ID MRAY_BEII9 Reviewed; 360 AA. AC B2IGF7; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-2008, sequence version 1. DT 04-NOV-2026, entry version 86. DE RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase {ECO:0000255|HAMAP-Rule:MF_00038}; DE EC=2.7.8.13 {ECO:0000255|HAMAP-Rule:MF_00038}; DE AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00038}; GN Name=mraY {ECO:0000255|HAMAP-Rule:MF_00038}; GN OrderedLocusNames=Bind_0689; OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB OS 8712). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Beijerinckiaceae; Beijerinckia. OX NCBI_TaxID=395963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712; RX PubMed=20601475; DOI=10.1128/jb.00656-10; RA Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C., RA Dunfield P.F.; RT "Complete genome sequence of Beijerinckia indica subsp. indica."; RL J. Bacteriol. 192:4532-4533(2010). 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:0000255|HAMAP-Rule:MF_00038}. CC -!- CATALYTIC ACTIVITY: CC Reaction=UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso- CC 2,6-diaminopimeloyl-D-alanyl-D-alanine + di-trans,octa-cis- CC undecaprenyl phosphate = di-trans,octa-cis-undecaprenyl diphospho-N- CC acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl- CC D-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:0000255|HAMAP-Rule:MF_00038}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00038}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00038}. CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP- CC Rule:MF_00038}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00038}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00038}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001016; ACB94339.1; -; Genomic_DNA. DR RefSeq; WP_012383697.1; NC_010581.1. DR AlphaFoldDB; B2IGF7; -. DR SMR; B2IGF7; -. DR STRING; 395963.Bind_0689; -. DR KEGG; bid:Bind_0689; -. DR eggNOG; COG0472; Bacteria. DR HOGENOM; CLU_023982_0_0_5; -. DR OMA; AACMGFL; -. DR OrthoDB; 9805475at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000001695; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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:RHEA. DR GO; GO:0071555; P:cell wall organization; IEA:TreeGrafter. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. 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; Cell division; Cell inner membrane; Cell membrane; Cell shape; KW Cell wall biogenesis/degradation; Magnesium; Membrane; Metal-binding; KW Peptidoglycan synthesis; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..360 FT /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase" FT /id="PRO_1000090592" FT TRANSMEM 27..47 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 72..92 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 94..114 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 135..155 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 167..187 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 199..219 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 236..256 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 263..283 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 289..309 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 337..357 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" SQ SEQUENCE 360 AA; 38699 MW; 03BDA2754CBEC807 CRC64; MLTWLAEFAV YFTPLNLFRY ITFRTGGAIA TALFFVFFFG PNIIKSLRIK QGKGQPIRSD GPQSHLLTKK GTPTMGGLMI LSGLFVSTLL WANLSNHYVW VVLWVMLGYG AIGFYDDYLK VTKQTHNGFS GRGRLACEAG VALVACIAMM KLGTPHMTSL AFPAVNGYVV DLGLFFLIFG PFVIVASGNA VNLTDGLDGL AIVPVMIAAG TFGIIAYLVG NAIYSDYLRI NFVPGAGELA VVSGAVIGAG LGFLWFNAPP AQIFMGDTGS LALGGLLGTI AVAIKHEMVL AIVGGLFALE TLSVIVQVVS FKLTGKRVFK MAPIHHHFEQ LGWSEPQVVV RFWIIAFVLA LVGLSTLKLR //