ID A0A0G1KN36_9BACT Unreviewed; 365 AA.
AC A0A0G1KN36;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Undecaprenyl-phosphate N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:KKT49379.1};
GN ORFNames=UW41_C0007G0010 {ECO:0000313|EMBL:KKT49379.1};
OS Candidatus Collierbacteria bacterium GW2011_GWC2_44_18.
OC Bacteria; Candidatus Collierbacteria.
OX NCBI_TaxID=1618392 {ECO:0000313|EMBL:KKT49379.1, ECO:0000313|Proteomes:UP000034172};
RN [1] {ECO:0000313|EMBL:KKT49379.1, ECO:0000313|Proteomes:UP000034172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKT49379.1}.
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DR EMBL; LCIE01000007; KKT49379.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KN36; -.
DR STRING; 1618392.UW41_C0007G0010; -.
DR PATRIC; fig|1618392.3.peg.374; -.
DR Proteomes; UP000034172; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKT49379.1};
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..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 365 AA; 39928 MW; 1CF125D646F8C3EB CRC64;
MINPVITIFP FIVAFLISIV VTPLTVIWFS KMGWKIDPKK TPHPAHIHRE PVPKGGGLPI
FVAVILTLAI FLRWDKHLIA IGVACLLVLI TGLVDDVKGI NPYLRLTINF LAVGIIVASG
IGIAYVSNPF GGVIDLSQWR WGFEFLGKYH EIWILADLFA LLWIPVLMNA INWSSGVDGQ
ISGVVTIAAI ALGLISLSFS ADIAQWPVAT LAFALSGSFA GLTIFHFFPQ KIMPGYSATS
LAGLLLGVIS ILATAKVGTV LVVLGVPLVD FTYIVIKRML SGKSPVWGDK SHLHHKLLKL
GWGKRRIALF YWLITAILGL TAVKVEARSK LIIMVGLVIL MLGFMLWQYS WHFSKKSGRD
SGSKI
//