ProGP350

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ProGP ID ProGP350
Validation Status Characterized
Organism Information
Organism NameProteus vulgaris
Domain Bacteria
Classification Family: Enterobacteriaceae
Order: "Enterobacteriales"
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 585
Genome Sequence(s)
GenBank GQ996964
EMBL GQ996964
Protein Information
Protein NameChondroitinase ABC
UniProtKB/SwissProt ID P59807
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 LocationSecreted
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 ProteinN282, N338, N345, N515, N675, N856, N963
Experimentally Validated Glycosite(s ) in Mature ProteinN282, 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
Technique(s) used for Glycosylation DetectionSlower 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.
Literature
Year of Identification2010
Year of Identification Month Wise2010.10.29
Year of Validation 2010
ReferenceMuir, 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]
AuthorMuir, E.M., Fyfe, I., Gardiner, S., Li, L., Warren, P., Fawcett, J.W., Keynes, R.J. and Rogers, J.H.
Research GroupDepartment of Physiology Development and Neuroscience, University of Cambridge, Downing St., Cambridge CB2 3EG, UK.
Corresponding Author Rogers, J.H.
ContactDepartment of Physiology Development and Neuroscience, University of Cambridge, Downing St., Cambridge CB2 3EG, UK.
Reference 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]
Author Huang, W., Lunin, V.V., Li, Y., Suzuki, S., Sugiura, N., Miyazono, H. Cygler, M.
Research GroupBiotechnology Research Institute, National Research Council of Canada, 6100 Royalmount Avenue, Montréal, Québec, Canada
Corresponding Author Cygler, M.
ContactBiotechnology Research Institute, National Research Council of Canada, 6100 Royalmount Avenue, Montréal, Québec, Canada