ID A0A1I0M5T9_9FIRM Unreviewed; 322 AA.
AC A0A1I0M5T9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000313|EMBL:SEV82731.1};
GN ORFNames=SAMN05216413_0105 {ECO:0000313|EMBL:SEV82731.1};
OS Ruminococcaceae bacterium KH2T8.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=1855400 {ECO:0000313|EMBL:SEV82731.1, ECO:0000313|Proteomes:UP000198503};
RN [1] {ECO:0000313|EMBL:SEV82731.1, ECO:0000313|Proteomes:UP000198503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH2T8 {ECO:0000313|EMBL:SEV82731.1,
RC ECO:0000313|Proteomes:UP000198503};
RA de Groot N.N.;
RL Submitted (OCT-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; FOIY01000001; SEV82731.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0M5T9; -.
DR STRING; 1855400.SAMN05216413_0105; -.
DR Proteomes; UP000198503; 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: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:UP000198503};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SEV82731.1};
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..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 192..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 160
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 322 AA; 35238 MW; 441D6FD31E5570A7 CRC64;
MLYYVGAAAA SVLSFILTFL CMKFLPLGDK LLGHDRGRLY AAGSEVNIGK PTGVGFYFVF
VTVIVSLIFT FSGSSYLFMM ILVLLSMLFG FLDDRSKNPW GEYIKGALDF LIAGIGAAVF
TLFYGTDVII GITGYPVHIP LWLFFFLAVM LIIVSVNATN ATDGVDGLSG TLTILTLITF
MIVARINGTI NYHGYVRGFV LIASLVAYLI FNFNPSKVLM GDAGSRAIGF FIAFYAMYLK
IPFAYLIVCL PFLIDGGLSI LKITIGRLTK KKIIILKNVT TPIHDHLKKR KGFSVKKTWA
FIVACAAVLD LIYVVVCAVV KG
//
