ID A0A0A1MP57_9BACI Unreviewed; 358 AA.
AC A0A0A1MP57;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Putative undecaprenyl-phosphate N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:CEI80846.1};
GN Name=tagO_2 {ECO:0000313|EMBL:CEI80846.1};
GN ORFNames=BN997_00656 {ECO:0000313|EMBL:CEI80846.1};
OS Oceanobacillus oncorhynchi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI80846.1, ECO:0000313|Proteomes:UP000040453};
RN [1] {ECO:0000313|EMBL:CEI80846.1, ECO:0000313|Proteomes:UP000040453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oc5 {ECO:0000313|EMBL:CEI80846.1,
RC ECO:0000313|Proteomes:UP000040453};
RA Urmite Genomes Urmite Genomes;
RL Submitted (NOV-2014) 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; CDGG01000001; CEI80846.1; -; Genomic_DNA.
DR RefSeq; WP_042529625.1; NZ_CDGG01000001.1.
DR AlphaFoldDB; A0A0A1MP57; -.
DR STRING; 545501.BN997_00656; -.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000040453; 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:UP000040453};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CEI80846.1};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 48..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 238..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 213
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 358 AA; 38982 MW; 9A1C8709DE072182 CRC64;
MWSAAELLIA FVIALLTAII TTPIIIWISK KCNLVDQPDN RKQHQRAVPS IGGLAIFIGI
AAGFLYLQPE HPQMTAIIIG GIIMLLTGFL DDILDLRPGT KLLGQIGAAS VVAYSGLVIE
KVTLPFMGTV FLGEYVGIAL TIFWIVAAAN AINLIDGLDG LAGGVSTIAF TSILIMAIMD
YRVIVIGLCV LLIGATLGFL AFNFHPAKIF MGDTGALFLG YSIAIISMLG LFKNVAFFSF
VIPIIVIALP VFDTLLAIIR RINNKQGISV ADRNHIHYLL LKNGYSHRQS VWIIYAFSMF
FGVMAIVVNN AQLMTSLAVF CFVLLGIHLF SVVCGIRARG SFISLVNKKE ELHKRRLK
//