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Database: UniProt
Entry: A0A087DX05_9BIFI
LinkDB: A0A087DX05_9BIFI
Original site: A0A087DX05_9BIFI 
ID   A0A087DX05_9BIFI        Unreviewed;       402 AA.
AC   A0A087DX05;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyltransferase {ECO:0000313|EMBL:KFJ00056.1};
DE            EC=2.7.8.35 {ECO:0000313|EMBL:KFJ00056.1};
GN   ORFNames=BSTEL_1106 {ECO:0000313|EMBL:KFJ00056.1};
OS   Bifidobacterium stellenboschense.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=762211 {ECO:0000313|EMBL:KFJ00056.1, ECO:0000313|Proteomes:UP000029004};
RN   [1] {ECO:0000313|EMBL:KFJ00056.1, ECO:0000313|Proteomes:UP000029004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23968 {ECO:0000313|EMBL:KFJ00056.1,
RC   ECO:0000313|Proteomes:UP000029004};
RA   Ventura M., Milani C., Lugli G.A.;
RT   "Genomics of Bifidobacteria.";
RL   Submitted (MAR-2014) 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:KFJ00056.1}.
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DR   EMBL; JGZP01000005; KFJ00056.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087DX05; -.
DR   STRING; 762211.BSTEL_1106; -.
DR   eggNOG; COG0472; Bacteria.
DR   OrthoDB; 9783652at2; -.
DR   Proteomes; UP000029004; 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   CDD; cd06853; GT_WecA_like; 1.
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:KFJ00056.1};
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:UP000029004};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFJ00056.1};
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..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        48..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        81..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        140..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        191..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        226..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        256..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        310..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        338..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          376..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..394
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         157
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT   BINDING         223
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ   SEQUENCE   402 AA;  43163 MW;  E04D79563E682C87 CRC64;
     MRIYLFIAAI AGGATYLLTP IVRHVAIEIG AVGEVRARDV HKIPTPRMGG LGMMLGFAVA
     MLFASRISFI QGLFQGSHLP WVVLAGAVMI CLLGMADDLW DLDWMLKLAG QLLISVFVAW
     GGLQIISLPL GSLVTASPSL SMAITAFLIV ASINAVNFVD GLDGLASGIV AIGGIAFAIY
     SYILARTSPS YASMATLIDV ALVGICVGFI LHNWHPAKLF MGDSGSMLLG YLITCASIVM
     TGRIDPASVH TSMYLPVFMP ILLPILVLFL PVLDMCLAIV RRLAKGQSPM HPDRMHLHHR
     MLRIGHTVRG AVAILWSWAA LISFGSLMIL FFRAWHVFVG MAVVGAVLAV VTMYPYLKRR
     VPEIMEENAR EAVAKAEHAS GRVNMGDPDD VDGDGKASGN AV
//
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