ID A0A3G9J8J6_9FIRM Unreviewed; 324 AA.
AC A0A3G9J8J6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000256|HAMAP-Rule:MF_00038};
DE EC=2.7.8.13 {ECO:0000256|HAMAP-Rule:MF_00038};
DE AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00038};
GN Name=mraY {ECO:0000256|HAMAP-Rule:MF_00038,
GN ECO:0000313|EMBL:BBH27517.1};
GN ORFNames=SG0102_24510 {ECO:0000313|EMBL:BBH27517.1};
OS Intestinibaculum porci.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Intestinibaculum.
OX NCBI_TaxID=2487118 {ECO:0000313|EMBL:BBH27517.1, ECO:0000313|Proteomes:UP000268059};
RN [1] {ECO:0000313|EMBL:BBH27517.1, ECO:0000313|Proteomes:UP000268059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG0102 {ECO:0000313|EMBL:BBH27517.1,
RC ECO:0000313|Proteomes:UP000268059};
RA Kim J.S., Choe H., Lee Y.R., Kim K.M., Park D.S.;
RT "Novel Erysipelotrichaceae bacterium isolated from small intestine of a
RT swine.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the initial step of the lipid cycle reactions in
CC the biosynthesis of the cell wall peptidoglycan: transfers
CC peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-
CC pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding
CC undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
CC {ECO:0000256|HAMAP-Rule:MF_00038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-
CC D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-
CC alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-
CC alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-
CC alanyl-D-alanine + UMP; Xref=Rhea:RHEA:28386, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:60392, ChEBI:CHEBI:61386, ChEBI:CHEBI:61387; EC=2.7.8.13;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00038};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00038,
CC ECO:0000256|PIRSR:PIRSR600715-1};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00038}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00038};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00038}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC subfamily. {ECO:0000256|ARBA:ARBA00005583, ECO:0000256|HAMAP-
CC Rule:MF_00038}.
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DR EMBL; AP019309; BBH27517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G9J8J6; -.
DR KEGG; ebm:SG0102_24510; -.
DR InParanoid; A0A3G9J8J6; -.
DR OrthoDB; 9805475at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000268059; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051992; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd06852; GT_MraY; 1.
DR HAMAP; MF_00038; MraY; 1.
DR InterPro; IPR000715; Glycosyl_transferase_4.
DR InterPro; IPR003524; PNAcMuramoyl-5peptid_Trfase.
DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS.
DR NCBIfam; TIGR00445; mraY; 1.
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 Pfam; PF10555; MraY_sig1; 1.
DR PROSITE; PS01347; MRAY_1; 1.
DR PROSITE; PS01348; MRAY_2; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00038};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_00038};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00038};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00038};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00038};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00038, ECO:0000256|PIRSR:PIRSR600715-
KW 1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00038};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00038,
KW ECO:0000256|PIRSR:PIRSR600715-1};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00038};
KW Reference proteome {ECO:0000313|Proteomes:UP000268059};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00038};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00038};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00038}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 154..173
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 180..198
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 204..221
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 228..247
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 253..276
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT BINDING 172
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 324 AA; 35470 MW; CB6DF247E0745BDE CRC64;
MNYIRLLASF ALALAIVFVV MPRMIPFLHK LKFGQVEREE GLASHKKKQG TPTMGGIVFI
IAAVVAVYLV NLHLLKNPYM NLLTYTFLGF GFIGFIDDFL IVAKHSNKGL SPKAKYGLQS
LFAIGFILLA KQFLPNYSTE IIIPGTHNDV DLAWFYPIFV FIMFTAESNA VNLADGLDGL
ATGLSMIAIA PFLVFALIQK NVPVALFSAA LEGGLLGFLY FNAHPAKIFM GDNGSLALGA
VLAALAVMTK QELLLILIGI VPLCETLSVI IQVISFKTTG KRVFKMAPIH HHFEMCGWSE
TKVVFVFWLV GFIAAILGLL LGVR
//
