| ProGlyProt ID | BC165 |
| Organism Information |
| Organism Name | Proteus vulgaris |
| Domain | Bacteria |
| Classification | Family: Enterobacteriaceae
Order: "Enterobacteriales"
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria" |
| Taxonomic ID (NCBI) | 585 |
| Genome Sequence (s) |
| EMBL | |
| Gene Information |
| Gene Name | |
| NCBI Gene ID | |
| Protein Information |
| Protein Name | Chondroitinase ABC |
| UniProtKB/SwissProt ID | P59807 |
| NCBI RefSeq | |
| EMBL-CDS | |
| UniProtKB Sequence | >sp|P59807|CABC_PROVU Chondroitin ABC endolyase 1 OS=Proteus vulgaris PE=1 SV=1
MPIFRFTALAMTLGLLSAPYNAMAATSNPAFDPKNLMQSEIYHFAQNNPLADFSSDKNSI
LTLSDKRSIMGNQSLLWKWKGGSSFTLHKKLIVPTDKEASKAWGRSSTPVFSFWLYNEKP
IDGYLTIDFGEKLISTSEAQAGFKVKLDFTGWRAVGVSLNNDLENREMTLNATNTSSDGT
QDSIGRSLGAKVDSIRFKAPSNVSQGEIYIDRIMFSVDDARYQWSDYQVKTRLSEPEIQF
HNVKPQLPVTPENLAAIDLIRQRLINEFVGGEKETNLALEENISKLKSDFDALNIHTLAN
GGTQGRHLITDKQIIIYQPENLNSQDKQLFDNYVILGNYTTLMFNISRAYVLEKDPTQKA
QLKQMYLLMTKHLLDQGFVKGSALVTTHHWGYSSRWWYISTLLMSDALKEANLQTQVYDS
LLWYSREFKSSFDMKVSADSSDLDYFNTLSRQHLALLLLEPDDQKRINLVNTFSHYITGA
LTQVPPGGKDGLRPDGTAWRHEGNYPGYSFPAFKNASQLIYLLRDTPFSVGESGWNNLKK
AMVSAWIYSNPEVGLPLAGRHPFNSPSLKSVAQGYYWLAMSAKSSPDKTLASIYLAISDK
TQNESTAIFGETITPASLPQGFYAFNGGAFGIHRWQDKMVTLKAYNTNVWSSEIYNKDNR
YGRYQSHGVAQIVSNGSQLSQGYQQEGWDWNRMEGATTIHLPLKDLDSPKPHTLMQRGER
GFSGTSSLEGQYGMMAFNLIYPANLERFDPNFTAKKSVLAADNHLIFIGSNINSSDKNKN
VETTLFQHAITPTLNTLWINGQKIENMPYQTTLQQGDWLIDSNGNGYLITQAEKVNVSRQ
HQVSAENKNRQPTEGNFSSAWIDHSTRPKDASYEYMVFLDATPEKMGEMAQKFRENNGLY
QVLRKDKDVHIILDKLSNVTGYAFYQPASIEDKWIKKVNKPAIVMTHRQKDTLIVSAVTP
DLNMTRQKAATPVTINVTINGKWQSADKNSEVKYQVSGDNTELTFTSYFGIPQEIKLSPL
P |
| Sequence length | 1021 AA |
| Subcellular Location | Secreted |
| Function | Chondroitin ABC endolyase 1 is a bacterial enzyme that degrades long sulphated glycosaminoglycan (GAG) chains of chondroitin sulphate proteoglycans (CSPGs). CSPGs are responsible for axon growth inhibition. EC: 4.2.2.20. |
| Protein Structure |
| PDB ID | 1HN0 |
| Glycosylation Status |
| Glycosylation Type | N (Asn) linked |
| Experimentally Validated Glycosite(s) in Full Length Protein | N282, N338, N345, N515, N675, N856, N963 |
| Experimentally Validated Glycosite(s ) in Mature Protein | N282, N338, N345, N515, N675, N856, N963 |
| Glycosite(s) Annotated Protein Sequence | >sp|P59807|CABC_PROVU Chondroitin ABC endolyase 1 OS=Proteus vulgaris PE=1 SV=1
MPIFRFTALAMTLGLLSAPYNAMAATSNPAFDPKNLMQSEIYHFAQNNPLADFSSDKNSI
LTLSDKRSIMGNQSLLWKWKGGSSFTLHKKLIVPTDKEASKAWGRSSTPVFSFWLYNEKP
IDGYLTIDFGEKLISTSEAQAGFKVKLDFTGWRAVGVSLNNDLENREMTLNATNTSSDGT
QDSIGRSLGAKVDSIRFKAPSNVSQGEIYIDRIMFSVDDARYQWSDYQVKTRLSEPEIQF
HNVKPQLPVTPENLAAIDLIRQRLINEFVGGEKETNLALEEN*(282)ISKLKSDFDALNIHTLAN
GGTQGRHLITDKQIIIYQPENLNSQDKQLFDNYVILGN*(338)YTTLMFN*(345)ISRAYVLEKDPTQKA
QLKQMYLLMTKHLLDQGFVKGSALVTTHHWGYSSRWWYISTLLMSDALKEANLQTQVYDS
LLWYSREFKSSFDMKVSADSSDLDYFNTLSRQHLALLLLEPDDQKRINLVNTFSHYITGA
LTQVPPGGKDGLRPDGTAWRHEGNYPGYSFPAFKN*(515)ASQLIYLLRDTPFSVGESGWNNLKK
AMVSAWIYSNPEVGLPLAGRHPFNSPSLKSVAQGYYWLAMSAKSSPDKTLASIYLAISDK
TQNESTAIFGETITPASLPQGFYAFNGGAFGIHRWQDKMVTLKAYNTNVWSSEIYNKDNR
YGRYQSHGVAQIVSN*(675)GSQLSQGYQQEGWDWNRMEGATTIHLPLKDLDSPKPHTLMQRGER
GFSGTSSLEGQYGMMAFNLIYPANLERFDPNFTAKKSVLAADNHLIFIGSNINSSDKNKN
VETTLFQHAITPTLNTLWINGQKIENMPYQTTLQQGDWLIDSNGNGYLITQAEKVNVSRQ
HQVSAENKNRQPTEGN*(856)FSSAWIDHSTRPKDASYEYMVFLDATPEKMGEMAQKFRENNGLY
QVLRKDKDVHIILDKLSNVTGYAFYQPASIEDKWIKKVNKPAIVMTHRQKDTLIVSAVTP
DLN*(963)MTRQKAATPVTINVTINGKWQSADKNSEVKYQVSGDNTELTFTSYFGIPQEIKLSPL
P
|
| Sequence Around Glycosites (21 AA) | EKETNLALEENISKLKSDFDA
QLFDNYVILGNYTTLMFNISR
ILGNYTTLMFNISRAYVLEKD
YPGYSFPAFKNASQLIYLLRD
QSHGVAQIVSNGSQLSQGYQQ
ENKNRQPTEGNFSSAWIDHST
LIVSAVTPDLNMTRQKAATPV
|
| Glycosite Sequence Logo | seqlogo |
| Glycosite Sequence Logo |  |
| Technique(s) used for Glycosylation Detection | Slower migration on SDS-PAGE than its predicted mass and N-glycosidase treatment |
| Technique(s) used for Glycosylated Residue(s) Detection | Multi-site-directed mutagenesis (mostly Asn→Gln) |
| Protein Glycosylation- Implication | Carbohydrate chains either distort the protein structure or produce steric hindrance of the active site resulting in an inactive form of the secreted protein. Secretion of underglycosylated protein was better when expressed in mammalian cells compared to fully glycosylated protein. |
| Glycan Information |
| Glycan Annotation | |
| Technique(s) used for Glycan Identification | |
| Protein Glycosylation linked (PGL) gene(s) |
| OST Gene Name | |
| OST NCBI Gene ID | |
| OST GenBank Gene Sequence | |
| OST Protein Name | |
| OST UniProtKB/ SwissProt ID | |
| OST NCBI RefSeq | |
| OST EMBL-CDS | |
| OST UniProtKB Sequence | |
| OST EC Number (BRENDA) | |
| OST Genome Context | |
| Characterized Accessory Gene(s) | |
| PGL Additional Links | CAZy |
| Literatures |
| Reference(s) | 1) Muir, E.M., Fyfe, I., Gardiner, S., Li, L., Warren, P., Fawcett, J.W., Keynes, R.J. and Rogers, J.H. (2010) Modification of N-glycosylation sites allows secretion of bacterial chondroitinase ABC from mammalian cells. J Biotechnol, 145, 103-110. [PubMed: 19900493]
2) Huang, W., Lunin, V.V., Li, Y., Suzuki, S., Sugiura, N., Miyazono, H. and Cygler, M. (2003) Crystal structure of Proteus vulgaris chondroitin sulfate ABC lyase I at 1.9A resolution. J Mol Biol, 328, 623-634. [PubMed: 12706721 |
| Additional Comments | Engineered glycoprotein
Sequon features: eukaryotic consensus sequence NXS/T gets glycosylated.
Chondroitinase ABC of Proteus vulgaris is an example of a protein of bacterial origin that is expressed as glycoprotein in mammalian cells. The glycosylated residues were mutated to abolish glycosylation that interferes with protein folding and secretion. |
| Year of Identification | 2010 |
| Year of Validation | 2010 |
