MRAY_STAA8
ID MRAY_STAA8 Reviewed; 321 AA.
AC Q2FZ93; O07322; O24815; P68784;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 105.
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:0000269|PubMed:4208473};
DE AltName: Full=UDP-MurNAc-pentapeptide phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00038};
GN Name=mraY {ECO:0000255|HAMAP-Rule:MF_00038};
GN OrderedLocusNames=SAOUHSC_01146;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9287029; DOI=10.1128/jb.179.17.5632-5635.1997;
RA Pucci M.J., Thanassi J.A., Discotto L.F., Kessler R.E., Dougherty T.J.;
RT "Identification and characterization of cell wall-cell division gene
RT clusters in pathogenic Gram-positive cocci.";
RL J. Bacteriol. 179:5632-5635(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9573165; DOI=10.1128/jb.180.10.2759-2765.1998;
RA Wada A., Watanabe H.;
RT "Penicillin-binding protein 1 of Staphylococcus aureus is essential for
RT growth.";
RL J. Bacteriol. 180:2759-2765(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=4208473; DOI=10.1016/s0021-9258(19)42649-5;
RA Hammes W.P., Neuhaus F.C.;
RT "On the specificity of phospho-N-acetylmuramyl-pentapeptide translocase.
RT The peptide subunit of uridine diphosphate-N-actylmuramyl-pentapeptide.";
RL J. Biol. Chem. 249:3140-3150(1974).
RN [5]
RP TOPOLOGY, AND SUBCELLULAR LOCATION.
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).
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:4208473}.
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:0000255|HAMAP-
CC Rule:MF_00038, ECO:0000269|PubMed:4208473};
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 membrane {ECO:0000255|HAMAP-Rule:MF_00038,
CC ECO:0000269|PubMed:10564498}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00038, ECO:0000269|PubMed:10564498}.
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; U94706; AAC45625.1; -; Genomic_DNA.
DR EMBL; AB007500; BAA22555.1; -; Genomic_DNA.
DR EMBL; CP000253; ABD30256.1; -; Genomic_DNA.
DR RefSeq; WP_000578458.1; NZ_LS483365.1.
DR RefSeq; YP_499688.1; NC_007795.1.
DR AlphaFoldDB; Q2FZ93; -.
DR SMR; Q2FZ93; -.
DR STRING; 1280.SAXN108_1180; -.
DR EnsemblBacteria; ABD30256; ABD30256; SAOUHSC_01146.
DR GeneID; 3920706; -.
DR KEGG; sao:SAOUHSC_01146; -.
DR PATRIC; fig|93061.5.peg.1051; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_0_1_9; -.
DR OMA; LMSPLHH; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:Q2FZ93; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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 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 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..321
FT /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase"
FT /id="PRO_0000247938"
FT TRANSMEM 1..21
FT /note="Helical"
FT TOPO_DOM 22..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..69
FT /note="Helical"
FT TOPO_DOM 70..75
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..91
FT /note="Helical"
FT TOPO_DOM 92..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..133
FT /note="Helical"
FT TOPO_DOM 134..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..165
FT /note="Helical"
FT TOPO_DOM 166..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT TOPO_DOM 198..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..216
FT /note="Helical"
FT TOPO_DOM 217..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..246
FT /note="Helical"
FT TOPO_DOM 247..249
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..268
FT /note="Helical"
FT TOPO_DOM 269..300
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..320
FT /note="Helical"
FT TOPO_DOM 321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CONFLICT 104
FT /note="Q -> P (in Ref. 1; AAC45625)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="F -> I (in Ref. 1; AAC45625)"
FT /evidence="ECO:0000305"
FT CONFLICT 299..321
FT /note="KVVTVFWAVGLISGLIGLWIGVH -> ESTYSILGCWSDFRFNRFMDWSALR
FT CLIIQG (in Ref. 1; AAC45625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 321 AA; 35232 MW; 0A2F82D042255848 CRC64;
MIFVYALLAL VITFVLVPVL IPTLKRMKFG QSIREEGPQS HMKKTGTPTM GGLTFLLSIV
ITSLVAIIFV DQANPIILLL FVTIGFGLIG FIDDYIIVVK KNNQGLTSKQ KFLAQIGIAI
IFFVLSNVFH LVNFSTSIHI PFTNVAIPLS FAYVIFIVFW QVGFSNAVNL TDGLDGLATG
LSIIGFTMYA IMSFVLGETA IGIFCIIMLF ALLGFLPYNI NPAKVFMGDT GSLALGGIFA
TISIMLNQEL SLIFIGLVFV IETLSVMLQV ASFKLTGKRI FKMSPIHHHF ELIGWSEWKV
VTVFWAVGLI SGLIGLWIGV H
