Latest update: September 24, 2018


ProGT108 (PAV_2c01640)

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ProGT ID ProGT108 (PAV_2c01640)
Organism Information
Organism NamePaenibacillus alvei CCM 2051T
DomainBacteria
PhylumFirmicutes
ClassificationFamily: Paenibacillaceae
Order: Bacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI)1206781
Genome Information
Gene BankAMBZ01000002
EMBLAMBZ01000002
Gene Information
Gene NamePAV_2c01640
Protein information
UniProtKB/ SwissProt IDK4ZPW8
UniProtKB Sequence>tr|K4ZPW8|K4ZPW8_PAEAL Glycosyl transferase family 2 OS=Paenibacillus alvei DSM 29 OX=1206781 GN=PAV_2c01640 PE=4 SV=1 MKSLISACMIVKDEESFIKESIASVLPYVEEVVVVDTGSKDDTVSIASYMGAKTIEMPWQ GDFSKARNAAIQHSNLPIVLMIDADERLDHRTVQALHDTARFLNENKSKAARIRIRNYTD DANTSISYATRMFPNNGKFKYMGRIHEQLCKEGNVPESIDTDIEFNHFGYMQEVIDQKQK ITRNIELLRKEASENEDNSYITYQLGKTHAIQKEYAEAEIYLRQAYQSASQDFHYCLPNI IYSLCHVLLQVKKYNDFSSIIDEAITLYPDYTDLYFMKGRAIVDNLDVTQFHLVPQLFER CVELGEVSNTQYESHVGVGTFKALYNLGIYYEMAGQKQQALDCYERCSEFGFKPAMERLL LLR
EMBL CDSEJW18400.1
Sequence length363 AA
Function in Native Organism 1) Essential for flagella production and bacterial motility.
Additional Information1) Deletion studies of PAV_2c01630 and PAV_2c01640 shows that flagellin glycosylation in P. alvei is essential for the flagella formation and bacterial motility.
2) Purified Hag protein (PAV_2c01710) is modified with an O-linked trisaccharide composed of one hexose and two N-acetyl-hexosamine residues, at three sites of glycosylation.
Glycosyltransferase Information
Glycosylation TypeO- (Ser/Thr) linked 
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferSequential
Glycan Information
Method of Glycan IndentificationMALDI-TOF-MS peptide mass fingerprinting, and LC-ESI-IT-MS/MS
Experimental_strategiesIn vivo 
Acceptor Subtrate Information
Acceptor Substrate name Hag
ProGPdb ID ProGP520
Litrature
Year Of Validation2016 
Reference Janesch, B., Schirmeister, F., Maresch, D., Altmann, F., Messner, P., Kolarich, D., & Schäffer, C. (2015). Flagellin glycosylation in Paenibacillus alvei CCM 2051T. Glycobiology, 26(1), 74-87.

Authors Janesch, B., Schirmeister, F., Maresch, D., Altmann, F., Messner, P., Kolarich, D., & Schäffer, C.
Research groups1 Department of NanoBiotechnology, NanoGlycobiology Unit, University of Natural Resources and Applied Life Sciences, Vienna, Muthgasse 11, Vienna A-1190, Austria. 2 Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany Institute of Chemistry and Biochemistry, Freie University Berlin, Arnimallee 22, Berlin 14195, Germany. 3 Department of Chemistry, Division of Biochemistry, Universität für Bodenkultur Wien, Muthgasse 18, Vienna A-1190, Austria.
Corresponding Author Schäffer, C.
ContactsDepartment of NanoBiotechnology, NanoGlycobiology Unit, University of Natural Resources and Applied Life Sciences, Vienna, Muthgasse 11, Vienna A-1190, Austria