ID MRAY_PORG3 Reviewed; 419 AA. AC B2RIE8; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 14-DEC-2022, entry version 75. 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}; OrderedLocusNames=PGN_0624; OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM OS 12257 / NCTC 11834 / 2561). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae; OC Porphyromonas. OX NCBI_TaxID=431947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561; RX PubMed=18524787; DOI=10.1093/dnares/dsn013; RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H., RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T., RA Nakayama K.; RT "Determination of the genome sequence of Porphyromonas gingivalis strain RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome RT rearrangements in P. gingivalis."; RL DNA Res. 15:215-225(2008). 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=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:0000255|HAMAP-Rule:MF_00038}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-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; AP009380; BAG33143.1; -; Genomic_DNA. DR RefSeq; WP_012457656.1; NZ_CP025930.1. DR AlphaFoldDB; B2RIE8; -. DR SMR; B2RIE8; -. DR STRING; 431947.PGN_0624; -. DR EnsemblBacteria; BAG33143; BAG33143; PGN_0624. DR GeneID; 29255850; -. DR KEGG; pgn:PGN_0624; -. DR eggNOG; COG0472; Bacteria. DR HOGENOM; CLU_023982_0_0_10; -. DR OMA; LMSPLHH; -. DR BioCyc; PGIN431947:G1G2V-685-MON; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000008842; 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 PANTHER; PTHR22926; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE; 1. DR Pfam; PF00953; Glycos_transf_4; 1. DR Pfam; PF10555; MraY_sig1; 1. DR TIGRFAMs; TIGR00445; mraY; 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; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..419 FT /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase" FT /id="PRO_1000090656" FT TRANSMEM 22..42 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 99..119 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 208..228 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 238..258 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 278..298 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 303..323 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 328..348 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" FT TRANSMEM 396..416 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038" SQ SEQUENCE 419 AA; 46695 MW; 5D91C69AF45441DA CRC64; MLYYLFDYLE KLQLPGARLF HYVSFRSAVA IILALLLATV IGNRIIERLR KAQIGETIRD LGLEGQLSKK GTPTMGGLII IISILIPTLL LARLDNVYIL LMIVTTLLLG SLGFLDDYIK VFRKKKEGLH GRYKIIGQVG LGFIIGIVLY MNPAVVIKEN SEVLRDGQVE RVHFNKQEVK STKTTIPFVK NNNFDYADIL PFEGKTKVLF GWILFVCVAV VVVTFISNCA NLTDGLDGLA TGSSAIIGVV LAIFAYVSSH IEMASYLNIM FIPGAEELTI FAFAFVGATI GFLWYNAYPA QVFMGDTGSL TLGGIIAVFA LIIRKEMLLP ILCFVFIIEG LSVMIQVFYF KLTKRRTGEG RRIFKMTPLH HHFQKPGNAG IDAWLQKPMQ AIPESKITVR FWLVGIIMAA ITIATLKMR //