ProGP197 (Subtilisin (SBL)-Cys mutant)
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| ProGP ID | ProGP197 (Subtilisin (SBL)-Cys mutant) |
| Validation Status | Characterized |
| Organism Information | |
| Organism Name | Bacillus lentus |
| Domain | Bacteria |
| Classification | Family: Bacillaceae Order: Bacillales Class: Bacilli (or Firmibacteria) Division or phylum: "Firmicutes" |
| Taxonomic ID (NCBI) | 1467 |
| Protein Information | |
| Protein Name | Subtilisin (SBL)- Cys mutant |
| UniProtKB/SwissProt ID | P29600 |
| UniProtKB Sequence | >sp|P29600|SUBS_BACLE Subtilisin Savinase OS=Bacillus lentus PE=1 SV=1 AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGN GHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGASGSGSVSSIAQGLEWAGNNGMHVA NLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGAGSISYPARYANAMAVGATDQNNNR ASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQI RNHLKNTATSLGSTNLYGSGLVNAEAATR |
| Sequence length | 269 AA |
| Subcellular Location | Secreted |
| Function | Subtilisin is an extracellular alkaline serine protease. EC = 3.4.21.62 |
| Protein Structure | |
| PDB ID | 1JEA |
| Glycosylation Status | |
| Glycosylation Type | S- (Cys) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | N62C, S156C, S166C and L217C (Residues that are shown glycosylated in vitro upon mutation from, N, S and L to C respectively) |
| Experimentally Validated Glycosite(s ) in Mature Protein | N62C, S156C, S166C and L217C (Residues that are shown glycosylated in vitro upon mutation from, N, S and L to C respectively) |
| Glycosite(s) Annotated Protein Sequence | >1JEA:A|PDBID|CHAIN|SEQUENCE
AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGNGHGTHVAGTIAALNNSIGVL
GVAPSAELYAVKVLGASGSGSVSSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGAGSIS
YPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQSTYPGSTYASLNGTSMATPHVAGAAALVKQKNPSWSNVQI
RNHLKNTATSLGSTNLYGSGLVNAEAATR This sequence was mutated at four residues to cysteines which were then glycosylated: >1JEA:A|PDBID|CHAIN|SEQUENCE AQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGC*(62)GHGTHVAGTIAALNNSIGVL GVAPSAELYAVKVLGASGSGSVSSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAASGNC*(156)GAGSIC*(166) YPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQSTYPGSTYASC*(217)NGTSMATPHVAGAAALVKQKNPSWSNVQI RNHLKNTATSLGSTNLYGSGLVNAEAATR |
| Sequence Around Glycosites (21 AA) | VPGEPSTQDGCGHGTHVAGTI
GVLVVAASGNCGAGSISYPAR ASGNSGAGSICYPARYANAMA STYPGSTYASCNGTSMATPHV |
| Technique(s) used for Glycosylation Detection | In vitro chemical glycosylation |
| Technique(s) used for Glycosylated Residue(s) Detection | Not applicable |
| Protein Glycosylation- Implication | In vitro engineered glycosylations of native subtilisin has been shown to affect structure as well as enzymatic activity. |
| Glycan Information | |
| Glycan Annotation | L217C-S-β-Glc(Ac)2, L217C-S-β-Glc(Ac)3, N62C-S-β-Glc(Ac)4, S156C-S-β-Glc(Ac)4, S16C-S-β-Glc(Ac)4. |
| Technique(s) used for Glycan Identification | Acetylated glycans were predetermined and synthesized in vitro |
| Literature | |
| Year of Identification | 2000 |
| Year of Identification Month Wise | 2000.09.10 |
| Year of Validation | 2000 |
| Reference | Davis, B.G., Lloyd, R.C. and Jones, J.B., 2000. Controlled site-selective protein glycosylation for precise glycan structure–catalytic activity relationships. Bioorganic & medicinal chemistry, 8(7), pp.1527-1535. |
| Corresponding Author | Benjamin G Davis |
| Contact | Department of Chemistry, University of Durham, UK. ben. |
| Reference | Lloyd, R.C., Davis, B.G. and Jones, J.B., 2000. Site-selective glycosylation of subtilisin Bacillus lentus causes dramatic increases in esterase activity. Bioorganic & medicinal chemistry, 8(7), pp.1537-1544. |
| Corresponding Author | J Bryan Jones Benjamin G Davis |
| Contact | Department of Chemistry, University of Toronto, 80 St. George Street, Toronto, ON, Canada M5S 3H6 |
| Reference | Graycar, T., Knapp, M., Ganshaw, G., Dauberman, J. and Bott, R., 1999. Engineered Bacillus lentus subtilisins having altered flexibility. Journal of molecular biology, 292(1), pp.97-109. |
| Corresponding Author | Richard Bott |
| Contact | Genencor International, 925 Page Mill Road, Palo Alto, CA 94304, USA. |
| Reference | Davis, B.G., Lloyd, R.C. and Jones, J.B. (2000) Controlled site-selective protein glycosylation for precise glycan structure-catalytic activity relationships. Bioorg Med Chem, 8, 1527-1535. [PubMed: 10976501]. |
| Author | Davis, B.G., Lloyd, R.C. and Jones, J.B. |
| Research Group | Department of Chemistry, University of Durham, UK |
| Corresponding Author | Jones, J.B |
| Contact | Department of Chemistry, University of Durham, UK |
| Reference | Lloyd, R.C. Davis, B.G. and Jones, J.B. (2000) Site-selective glycosylation of subtilisin Bacillus lentus causes dramatic increases in esterase activity. Bioorg Med Chem, 8, 1537-44. [PubMed: 10976502] |
| Author | Lloyd, R.C. Davis, B.G. and Jones, J.B |
| Research Group | Department of Chemistry, University of Toronto, ON, Canada. |
| Corresponding Author | Jones, J.B. |
| Contact | Department of Chemistry, University of Toronto, ON, Canada. |
| Reference | Lloyd, R.C. Davis, B.G. and Jones, J.B. (2000) Site-selective glycosylation of subtilisin Bacillus lentus causes dramatic increases in esterase activity. Bioorg Med Chem, 8, 1537-44. [PubMed: 10976502] |
| Author | Lloyd, R.C. Davis, B.G. Jones, J.B. |
| Research Group | Department of Chemistry, University of Toronto, ON, Canada. |
| Corresponding Author | Jones, J.B. |
| Contact | Department of Chemistry, University of Toronto, ON, Canada. |
| Reference | Graycar, T., Knapp, M., Ganshaw, G., Dauberman, J. and Bott, R. (1999) Engineered Bacillus lentus subtilisins having altered flexibility. J Mol Biol, 292, 97-109. [PubMed: 10493860] |
| Author | Graycar, T., Knapp, M., Ganshaw, G., Dauberman, J. Bott, R. |
| Research Group | Genencor International, 925 Page Mill Road, Palo Alto, CA 94304, USA. |
| Corresponding Author | Bott, R. |
| Contact | Genencor International, 925 Page Mill Road, Palo Alto, CA 94304, USA. |