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acyltransferase [Listeria monocytogenes EGD-e].


LOCUS       NP_464816                622 aa            linear   CON 28-AUG-2016
ACCESSION   NP_464816
VERSION     NP_464816.1
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 622)
  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 622)
  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 622)
  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 622)
  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 622)
  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 CAC99369.
            RefSeq Category: Reference Genome
                        FGS: First Genome sequenced
                        MOD: Model Organism
                        UPR: UniProt Genome
            Method: conceptual translation.
FEATURES             Location/Qualifiers
     source          1..622
                     /organism="Listeria monocytogenes EGD-e"
                     /strain="EGD-e"
                     /db_xref="taxon:169963"
     Protein         1..622
                     /product="acyltransferase"
                     /calculated_mol_wt=70194
     Region          8..358
                     /region_name="OafA"
                     /note="Peptidoglycan/LPS O-acetylase OafA/YrhL, contains
                     acyltransferase and SGNH-hydrolase domains [Cell
                     wall/membrane/envelope biogenesis]; COG1835"
                     /db_xref="CDD:441440"
     Region          473..620
                     /region_name="SGNH_hydrolase_yrhL_like"
                     /note="yrhL-like subfamily of SGNH-hydrolases, a diverse
                     family of lipases and esterases. The tertiary fold of the
                     enzyme is substantially different from that of the
                     alpha/beta hydrolase family and unique among all known
                     hydrolases; its active site closely...; cd01840"
                     /db_xref="CDD:238878"
     Site            order(480,504,533,600,603)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238878"
     Site            order(480,600,603)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:238878"
     Site            order(480,504,533)
                     /site_type="active"
                     /note="oxyanion hole [active]"
                     /db_xref="CDD:238878"
     CDS             1..622
                     /locus_tag="lmo1291"
                     /coded_by="complement(NC_003210.1:1317596..1319464)"
                     /experiment="EXISTENCE:[PMID:19448609]"
                     /transl_table=11
                     /db_xref="GeneID:985119"
CONTIG      join(WP_009932001.1:1..622)
ORIGIN      
        1 mkrttrysrk yvpsidglra laviaviayh lnfswakggf igvdiffvls gylitnillt
       61 qweknqslql kqfwirrfrr lipavyvmiv vvviysvffh peilknlrgd aiasffyvsn
      121 wwfifhnvsy fdsfglpspl knlwslaiee qfyliwpafl lvflkwvknp klllkivigl
      181 gllsavwmti lyvpgtdpsr vyygtdtraf dllsgcalaf vwpfnrlspv vprkskavln
      241 iagtisilcf ilftafvsey qpflyrggll fvailgvimi atishpasyl skifsfkplr
      301 wigtrsygiy lwhypiitlt tpvleitqpn iwrailqvaa tfiiaelsfr fietpirkng
      361 finyfkgfkd knyfiwknkp vgkwlsiagv vavlaiftlg msnvlsvntn aekqqtsvkt
      421 ttstpdekkd dkkedkatkd keadsnkase qketqkpdnk nksaatpkti itqtvaigds
      481 vmldiepylk eavpnitidg lvgrqlrdai ttatgykkfn senssvilel gtngpftedq
      541 lndlldqfdk atiylvntrv prgwqsdvnk sianaasrpn vtvvdwysrs sgqsqyfapd
      601 gvhltkagaq ayvamltsvm nk