ID A0A1Y0IGS4_9GAMM Unreviewed; 348 AA.
AC A0A1Y0IGS4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphatetransferase {ECO:0000313|EMBL:ARU59500.1};
GN ORFNames=OLMES_5520 {ECO:0000313|EMBL:ARU59500.1};
OS Oleiphilus messinensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oleiphilaceae; Oleiphilus.
OX NCBI_TaxID=141451 {ECO:0000313|EMBL:ARU59500.1, ECO:0000313|Proteomes:UP000196027};
RN [1] {ECO:0000313|EMBL:ARU59500.1, ECO:0000313|Proteomes:UP000196027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ME102 {ECO:0000313|EMBL:ARU59500.1,
RC ECO:0000313|Proteomes:UP000196027};
RA Kozyavkin S.A., Slesarev A.I., Golyshin P.N., Korzhenkov A.,
RA Golyshina O.N., Toshchakov S.V.;
RT "Genomic insights into alkan degradation activity of Oleiphilus
RT messinensis.";
RL Submitted (MAY-2017) 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; CP021425; ARU59500.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0IGS4; -.
DR KEGG; ome:OLMES_5520; -.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000196027; 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 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:UP000196027};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ARU59500.1};
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 69..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 150
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 348 AA; 37716 MW; F8D86169EF089B11 CRC64;
MSGVLHLIPS FLATITAIYL LTPIARAVGL VDLPGGRKQH DFPTPLVGGL SIYLGSMTMA
IVSPPIFEMY SNIFFIGGIV LVTGLLDDWK NLKVITRLSV YSLSGLVMIW STDTAITSFG
DILTFGDLSL GLIAIPVTLL SINCAINAVN MSDGLDGLAA GLVLVTLSAL IFIGYSKGNE
YEIRLLFFIC VSVTAFFVLN FRFPWVTQAS VFLGDSGSVF LGFIISWALI TLSQGELAVI
SPPVSLWLFA VPLLDITNVV VKRLISGTSP TQSDRRHLHH ILLRAGFGVR ATVLILILLA
TFYAVIGILF TFYNTPDSII FWIFIALGAT TLHAVNLLEK RCSESSHI
//
