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Database: UniProt
Entry: A0A1M5J808_9FIRM
LinkDB: A0A1M5J808_9FIRM
Original site: A0A1M5J808_9FIRM 
ID   A0A1M5J808_9FIRM        Unreviewed;       273 AA.
AC   A0A1M5J808;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate transferase {ECO:0000313|EMBL:SHG36714.1};
GN   ORFNames=SAMN02745221_00009 {ECO:0000313|EMBL:SHG36714.1};
OS   Thermosyntropha lipolytica DSM 11003.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC   Thermosyntropha.
OX   NCBI_TaxID=1123382 {ECO:0000313|EMBL:SHG36714.1, ECO:0000313|Proteomes:UP000242329};
RN   [1] {ECO:0000313|Proteomes:UP000242329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11003 {ECO:0000313|Proteomes:UP000242329};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-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; FQWY01000002; SHG36714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M5J808; -.
DR   STRING; 1123382.SAMN02745221_00009; -.
DR   Proteomes; UP000242329; 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   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:UP000242329};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SHG36714.1};
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        47..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        117..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        171..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        221..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         157
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   273 AA;  29960 MW;  36DF4E6E338C6165 CRC64;
     MTTFYLMQVI PLLLGALAEG AVLFLLLNML RETGATAKNF QGVDIPVSAG LSFPMALIIV
     VVIYELWGWY EDAYLLFIFG VVAISFLGFI DDRLGGRDTL GFKGHFSALF KGRLTTGGLK
     ALGGGFISLF LALALSNGWY DIIINTLIIA LFTNLLNLLD LRPGRAVKGF LFLGLIIAAL
     ARWQLNFLLI LPVVGAVIVY FPVDLKARAM MGDAGSNVLG LVLGYLCVTS LDFPYRLGIL
     VFLLAVHLYT EKYSLTETIE HSKVLKWLDD LGR
//
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