GenomeNet

Database: RefSeq
Entry: WP_015749659
LinkDB: WP_015749659
Original site: WP_015749659 
LOCUS       WP_015749659             559 aa            linear   BCT 29-DEC-2023
DEFINITION  phospholipid carrier-dependent glycosyltransferase [Nakamurella
            multipartita].
ACCESSION   WP_015749659
VERSION     WP_015749659.1
KEYWORDS    RefSeq.
SOURCE      Nakamurella multipartita
  ORGANISM  Nakamurella multipartita
            Bacteria; Actinomycetota; Actinomycetes; Nakamurellales;
            Nakamurellaceae; Nakamurella.
REFERENCE   1  (residues 1 to 559)
  AUTHORS   Tavares-Carreon,F., Fathy Mohamed,Y., Andrade,A. and Valvano,M.A.
  TITLE     ArnT proteins that catalyze the glycosylation of lipopolysaccharide
            share common features with bacterial N-oligosaccharyltransferases
  JOURNAL   Glycobiology 26 (3), 286-300 (2016)
   PUBMED   26515403
REFERENCE   2  (residues 1 to 559)
  AUTHORS   Petrou,V.I., Herrera,C.M., Schultz,K.M., Clarke,O.B., Vendome,J.,
            Tomasek,D., Banerjee,S., Rajashankar,K.R., Belcher Dufrisne,M.,
            Kloss,B., Kloppmann,E., Rost,B., Klug,C.S., Trent,M.S., Shapiro,L.
            and Mancia,F.
  TITLE     Structures of aminoarabinose transferase ArnT suggest a molecular
            basis for lipid A glycosylation
  JOURNAL   Science 351 (6273), 608-612 (2016)
   PUBMED   26912703
REFERENCE   3  (residues 1 to 559)
  AUTHORS   Gentzsch,M. and Tanner,W.
  TITLE     The PMT gene family: protein O-glycosylation in Saccharomyces
            cerevisiae is vital
  JOURNAL   EMBO J 15 (21), 5752-5759 (1996)
   PUBMED   8918452
REFERENCE   4  (residues 1 to 559)
  AUTHORS   Martin-Blanco,E. and Garcia-Bellido,A.
  TITLE     Mutations in the rotated abdomen locus affect muscle development
            and reveal an intrinsic asymmetry in Drosophila
  JOURNAL   Proc Natl Acad Sci U S A 93 (12), 6048-6052 (1996)
   PUBMED   8650217
REFERENCE   5  (residues 1 to 559)
  AUTHORS   Lussier,M., Gentzsch,M., Sdicu,A.M., Bussey,H. and Tanner,W.
  TITLE     Protein O-glycosylation in yeast. The PMT2 gene specifies a second
            protein O-mannosyltransferase that functions in addition to the
            PMT1-encoded activity
  JOURNAL   J Biol Chem 270 (6), 2770-2775 (1995)
   PUBMED   7852348
COMMENT     REFSEQ: This record represents a single, non-redundant, protein
            sequence which may be annotated on many different RefSeq genomes
            from the same, or different, species.
            
            ##Evidence-For-Name-Assignment-START##
            Evidence Category  :: HMM
            Evidence Accession :: NF014425.4
            Evidence Source    :: EMBL-EBI
            Source Identifier  :: PF02366.22
            ##Evidence-For-Name-Assignment-END##
            COMPLETENESS: full length.
FEATURES             Location/Qualifiers
     source          1..559
                     /organism="Nakamurella multipartita"
                     /db_xref="taxon:53461"
     Protein         1..559
                     /product="phospholipid carrier-dependent
                     glycosyltransferase"
                     /GO_component="GO:0016020 - membrane [Evidence IEA]"
                     /GO_function="GO:0000030 - mannosyltransferase activity
                     [Evidence IEA]"
                     /GO_process="GO:0006493 - protein O-linked glycosylation
                     [Evidence IEA]"
                     /calculated_mol_wt=61312
     Region          45..558
                     /region_name="PMT1"
                     /note="Dolichyl-phosphate-mannose--protein O-mannosyl
                     transferase [Posttranslational modification, protein
                     turnover, chaperones]; COG1928"
                     /db_xref="CDD:224839"
ORIGIN      
        1 msappsladp ateddiaaar sagatapdte perpdpagtv vaigevpalt rpvrpartlr
       61 papptdrarg wvvtgvvtli aamvrlvnlg satdggtplf dekyyaiqaw emlrnggved
      121 nqafgvvvhp plgkqliaig ewllgynatg wrlasavagi vsvllivrvt rrmtgstllg
      181 giagvllicd gvshvqsrsa lldifqavfv lgafacliad rdqvrarlal avadgsltgt
      241 kagppmgarw wrfgagvllg lttavkwsga ywilafvals liwdmqarre agvrrpvrag
      301 lrrdllpsiw slavvpvlvy vgswwawfas etswprhtlv aepsnrsdwk sgflydvasa
      361 wsnslwqwtw kmldfhahll tptdpskrhp weskpwtwpl gtrpvlyysp adapcpadpa
      421 tecvrrifli gtpalwwisl fvliwalwka igrldwryaa vlvaygagyl pwftnldrqm
      481 yffyatplap flvigitlvl gdilgrrgag ierrltsiav vamyvglvva nfiwlwpiln
      541 gepitherli metwlpswg
//
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