ID A0A0G1R8W6_9BACT Unreviewed; 342 AA.
AC A0A0G1R8W6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000313|EMBL:KKU26493.1};
GN ORFNames=UX37_C0002G0059 {ECO:0000313|EMBL:KKU26493.1};
OS Microgenomates group bacterium GW2011_GWA2_46_16.
OC Bacteria.
OX NCBI_TaxID=1618501 {ECO:0000313|EMBL:KKU26493.1, ECO:0000313|Proteomes:UP000034885};
RN [1] {ECO:0000313|EMBL:KKU26493.1, ECO:0000313|Proteomes:UP000034885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKU26493.1}.
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DR EMBL; LCLY01000002; KKU26493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1R8W6; -.
DR PATRIC; fig|1618501.3.peg.100; -.
DR Proteomes; UP000034885; 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 InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
DR PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE; 1.
DR PANTHER; PTHR22926:SF5; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE HOMOLOG; 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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KKU26493.1};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 61..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 102..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 342 AA; 37700 MW; 4D7F2CAEDC558586 CRC64;
MNTLLGFLLF SFTINAALIV PFINLLYYLK FQRPHRGTSD FMGTVNSIFN KLHKKKAGTP
VGGGLLIIIA TTILFTLVTS ILRLVGADMQ SVYDYQREIS VLFATFILYG LLGLYDDVIK
FFGKTTRLVG ISWRLKLIGQ IFIGLGIGWY LYTQLGISII NVPYFGVMDL GWFFVPFVAF
ILTAFSNAVN VTDGLDGLAG GLLMISLFAL IILATSIIDT PITLFIALWL GGILAFLYFN
TYPARIFLGD VGALSFGATL AVIGLMLGKI IAVTIIGGLF VLEIGTSTLQ MFGKRYLGHR
LLPISPFHLW LQTIGWVEPK IVTRAWLAGI ILALFGLWLA FL
//
