ID A0A6A1Z7X8_9LACO Unreviewed; 322 AA. AC A0A6A1Z7X8; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 22-FEB-2023, entry version 9. 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 ORFNames=F8251_02565 {ECO:0000313|EMBL:KAB1977720.1}; OS Lactobacillus crispatus. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=47770 {ECO:0000313|EMBL:KAB1977720.1, ECO:0000313|Proteomes:UP000430323}; RN [1] {ECO:0000313|EMBL:KAB1977720.1, ECO:0000313|Proteomes:UP000430323} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BIO6272 {ECO:0000313|EMBL:KAB1977720.1, RC ECO:0000313|Proteomes:UP000430323}; RA Jaomanjaka F., Blanc P.; RT "Investigation of probiotic properties of different lactic acid bacteria."; RL Submitted (SEP-2019) 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-L-lysyl-D-alanyl-D-alanine = CC Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis- CC undecaprenyl diphosphate + UMP; Xref=Rhea:RHEA:21920, CC ChEBI:CHEBI:57865, ChEBI:CHEBI:60032, ChEBI:CHEBI:60392, CC ChEBI:CHEBI:70758; EC=2.7.8.13; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00038}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00038}; 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}. 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:KAB1977720.1}. 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; WBOB01000007; KAB1977720.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6A1Z7X8; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000430323; Unassembled WGS sequence. 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 PANTHER; PTHR22926:SF5; PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE HOMOLOG; 1. DR Pfam; PF00953; Glycos_transf_4; 1. DR Pfam; PF10555; MraY_sig1; 1. DR TIGRFAMs; TIGR00445; mraY; 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|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00038}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00038}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00038}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00038}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00038}; 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..26 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038" FT TRANSMEM 54..75 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038" FT TRANSMEM 81..102 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038" FT TRANSMEM 114..133 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038" FT TRANSMEM 139..164 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038" FT TRANSMEM 176..195 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038" FT TRANSMEM 201..220 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038" FT TRANSMEM 227..248 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038" FT TRANSMEM 254..275 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038" FT TRANSMEM 304..321 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038" SQ SEQUENCE 322 AA; 35537 MW; 314CE03F01F59958 CRC64; MNMMLASCIA LVSSLVLTVI FIPLLIKFMR SHHEGQEIRD EGPKWHQKKS GTPTMGGTVF VIAAVISVIW VAAMQHSLNK VIWILVISLL GYGIIGFLDD GIKLYFKRNL GLRAWQKLAL QIIIAILIVL IATSDHFQFG LYIPFAGVVH SLVLFVAFII FWLVGFSNAV NLSDGLDGLA TGLSVVAYGT YAYIAFKQKN FAVLAFCMSV IGGLIAFFIF NHKPAKIFMG DAGSLALGGG LATISIMLNR PWSLLLVGIV FVCETASVIL QVISFQTTGK RIFKMTPIHH HFEMLGWSEW KVDIVFWLVG LIGSILYLVI WG //