., Golbik, R., Lupas, A., Kellermann, J., Engelhardt, H., Pfander, J.P., Muller, S., Goldie, K. et al. (1995) Tetrabrachion: a filamentous archaebacterial surface protein assembly of unusual structure and extreme stability. J Mol Biol, 245, 385-401. [PubMed: 7837271]
Author Peters, J., Nitsch, M., Kuhlmorgen, B., Golbik, R., Lupas, A., Kellermann, J., Engelhardt, H., Pfander, J.P., Muller, S., Goldie, K. et al.
Research GroupStructural Biochemistry Group, Michael Swann
Corresponding Author Ju¨rgen Peters
ContactStructural Biochemistry Group, Michael Swann
Reference1) Ozbek, S., Muller, J.F., Figgemeier, E. and Stetefeld, J. (2005) Favourable mediation of crystal contacts by cocoamidopropylbetaine (CAPB). Acta Crystallogr D Biol Crystallogr, 61, 477-480. [PubMed: 15805603]
AuthorOzbek, S., Muller, J.F., Figgemeier, E. and Stetefeld, J.
Research GroupDepartment of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrase 70, CH-4056 Basel, Switzerland.
Corresponding Author Stetefeld, J.
ContactDepartment of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrase 70, CH-4056 Basel, Switzerland.
Reference Peters, J., Baumeister, W. and Lupas, A. (1996) Hyperthermostable surface layer protein tetrabrachion from the archaebacterium Staphylothermus marinus: evidence for the presence of a right-handed coiled coil derived from the primary structure. J Mol Biol, 257, 1031-1041. [PubMed: 8632466]
Author Lupas, A.
Research GroupMax-Planck-Institut fur Biochemie, Martinsried Germany.
Corresponding Author Peters, J., Baumeister, W. Lupas, A.
ContactMax-Planck-Institut fur Biochemie, Martinsried Germany.