MRAY_CUTAK
ID MRAY_CUTAK Reviewed; 356 AA.
AC Q6A9Q5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 119.
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=PPA0755;
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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; AE017283; AAT82511.1; -; Genomic_DNA.
DR RefSeq; WP_002513927.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6A9Q5; -.
DR SMR; Q6A9Q5; -.
DR STRING; 267747.PPA0755; -.
DR EnsemblBacteria; AAT82511; AAT82511; PPA0755.
DR KEGG; pac:PPA0755; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_0_1_11; -.
DR OMA; LMSPLHH; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000603; Chromosome.
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 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..356
FT /note="Phospho-N-acetylmuramoyl-pentapeptide-transferase"
FT /id="PRO_0000108867"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 53..73
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 116..136
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 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 278..298
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
FT TRANSMEM 333..353
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00038"
SQ SEQUENCE 356 AA; 38314 MW; 1F263D510C2167FB CRC64;
MKNILLAGAV SMIGTLVGTR WFIHWLAAKG YGQFIRDDGP TTHKTKKGTP TMGGAVIIVS
VLLAYLVAHL VTWTHPSISA LLVLWLFSGL GFIGFLDDWT KISKQRSLGL KPKGKLLGQA
FVAITFAIGV MYFPDVHGVT PGSPAISFLR DISWLYLPVW LGIVWVILLI AGSSNAVNLT
DGLDGLATGA STMVFGAYTV LSIWQFNQWC SRPTTAGNHC YAVRDPHDIA VVAIAIAGAC
FGFLWWNAKP AQIFLGDTGS LALGGAVAGM AVVSRTELLL VIIGALFVIE TVSVMLQVSV
FKITGGKRVF KMAPLHHHFE LKGWAEVTVV IRFWIICGLA VSAGLGIFYA EWVAGQ
