ProGP436 (Acm2)

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ProGP ID ProGP436 (Acm2)
Validation Status Characterized
Organism Information
Organism NameLactobacillus plantarum
Domain Bacteria
Classification Family: Lactobacillaceae
Order: Lactobacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI) 220668
Genome Information
GenBank NC_004567.2.
EMBL AL935263
Gene Information
Gene Nameacm2
GenBank Gene Sequence NC_004567.2.
Protein Information
Protein NameAcm2
UniProtKB/SwissProt ID F9URD9
NCBI RefSeq WP_011101863.1.
EMBL-CDSCCC79778.1.
UniProtKB Sequence >tr|F9URD9|F9URD9_LACPL Cell wall hydrolase/muramidase OS=Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) GN=acm2 PE=4 SV=1 MKIGMTKKVVTSLLLSTALLPMLSGKADTASANQKPAAATKGNSAASAASQQVTLSAGSQ TETTAAGATDQSVASDGAKTDDQAESTSTTTATTSATSRVTVRAASQAAKADSTGPQSQS SASEAAKDNAATSATADSTTSAVDQLDKTAKASAATSQASHSTTNETAKASAAASQDSHV TTDQSSVTVTSEVAKSAASSAAPKQATEQAVAAKISPKIETAVAADAVQSSAMMARSTRA MTSQEIFLSQIKAGAISGWNKYQVLPSVTAAQAILESGWGQSQLATQGNNLFGIKGSYQG QSIYFPTQEWNGSQYITIQDAFRKYPNWSASVEDHGAFLVVNPRYSNLIGVTDYRRVASL LQQDGYATAPTYASSLISIIEYNKLHEWDQEALSGQASGGNDNNQVQPDQDVTPTSGTHK FTKTTTIHNAPDATSAVVGTYNAGETVNYNGKLTVGNATWLRYQSYSGVSRYVMISQTTT NDNNNQATVTPASGSYKFTAKTNIRSAASKTAQVVGTYNAGETVYYNGKITTGGTTWLRY LSYSGAQHYVAMSGDEVGSVAKPDVVATSGSYRFTKTTAIKSSPATSATTVGSYNAGDTV YYNGKVTTNGQTWLRYMSYSGAQHYVQISGESTSTNVDKPQVTPQSGSYRFTQTTAIKNT PAGNAPSVGTYSAGDTVYYNAKVTANGQTWLRYLSYSGAQHYVAISGNAATGNTTSKPVT NSQGAFRFVTTTNIRTAPSTRASVVGEYNPGETVYYNGTVQAEGYTWLRYLSRSGATHYV AKLEG
Sequence length 785 AA
Subcellular LocationExtracellular
Function Acm2 is the major autolysin of Lactobacillus plantarum.
Glycosylation Status
Glycosylation Type O- (Ser) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS86 and S95
Glycosite(s) Annotated Protein Sequence >tr|F9URD9|F9URD9_LACPL Cell wall hydrolase/muramidase OS=Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) GN=acm2 PE=4 SV=1 MKIGMTKKVVTSLLLSTALLPMLSGKADTASANQKPAAATKGNSAASAASQQVTLSAGSQ TETTAAGATDQSVASDGAKTDDQAES*(83)TSTTTATTSATS*(95)RVTVRAASQAAKADSTGPQSQS SASEAAKDNAATSATADSTTSAVDQLDKTAKASAATSQASHSTTNETAKASAAASQDSHV TTDQSSVTVTSEVAKSAASSAAPKQATEQAVAAKISPKIETAVAADAVQSSAMMARSTRA MTSQEIFLSQIKAGAISGWNKYQVLPSVTAAQAILESGWGQSQLATQGNNLFGIKGSYQG QSIYFPTQEWNGSQYITIQDAFRKYPNWSASVEDHGAFLVVNPRYSNLIGVTDYRRVASL LQQDGYATAPTYASSLISIIEYNKLHEWDQEALSGQASGGNDNNQVQPDQDVTPTSGTHK FTKTTTIHNAPDATSAVVGTYNAGETVNYNGKLTVGNATWLRYQSYSGVSRYVMISQTTT NDNNNQATVTPASGSYKFTAKTNIRSAASKTAQVVGTYNAGETVYYNGKITTGGTTWLRY LSYSGAQHYVAMSGDEVGSVAKPDVVATSGSYRFTKTTAIKSSPATSATTVGSYNAGDTV YYNGKVTTNGQTWLRYMSYSGAQHYVQISGESTSTNVDKPQVTPQSGSYRFTQTTAIKNT PAGNAPSVGTYSAGDTVYYNAKVTANGQTWLRYLSYSGAQHYVAISGNAATGNTTSKPVT NSQGAFRFVTTTNIRTAPSTRASVVGEYNPGETVYYNGTVQAEGYTWLRYLSRSGATHYV AKLEG
Sequence Around Glycosites (21 AA) DGAKTDDQAESTSTTTATTSA
ESTSTTTATTSATSRVTVRAA
ProGP Web Logo
Technique(s) used for Glycosylation DetectionMigration on SDS-PAGE , a lectin blot using GlcNAc-specific succinylated wheat germ agglutinin (sWGA), Glycoprotein enrichment with agarose bound WGA
Technique(s) used for Glycosylated Residue(s) Detection MALDI-TOF/TOF, LC-MS/MS analysis
Glycan Information
Glycan Annotation Monosaccharide (Double HexNAc, HexNAc)
Protein Glycosylation linked (PGL) gene(s)
OST ProGT ID
Literature
ReferenceRolain, T., Bernard, E., Beaussart, A., Degand, H., Courtin, P., Egge-Jacobsen, W., Bron, P.A., Morsomme, P., Kleerebezem, M., Chapot-Chartier, M.P. and Dufrêne, Y.F., 2013. O-glycosylation as a novel control mechanism of peptidoglycan hydrolase activity. Journal of Biological Chemistry, 288(31), pp.22233-22247.
Corresponding Author Pascal Hols
ContactInstitute of Life Sciences, Catholic University of Louvain, B-1348 Louvain-la-Neuve, Belgium
ReferenceFredriksen, L., Moen, A., Adzhubei, A.A., Mathiesen, G., Eijsink, V.G. and Egge-Jacobsen, W., 2013. Lactobacillus plantarum WCFS1 O-linked protein glycosylation: an extended spectrum of target proteins and modification sites detected by mass spectrometry. Glycobiology, 23(12), pp.1439-1451.
Corresponding Author Wolfgang Egge-Jacobsen
ContactNORBRAIN Mass Spectrometry Facility, Unit for Genome Dynamics, Department of Microbiology, Oslo University Hospital, Rikshospitalet, 0372 Oslo, Norway
ReferenceRolain T, Bernard E, Beaussart A, Degand H, Courtin P, Egge-Jacobsen W, Bron PA, Morsomme P, Kleerebezem M, Chapot-Chartier MP, Dufrêne YF, Hols P. (2013) O-glycosylation as a novel control mechanism of peptidoglycan hydrolase activity. J Biol Chem., 288(31):22233-47. [PubMed: 23760506]
AuthorRolain T, Bernard E, Beaussart A, Degand H, Courtin P, Egge-Jacobsen W, Bron PA, Morsomme P, Kleerebezem M, Chapot-Chartier MP, Dufrêne YF, Hols P
Research GroupInstitute of Life Sciences, Catholic University of Louvain, B-1348 Louvain-la-Neuve, Belgium
Corresponding Author Hols P
ContactInstitute of Life Sciences, Catholic University of Louvain, B-1348 Louvain-la-Neuve, Belgium
ReferenceFredriksen L, Moen A, Adzhubei AA, Mathiesen G, Eijsink VG, Egge-Jacobsen W. (2013) Lactobacillus plantarum WCFS1 O-linked protein glycosylation: an extended spectrum of target proteins and modification sites detected by mass spectrometry. Glycobiology, 23(12), 1439-51. [PubMed: 24000282]
AuthorFredriksen L, Moen A, Adzhubei AA, Mathiesen G, Eijsink VG, Egge-Jacobsen W
Research GroupDepartment of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, 1432 Aas, Norway.
Corresponding Author Egge-Jacobsen W
ContactDepartment of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, 1432 Aas, Norway.