ID A0A1P8NDB2_9MICO Unreviewed; 374 AA.
AC A0A1P8NDB2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:APX32287.1};
GN ORFNames=BH708_05610 {ECO:0000313|EMBL:APX32287.1};
OS Brachybacterium sp. P6-10-X1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=1903186 {ECO:0000313|EMBL:APX32287.1, ECO:0000313|Proteomes:UP000185991};
RN [1] {ECO:0000313|EMBL:APX32287.1, ECO:0000313|Proteomes:UP000185991}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P6-10-X1 {ECO:0000313|EMBL:APX32287.1,
RC ECO:0000313|Proteomes:UP000185991};
RA Zhao B., Liao L., Chen B.;
RT "Complete genome of Brachybacterium sp. P6-10-X1.";
RL Submitted (SEP-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}.
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DR EMBL; CP017297; APX32287.1; -; Genomic_DNA.
DR RefSeq; WP_076807287.1; NZ_CP017297.1.
DR AlphaFoldDB; A0A1P8NDB2; -.
DR STRING; 1903186.BH708_05610; -.
DR KEGG; brx:BH708_05610; -.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000185991; Chromosome.
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:APX32287.1};
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..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 374 AA; 40119 MW; 5BA0BF3B2BA0338D CRC64;
MRIYLFILLV AAAVTYLITP AVRLLARRAG AMTAVRERDV HDAVTPRLGG LAMLAGVVVA
MLIASNVPFL EGLFRDTRQP WAILVAAALV CLLGAADDKW DLDWWAKLAG QVLAAMLLAW
QGVSLVSLPI GGVTILSERS ALILTVLVVV VSMNAVNFVD GLDGLAAGVM AIGGSAFFLY
AYMLTRTVST TDYSSLAALL TAVLIGACVG FLPHNMTRAR IFMGDSGSML LGLLLAASTI
AVTGQVDPAR LSGADIFGQF LPILLPIGVM VIPFLDFALA VVRRIGSGKS PFHADKAHLH
HRLLRLGHSK RTAVLIMYTW TVVVSVGLLL PIMVSTRAVV IFWVCGLLFA LLLTFDPLRW
RPGRHRKDSD VPST
//
