MRAY_THEFY
ID MRAY_THEFY Reviewed; 351 AA.
AC Q47QX2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 114.
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=Tfu_1107;
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX;
RX PubMed=17209016; DOI=10.1128/jb.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M., DiBartolo G.,
RA Martinez M., Lapidus A., Lucas S., Copeland A., Richardson P., Wilson D.B.,
RA Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00038};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00038}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. MraY
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00038}.
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DR EMBL; CP000088; AAZ55145.1; -; Genomic_DNA.
DR RefSeq; WP_011291554.1; NC_007333.1.
DR AlphaFoldDB; Q47QX2; -.
DR SMR; Q47QX2; -.
DR STRING; 269800.Tfu_1107; -.
DR EnsemblBacteria; AAZ55145; AAZ55145; Tfu_1107.
DR KEGG; tfu:Tfu_1107; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_0_1_11; -.
DR OMA; LMSPLHH; -.
DR OrthoDB; 1151822at2; -.
DR UniPathway; UPA00219; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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 3: Inferred from homology;
KW Cell cycle; Cell division; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Magnesium; Membrane; Metal-binding;
KW Peptidoglycan synthesis; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..351
FT /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase"
FT /id="PRO_0000235496"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 76..96
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
SQ SEQUENCE 351 AA; 37730 MW; 163C554072956CC6 CRC64;
MTGIIAAAGI SLLVSFLLLP PLIRILYRFK FGQEIRDDGP QGHKTKQGTP TMGGIAIIFG
TVVGYFGAHA VTMTPPTVSG VLVILLFVGL GCVGFLDDFI KIYKRRSLGL RSGAKMLGQI
IVGVGFAIGV TMFPNSYTYT PGSTHLSLLR DFGPPMAVWL FVIWALLLIV ATSNAVNLTD
GLDGLATGAT ILSLVAYVII GNWQLRQSCI NALEPNCYTV RDPLDLAVVA AAALGGCIAF
LWFNAPPAKI FMGDTGSLAL GGLLVGLAIT TRTQLLLLVI GGLFVLITAS VIIQVGSFRL
TGKRVFRMAP LQHHFELKGW AETTIVIRFW IIQGLFVAAA MALFYLEWMP R
