MRAY_ECOLI
ID MRAY_ECOLI Reviewed; 360 AA.
AC P0A6W3; P15876;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 133.
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, ECO:0000305|PubMed:1846850, ECO:0000305|PubMed:215212};
DE AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00038};
GN Name=mraY {ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000303|PubMed:1846850};
GN Synonyms=murX; OrderedLocusNames=b0087, JW0085;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2179861; DOI=10.1093/nar/18.4.1058;
RA Ikeda M., Wachi M., Ishino F., Matsuhashi M.;
RT "Nucleotide sequence involving murD and an open reading frame ORF-Y spacing
RT murF and ftsW in Escherichia coli.";
RL Nucleic Acids Res. 18:1058-1058(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND PATHWAY.
RC STRAIN=K12;
RX PubMed=215212; DOI=10.1016/0005-2744(78)90355-8;
RA Geis A., Plapp R.;
RT "Phospho-N-acetylmuramoyl-pentapeptide-transferase of Escherichia coli K12.
RT Properties of the membrane-bound and the extracted and partially purified
RT enzyme.";
RL Biochim. Biophys. Acta 527:414-424(1978).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=1846850; DOI=10.1128/jb.173.3.1021-1026.1991;
RA Ikeda M., Wachi M., Jung H.K., Ishino F., Matsuhashi M.;
RT "The Escherichia coli mraY gene encoding UDP-N-acetylmuramoyl-pentapeptide:
RT undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide transferase.";
RL J. Bacteriol. 173:1021-1026(1991).
RN [7]
RP TOPOLOGY.
RX PubMed=10564498; DOI=10.1046/j.1365-2958.1999.01623.x;
RA Bouhss A., Mengin-Lecreulx D., Le Beller D., Van Heijenoort J.;
RT "Topological analysis of the mraY protein catalyzing the first membrane
RT step of peptidoglycan synthesis.";
RL Mol. Microbiol. 34:576-585(1999).
RN [8]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
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, ECO:0000269|PubMed:1846850,
CC ECO:0000269|PubMed:215212}.
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 ECO:0000305|PubMed:1846850, ECO:0000305|PubMed:215212};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00038,
CC ECO:0000269|PubMed:215212};
CC Note=Replacement of Mg(2+) by Mn(2+) restores only 10% of the activity.
CC {ECO:0000269|PubMed:215212};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000305|PubMed:215212}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00038, ECO:0000269|PubMed:15919996}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000305}.
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DR EMBL; X51584; CAA35932.1; -; Genomic_DNA.
DR EMBL; X55034; CAA38864.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73198.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96655.1; -; Genomic_DNA.
DR PIR; S08395; S08395.
DR RefSeq; NP_414629.1; NC_000913.3.
DR RefSeq; WP_000964131.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P0A6W3; -.
DR SMR; P0A6W3; -.
DR BioGRID; 4261478; 375.
DR STRING; 511145.b0087; -.
DR BindingDB; P0A6W3; -.
DR ChEMBL; CHEMBL3957; -.
DR SwissLipids; SLP:000001813; -.
DR TCDB; 9.B.146.1.6; the putative undecaprenyl-phosphate n-acetylglucosaminyl transferase (murg) family.
DR jPOST; P0A6W3; -.
DR PaxDb; P0A6W3; -.
DR PRIDE; P0A6W3; -.
DR EnsemblBacteria; AAC73198; AAC73198; b0087.
DR EnsemblBacteria; BAB96655; BAB96655; BAB96655.
DR GeneID; 66671623; -.
DR GeneID; 944814; -.
DR KEGG; ecj:JW0085; -.
DR KEGG; eco:b0087; -.
DR PATRIC; fig|1411691.4.peg.2193; -.
DR EchoBASE; EB0599; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_0_0_6; -.
DR InParanoid; P0A6W3; -.
DR OMA; LMSPLHH; -.
DR PhylomeDB; P0A6W3; -.
DR BioCyc; EcoCyc:PHOSNACMURPENTATRANS-MON; -.
DR BioCyc; MetaCyc:PHOSNACMURPENTATRANS-MON; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:P0A6W3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IDA:EcoliWiki.
DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IBA:GO_Central.
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:0044038; P:cell wall macromolecule biosynthetic process; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
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; PTHR22926; 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 1: Evidence at protein level;
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_0000108820"
FT TOPO_DOM 1..18
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10564498"
FT TRANSMEM 19..45
FT /note="Helical"
FT TOPO_DOM 46..76
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10564498"
FT TRANSMEM 77..90
FT /note="Helical"
FT TOPO_DOM 91..96
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10564498"
FT TRANSMEM 97..113
FT /note="Helical"
FT TOPO_DOM 114..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10564498"
FT TRANSMEM 134..156
FT /note="Helical"
FT TOPO_DOM 157..173
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10564498"
FT TRANSMEM 174..188
FT /note="Helical"
FT TOPO_DOM 189..199
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10564498"
FT TRANSMEM 200..220
FT /note="Helical"
FT TOPO_DOM 221..238
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10564498"
FT TRANSMEM 239..251
FT /note="Helical"
FT TOPO_DOM 252..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10564498"
FT TRANSMEM 271..284
FT /note="Helical"
FT TOPO_DOM 285..287
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10564498"
FT TRANSMEM 288..299
FT /note="Helical"
FT TOPO_DOM 300..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:10564498"
FT TRANSMEM 342..357
FT /note="Helical"
FT TOPO_DOM 358..360
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:10564498"
SQ SEQUENCE 360 AA; 39875 MW; F3550AFA3CD636AE CRC64;
MLVWLAEHLV KYYSGFNVFS YLTFRAIVSL LTALFISLWM GPRMIAHLQK LSFGQVVRND
GPESHFSKRG TPTMGGIMIL TAIVISVLLW AYPSNPYVWC VLVVLVGYGV IGFVDDYRKV
VRKDTKGLIA RWKYFWMSVI ALGVAFALYL AGKDTPATQL VVPFFKDVMP QLGLFYILLA
YFVIVGTGNA VNLTDGLDGL AIMPTVFVAG GFALVAWATG NMNFASYLHI PYLRHAGELV
IVCTAIVGAG LGFLWFNTYP AQVFMGDVGS LALGGALGII AVLLRQEFLL VIMGGVFVVE
TLSVILQVGS FKLRGQRIFR MAPIHHHYEL KGWPEPRVIV RFWIISLMLV LIGLATLKVR
