ID A0A0E9M0R4_9BACT Unreviewed; 314 AA.
AC A0A0E9M0R4;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Undecaprenyl-phosphate N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:GAO31089.1};
GN ORFNames=JCM15548_13425 {ECO:0000313|EMBL:GAO31089.1};
OS Geofilum rubicundum JCM 15548.
OC Bacteria; Bacteroidota; Bacteroidia; Marinilabiliales; Marinilabiliaceae;
OC Geofilum.
OX NCBI_TaxID=1236989 {ECO:0000313|EMBL:GAO31089.1, ECO:0000313|Proteomes:UP000032900};
RN [1] {ECO:0000313|EMBL:GAO31089.1, ECO:0000313|Proteomes:UP000032900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15548 {ECO:0000313|EMBL:GAO31089.1};
RX PubMed=25736980;
RA Inoue J., Oshima K., Suda W., Sakamoto M., Iino T., Noda S., Hongoh Y.,
RA Hattori M., Ohkuma M.;
RT "Distribution and evolution of nitrogen fixation genes in the phylum
RT bacteroidetes.";
RL Microbes Environ. 30:44-50(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:GAO31089.1}.
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DR EMBL; BAZW01000037; GAO31089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E9M0R4; -.
DR STRING; 1236989.JCM15548_13425; -.
DR Proteomes; UP000032900; 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 InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
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.
DR PROSITE; PS01348; MRAY_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000032900};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:GAO31089.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 22..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..219
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 240..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 274..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 163
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 314 AA; 35190 MW; 7ADE0BB0DB9DDC6D CRC64;
MAIFFGILFT YSFYLDWFDY RAIPYLIPSL LIIFSIGIKD DIMVTAPIMK LMGQVIAALI
IVGFGDLRIT DFHGFFGLRP DYFVSLAFSL LFLVFIVNGF NLIDGVDGLA AITGIVSITG
FSVWFYINGE VVLPVLGAIV NGALLAFLYF NVLSKSQKIF MGDTGSLLIG FIVAVFGIRF
MEYNVEPLRP ALRFTMISAP AVALAILIVP VIDTIRVFFL RLSKGQSPFA ADKTHIHHRL
LTLGFSHIQV ALLLGSVNVI FILLSYWLRD LGTIKLLSIN MILGLVVFHL PSLAIRYRLR
KMRSRKLNER SLHK
//
