ID A0A0W0VWF7_9GAMM Unreviewed; 336 AA.
AC A0A0W0VWF7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Alpha-N-acetylglucosaminyltransferase {ECO:0000313|EMBL:KTD24344.1};
GN Name=wecA {ECO:0000313|EMBL:KTD24344.1};
GN ORFNames=Llan_0483 {ECO:0000313|EMBL:KTD24344.1};
OS Legionella lansingensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45067 {ECO:0000313|EMBL:KTD24344.1, ECO:0000313|Proteomes:UP000054869};
RN [1] {ECO:0000313|EMBL:KTD24344.1, ECO:0000313|Proteomes:UP000054869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49751 {ECO:0000313|EMBL:KTD24344.1,
RC ECO:0000313|Proteomes:UP000054869};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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:KTD24344.1}.
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DR EMBL; LNYI01000010; KTD24344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0VWF7; -.
DR STRING; 45067.Llan_0483; -.
DR PATRIC; fig|45067.4.peg.508; -.
DR eggNOG; COG0472; Bacteria.
DR Proteomes; UP000054869; 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; cd06854; GT_WbpL_WbcO_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:KTD24344.1};
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:UP000054869};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KTD24344.1};
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..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 47..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 151
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 336 AA; 37017 MW; DB45337062106F67 CRC64;
MVWFGFFLFV FSLCWVLTGL LRRYALATNL LDIPNHRSSH VVPTPRGGGL AFIVSFLAAV
LFLFYLDLIS FSLSLALLGS GTFVAILGFL DDRRSIPARW RLLGHFVVAG FSIYVLGGMP
SISVFNWIFP AGVLINILAV FYLVWLLNLY NFMDGIDGIA AVEAVTVCLG GALLYYLCGD
ETEIRLPLTL TVAVGGFLCW NFPPARIFMG DAGSGFLGMV LGILSIQAAR IDGNFFWAWL
ILLGVFIVDA TITLLCRAYR GEVLLQAHCS HAYQNASRRY NTHLPVTMGV LVINLLWLFP
MAMMVGLGFI NGSFGLLIAY LPLVVLAFKF NAGKRE
//
