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 13-JUL-2010, entry version 20. DE RecName: Full=Phospho-N-acetylmuramoyl-pentapeptide-transferase; DE EC=2.7.8.13; DE AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase; GN Name=mraY; OrderedLocusNames=PGN_0624; OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / JCM 12257). OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=431947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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 RT strain ATCC 33277 and genomic comparison with strain W83 revealed RT extensive genome rearrangements in P. gingivalis."; RL DNA Res. 15:215-225(2008). CC -!- FUNCTION: First step of the lipid cycle reactions in the CC biosynthesis of the cell wall peptidoglycan (By similarity). CC -!- CATALYTIC ACTIVITY: UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala- CC D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D- CC Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane CC protein (By similarity). CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY CC subfamily. 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; YP_001928740.1; -. DR GeneID; 6329658; -. DR GenomeReviews; AP009380_GR; PGN_0624. DR KEGG; pgn:PGN_0624; -. DR HOGENOM; HBG708263; -. DR OMA; LRQGKGQ; -. DR ProtClustDB; PRK00108; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-trans...; IEA:HAMAP. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007047; P:cellular cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00038; MraY; 1; -. DR InterPro; IPR000715; Glycosyl_transferase_4. DR InterPro; IPR018481; Glycosyl_Trfase_4_cons-reg. DR InterPro; IPR003524; PNAcMuramoyl-5peptid_Trfase. DR InterPro; IPR018480; PNAcMuramoyl-5peptid_Trfase_CS. DR PANTHER; PTHR22926; Glyco_trans_4; 1. DR PANTHER; PTHR22926:SF3; PNAcPpept_trans; 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; KW Cell shape; Cell wall biogenesis/degradation; Complete proteome; KW Membrane; Peptidoglycan synthesis; Transferase; Transmembrane. FT CHAIN 1 419 Phospho-N-acetylmuramoyl-pentapeptide- FT transferase. FT /FTId=PRO_1000090656. FT TRANSMEM 22 42 Helical; (Potential). FT TRANSMEM 72 92 Helical; (Potential). FT TRANSMEM 99 119 Helical; (Potential). FT TRANSMEM 135 155 Helical; (Potential). FT TRANSMEM 208 228 Helical; (Potential). FT TRANSMEM 238 258 Helical; (Potential). FT TRANSMEM 278 298 Helical; (Potential). FT TRANSMEM 303 323 Helical; (Potential). FT TRANSMEM 328 348 Helical; (Potential). FT TRANSMEM 396 416 Helical; (Potential). 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 //