ID A0A0G0GJ54_9BACT Unreviewed; 355 AA.
AC A0A0G0GJ54;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Undecaprenyl-phosphate N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:KKQ26140.1};
GN ORFNames=US39_C0002G0066 {ECO:0000313|EMBL:KKQ26140.1};
OS Microgenomates group bacterium GW2011_GWC1_37_12b.
OC Bacteria.
OX NCBI_TaxID=1618510 {ECO:0000313|EMBL:KKQ26140.1, ECO:0000313|Proteomes:UP000034251};
RN [1] {ECO:0000313|EMBL:KKQ26140.1, ECO:0000313|Proteomes:UP000034251}
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:KKQ26140.1}.
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DR EMBL; LBSU01000002; KKQ26140.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0GJ54; -.
DR STRING; 1618510.US39_C0002G0066; -.
DR PATRIC; fig|1618510.3.peg.293; -.
DR Proteomes; UP000034251; 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:KKQ26140.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..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..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..350
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 355 AA; 38618 MW; B9648D2F85A1E05A CRC64;
MNGFFKLVLP LLFSALAAYI ITPVVIKVAH KYKLIDDPKK NKHPKVIHDR PTPRGGGLAI
YLAFASASLI FLPLDKHLVG ILLGAAVLVI TGLLDDRYNL NPYLRLIIQF FAAALPIASG
IGIAFINNPL GGSIDLSLPQ ITFNLLGETR SIWLLSDMFA LFWIVGLMNI LNMGAKGVDG
QLSGVVIISS LVIAILSFKY SADITEWPVL ILSLIVAGSF LGFLPWHFFP QKIMPGFSGS
TLAGFLLAVL SILTTTKVGT LLVVLGIPIV DTGYTITRRI LSGKSPLWGD TGHLHHKLLA
AGYSKKQVSF IYWGFSLTLG IIALNLNTSF KFYTIIGIVL IVGAMLLWLT HKPKK
//
