ID A0A1G8FTD5_9MICC Unreviewed; 336 AA.
AC A0A1G8FTD5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate transferase {ECO:0000313|EMBL:SDH85419.1};
GN ORFNames=SAMN04488693_103189 {ECO:0000313|EMBL:SDH85419.1};
OS Arthrobacter subterraneus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=335973 {ECO:0000313|EMBL:SDH85419.1, ECO:0000313|Proteomes:UP000199258};
RN [1] {ECO:0000313|EMBL:SDH85419.1, ECO:0000313|Proteomes:UP000199258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP_1H {ECO:0000313|EMBL:SDH85419.1,
RC ECO:0000313|Proteomes:UP000199258};
RA de Groot N.N.;
RL Submitted (OCT-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; FNDT01000003; SDH85419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8FTD5; -.
DR STRING; 335973.SAMN04488693_103189; -.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000199258; 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; cd06854; GT_WbpL_WbcO_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:UP000199258};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SDH85419.1};
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..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 45..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 204
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 336 AA; 35684 MW; 82777A1B83CEF94C CRC64;
MLLWTVVGTS LLLSLVLPFV LKPILHRLGV LDIPNERSSH HSVVIRGVGI TVAVGIVVGL
ALSVLTGLVP VDRSVVLIVL FMLSAAALLG WIEDYRGVSI RSRALIQLMI GAVGTLALAW
TIEQSYWWVP VGALAVAAYI NAANFMDGIN GISGLHGVLV GIFYSVAGTM VGQFWLTVAG
LVVAAAFAGF LPWNLGRGFV FLGDVGSYLL GASIAGMAVA GLLAGVYLEY LFSPVLIYLA
DTFLTFLRRV RAGKRWYASH REHVYQRLTD VGLTHLQSAL VVTVCSALVG VAGFILATAP
PPLAIACSLF AAAVVALYIY SPVILARLRR SASADR
//
