ProGP436 (Acm2)

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ProGP ID ProGP436 (Acm2)
Validation Status Characterized
Organism Information
Organism NameLactobacillus plantarum
Domain Bacteria
Classification Phylum : Firmicutes
Class : Bacilli
Orders : Lactobacillales
Family : Lactobacillaceae
Genus : Lactobacillus
Species : plantarum
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 IDProGT69 ProGT70
Literature
Year of Identification2013
Year of Identification Month Wise2013.8.2
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