ID A0A0J6WUF5_9FIRM Unreviewed; 345 AA.
AC A0A0J6WUF5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=UDP-phosphate N-acetylglucosaminyl 1-phosphate transferase {ECO:0000313|EMBL:KMO86164.1};
GN ORFNames=AB840_09615 {ECO:0000313|EMBL:KMO86164.1};
OS Megasphaera cerevisiae DSM 20462.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Megasphaera.
OX NCBI_TaxID=1122219 {ECO:0000313|EMBL:KMO86164.1, ECO:0000313|Proteomes:UP000036503};
RN [1] {ECO:0000313|EMBL:KMO86164.1, ECO:0000313|Proteomes:UP000036503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20462 {ECO:0000313|EMBL:KMO86164.1,
RC ECO:0000313|Proteomes:UP000036503};
RA Kutumbaka K., Pasmowitz J., Mategko J., Reyes D., Friedrich A., Han S.,
RA Martens-Habbena W., Neal-McKinney J., Janagama H.K., Nadala C.,
RA Samadpour M.;
RT "Draft genome sequence of beer spoilage bacterium Megasphaera cerevisiae
RT type strain 20462.";
RL Submitted (JUN-2015) 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:KMO86164.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LEKT01000031; KMO86164.1; -; Genomic_DNA.
DR RefSeq; WP_048514628.1; NZ_LEKT01000031.1.
DR AlphaFoldDB; A0A0J6WUF5; -.
DR STRING; 39029.BSR42_10850; -.
DR PATRIC; fig|1122219.3.peg.1742; -.
DR InParanoid; A0A0J6WUF5; -.
DR OrthoDB; 9783652at2; -.
DR Proteomes; UP000036503; 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:UP000036503};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KMO86164.1};
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..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..256
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 312..328
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 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 345 AA; 36943 MW; A07DB561287E88E2 CRC64;
MLEYLVPFAI ALIVSYVLTP GVKTLAIKIG AIDKPNARKV HTHVIPRLGG LAIYIGFMAA
VLFSMPVRHD LLGLLLGCSA IVALGIWDDI CNIPAKVKLI GQILAAAIPV AFGIQIEWLT
NPFGTLIVLP EIIAVPVTIF WIIGFTNTVN LIDGLDGLAA GVSFIASISM FLMAYNMNQY
LPAMIIVAMA GAALGFLQYN FNPAKIFMGD TGSMLLGYTM AVSAVLGLVK TAATVALIVP
VIALGLPILD TLFAIIRRKM SGVPVFQPDK GHLHHRLLAL GMTQKQAVLI MYFVSMILGV
VALFVASVSY KTGIVTVLVV LAIIIYSAKR IGILRKTTTN STRKN
//