ID A0A151C183_9MICO Unreviewed; 365 AA.
AC A0A151C183;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:KYH45827.1};
GN ORFNames=AZH51_09060 {ECO:0000313|EMBL:KYH45827.1};
OS Branchiibius sp. NY16-3462-2.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC Branchiibius.
OX NCBI_TaxID=1807500 {ECO:0000313|EMBL:KYH45827.1, ECO:0000313|Proteomes:UP000075667};
RN [1] {ECO:0000313|EMBL:KYH45827.1, ECO:0000313|Proteomes:UP000075667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NY16-3462-2 {ECO:0000313|EMBL:KYH45827.1};
RA Lapierre P., Halse T.A., Shea J., Musser K.A., Escuyer V.E.;
RT "Draft genome assembly of Branchiibius sp. 15-3462-2 from a clinical sputum
RT sample.";
RL Submitted (MAR-2016) 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:KYH45827.1}.
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DR EMBL; LVCF01000001; KYH45827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151C183; -.
DR STRING; 1807500.AZH51_09060; -.
DR Proteomes; UP000075667; 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 Reference proteome {ECO:0000313|Proteomes:UP000075667};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KYH45827.1};
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..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..356
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 158
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 365 AA; 38510 MW; 4832C51A16A018BA CRC64;
MREYVLVAVI AGVITFVITP AVRWLAIRFG AFTPVRGRDV HTTPVPRLGG VGMLVGFAAA
LVVADHLPYL SRTISDNFGP LVGVLIAATL ITALGAVDDF RELDPITKFA GQMIAAGVMA
YAGVTMVNIP LGGQTILPAP ILVAITILIV IATTTAVNFV DGLDGLAAGI VAIAGITFFL
WTYSIASRDV PGSVFSSAAF IAAALIGICL GFLPHNFHPA RLFMGDAGAL LLGLLLSAAT
ISFTGNFDPA GATGQSATYA SWLPIALPML VLALPIIDVV WAVVRRRGKF WTADSKHLHH
RMLQMGHPHR EAVLLLYLWS AAGALSILAL AYLPAVVALV LLAVLLVASL ALTWGLPKWR
RTRSL
//
