ID A0A318MYK3_9PROT Unreviewed; 344 AA.
AC A0A318MYK3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=UDP-phosphate alpha N-acetylglucosaminyltransferase {ECO:0000313|EMBL:PXZ01661.1};
GN ORFNames=DK869_01220 {ECO:0000313|EMBL:PXZ01661.1};
OS Commensalibacter melissae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae.
OX NCBI_TaxID=2070537 {ECO:0000313|EMBL:PXZ01661.1, ECO:0000313|Proteomes:UP000247565};
RN [1] {ECO:0000313|EMBL:PXZ01661.1, ECO:0000313|Proteomes:UP000247565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ESL0284 {ECO:0000313|EMBL:PXZ01661.1,
RC ECO:0000313|Proteomes:UP000247565};
RA Ellegaard K.M.;
RT "Reference genomes for bee gut microbiota database.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR600715-1};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PXZ01661.1}.
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DR EMBL; QGLT01000001; PXZ01661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A318MYK3; -.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000247565; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE; 1.
DR PANTHER; PTHR22926:SF3; UNDECAPRENYL-PHOSPHATE ALPHA-N-ACETYLGLUCOSAMINYL 1-PHOSPHATE TRANSFERASE; 1.
DR Pfam; PF00953; Glycos_transf_4; 1.
PE 4: Predicted;
KW Glycosyltransferase {ECO:0000313|EMBL:PXZ01661.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR600715-1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR600715-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000247565};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PXZ01661.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 148
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 205
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 344 AA; 38887 MW; 31DDA7192D492ED3 CRC64;
MNSVNYKYLL LIWLISNTLL SATIVKYVAS VGIMDNPNQR SSHTFPIPKG GGIGIISAFL
TANISFIYLF NQHYSLSIIG LLSIITFISL FSWLDDIKQW SALSKLAIQF IASVSVCIFV
FPASFLENHL YLLPFFIIWL VYITNAYNFM DGLNGLAAGV AAICCLFIYF YSTNLENKIF
ALSLLTGLLG FLPFNFPKAE IFMGDVGSQA CGLILASFAI IPLGTAINSD FVTLISQNVI
IFFLLFGFIF DVTFTLIRRI INKEPYLQAH RSHLYQMAHR SHISPILITF IECLFCIWGG
FLFYIFPLTS LQNIELACSL LILPQLIWTL FILYKTQSLN IKKW
//
