ID A0A317MRS8_9GAMM Unreviewed; 344 AA.
AC A0A317MRS8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=UDP-N-acetylmuramyl pentapeptide phosphotransferase/UDP-N-acetylglucosamine-1-phosphate transferase {ECO:0000313|EMBL:PWV58580.1};
GN ORFNames=C7443_1157 {ECO:0000313|EMBL:PWV58580.1};
OS Plasticicumulans acidivorans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria;
OC Candidatus Competibacteraceae; Plasticicumulans.
OX NCBI_TaxID=886464 {ECO:0000313|EMBL:PWV58580.1, ECO:0000313|Proteomes:UP000246569};
RN [1] {ECO:0000313|EMBL:PWV58580.1, ECO:0000313|Proteomes:UP000246569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23606 {ECO:0000313|EMBL:PWV58580.1,
RC ECO:0000313|Proteomes:UP000246569};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PWV58580.1}.
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DR EMBL; QGTJ01000015; PWV58580.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317MRS8; -.
DR Proteomes; UP000246569; 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; cd06854; GT_WbpL_WbcO_like; 1.
DR InterPro; IPR000715; Glycosyl_transferase_4.
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.
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:UP000246569};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:PWV58580.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 76..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..122
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..180
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 344 AA; 36918 MW; 2C127DBA72515438 CRC64;
MALFPFLVAF VVALWLTRSL CDPASRFRLR LIDHPNERSL HTLPTPRSGG VAVLGGVGAG
LSIAFIQQPI LRAEDLFWLI LPAALIAVIS LLDDRKSIAA RWRLLVHFVA AIAFLLLGPA
PADIGMPGGG GLSAEGLMVV FVIIFLVWMT NLYNFMDGMD GFAGGMAAIG FGAFALLGMM
AGADGFSVVA GVIAAAATGF LCLNFPPARI FMGDTGSATL GFLAGGMILW AQHDGVFPFW
IGVLVFSPFA VDATVTLIRR AVQGERVWEP HRTHFYQRLV QLGWGHRKTV LAEYTLMLAC
AIAAFVAGRL GVLGQQLLVF AVVIVYGVLM IVVTRLERRV GAHQ
//