ID A0A094PVP8_9ACTN Unreviewed; 374 AA.
AC A0A094PVP8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=UDP-N-acetylmuramyl pentapeptide phosphotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=GM43_0240 {ECO:0000313|EMBL:KGA06111.1};
OS actinobacterium acMicro-4.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504317 {ECO:0000313|EMBL:KGA06111.1, ECO:0000313|Proteomes:UP000029304};
RN [1] {ECO:0000313|EMBL:KGA06111.1, ECO:0000313|Proteomes:UP000029304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) 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:KGA06111.1}.
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DR EMBL; JNSD01000001; KGA06111.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094PVP8; -.
DR STRING; 1504317.GM43_0240; -.
DR PATRIC; fig|1504317.4.peg.51; -.
DR Proteomes; UP000029304; 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 Transferase {ECO:0000256|ARBA:ARBA00022679};
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..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..133
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 315..348
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 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 374 AA; 39775 MW; 63F54D4449A1ED78 CRC64;
MSFYVVITLI AFAVSFGLAL VLWRLGIKHR WHREIRPRDV HKEPTPRLGG IAVFVGMATA
AVIASPFEAF AGVFDDPRPI LSVFAAAFIV VALGVVDDLI ELDWLTKLSG QIIAAGVVAW
QGVQIVSLPI GGITLFSPAL SLILTVLAIV LVMNAVNFID GLDGLVAGVA LISTGVFFLY
SFVLSIGDSR VTGFSLATFL TLLLAGGLLG FLPLNWHPAK LFLGDSGSLL VGLMMSVSAI
SVTGQIDPAT VSPTQLLPAF LPVILPLAVL IVPLVDFSWA VGRRLRRGMS PFDADRAHLH
HRLLDMGHTH QQAVLILYAW TAVLAIGTLM FLFVAWYFAV AIIAIGLIGS ALVTVSPGSS
ATNDPLALDQ EVSP
//
