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LOCUS NP_465285 225 aa linear CON 28-AUG-2016 monocytogenes EGD-e]. ACCESSION NP_465285 VERSION NP_465285.1 DBLINK BioProject: PRJNA61583 Assembly: GCF_000196035.1 DBSOURCE REFSEQ: accession NC_003210.1 KEYWORDS RefSeq. SOURCE Listeria monocytogenes EGD-e ORGANISM Listeria monocytogenes EGD-e Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria. REFERENCE 1 (residues 1 to 225) AUTHORS Toledo-Arana,A., Dussurget,O., Nikitas,G., Sesto,N., Guet-Revillet,H., Balestrino,D., Loh,E., Gripenland,J., Tiensuu,T., Vaitkevicius,K., Barthelemy,M., Vergassola,M., Nahori,M.A., Soubigou,G., Regnault,B., Coppee,J.Y., Lecuit,M., Johansson,J. and Cossart,P. TITLE The Listeria transcriptional landscape from saprophytism to virulence JOURNAL Nature 459 (7249), 950-956 (2009) PUBMED 19448609 REFERENCE 2 (residues 1 to 225) AUTHORS Chatterjee,S.S., Hossain,H., Otten,S., Kuenne,C., Kuchmina,K., Machata,S., Domann,E., Chakraborty,T. and Hain,T. TITLE Intracellular gene expression profile of Listeria monocytogenes JOURNAL Infect. Immun. 74 (2), 1323-1338 (2006) PUBMED 16428782 REFERENCE 3 (residues 1 to 225) AUTHORS Glaser,P., Frangeul,L., Buchrieser,C., Amend,A., Baquero,F., Berche,P., Bloecker,H., Brandt,P., Chakraborty,T., Charbit,A., Chetouani,F., Couve,E., de Daruvar,A., Dehoux,P., Domann,E., Dominguez-Bernal,G., Duchaud,E., Durand,L., Dussurget,O., Entian,K.-D., Fsihi,H., Garcia-Del Portillo,F., Garrido,P., Gautier,L., Goebel,W., Gomez-Lopez,N., Hain,T., Hauf,J., Jackson,D., Jones,L.-M., Karst,U., Kreft,J., Kuhn,M., Kunst,F., Kurapkat,G., Madueno,E., Maitournam,A., Mata Vicente,J., Ng,E., Nordsiek,G., Novella,S., de Pablos,B., Perez-Diaz,J.-C., Remmel,B., Rose,M., Rusniok,C., Schlueter,T., Simoes,N., Tierrez,A., Vazquez-Boland,J.-A., Voss,H., Wehland,J. and Cossart,P. TITLE Comparative genomics of Listeria species JOURNAL Science 294 (5543), 849-852 (2001) PUBMED 11679669 REFERENCE 4 (residues 1 to 225) CONSRTM NCBI Genome Project TITLE Direct Submission JOURNAL Submitted (08-NOV-2001) National Center for Biotechnology Information, NIH, Bethesda, MD 20894, USA REFERENCE 5 (residues 1 to 225) AUTHORS Glaser,P., Frangeul,L. and Rusniok,C. TITLE Direct Submission JOURNAL Submitted (06-JUN-2001) Glaser P., Institut Pasteur, Genomique des Microorganismes Pathogenes, 25 rue du Docteur Roux, 75724 Paris Cedex 15, FRANCE COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The reference sequence was derived from CAC99838. RefSeq Category: Reference Genome FGS: First Genome sequenced MOD: Model Organism UPR: UniProt Genome Method: conceptual translation. FEATURES Location/Qualifiers source 1..225 /organism="Listeria monocytogenes EGD-e" /strain="EGD-e" /db_xref="taxon:169963" Protein 1..225 /product="geranylgeranylglyceryl phosphate synthase-like protein" /calculated_mol_wt=25229 Region 2..217 /region_name="PcrB_like" /note="PcrB_like proteins. One member of this family, a protein from Archaeoglobus fulgidus, has been characterized as a (S)-3-O-geranylgeranylglyceryl phosphate synthase (AfGGGPS). AfGGGPS catalyzes the formation of an ether linkage between...; cd02812" /db_xref="CDD:239206" Site order(6,153,155,158,181..183,204) /site_type="other" /note="substrate binding site [chemical binding]" /db_xref="CDD:239206" Site order(8,34,153,155,157) /site_type="active" /note="putative active site [active]" /db_xref="CDD:239206" Site order(79,84,88,92,96,134,137..138,142,145,168) /site_type="other" /note="dimer interface [polypeptide binding]" /db_xref="CDD:239206" CDS 1..225 /locus_tag="lmo1760" /coded_by="complement(NC_003210.1:1832242..1832919)" /experiment="EXISTENCE:[PMID:19448609]" /note="PcrB-like protein; GGGP synthase; member of prenyltransferases that transfer isoprenoid groups to nonisoprenoid acceptors; functions in form GGGP from glycerol-1-phosphate (G-1-P) and geranylgeranyl pyrophosphate (GGPP); important in lipid metabolism and especially important as the ether linkages in archaea are different than those in bacteria; GGGP synthase lies at the branch point for membrane lipid biosynthesis; cytosolic; T acidophilum protein acts as a homodimer while M thermoautotrophicum protein has been reported to function as a pentamer" /transl_table=11 /db_xref="GeneID:985989" CONTIG join(WP_009930607.1:1..225) ORIGIN 1 mkhlfkldpa knlptndvtk lihsgtdgfi iggtdnvqie avqnlyellv etdlpiflei 61 snesmilpea dhflipvvln tenskwthgl hkelikemge fipwkrvtse gyvilnkdak 121 vahlteaktd ltdedivaya rlaenifhlp ifyveysgmy gdpevvrkas aalsntkfwy 181 gggirskeqa aemakyadti ivgniiyedl ekaletatif rkktv