ID I6SUM0_ENTHA Unreviewed; 320 AA.
AC I6SUM0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 60.
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 OrderedLocusNames=EHR_00390 {ECO:0000313|EMBL:AFM69072.1};
OS Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 /
OS NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=768486 {ECO:0000313|EMBL:AFM69072.1, ECO:0000313|Proteomes:UP000002895};
RN [1] {ECO:0000313|EMBL:AFM69072.1, ECO:0000313|Proteomes:UP000002895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB
RC 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R
RC {ECO:0000313|Proteomes:UP000002895};
RX PubMed=22933757; DOI=10.1128/JB.01075-12;
RA Gaechter T., Wunderlin C., Schmidheini T., Solioz M.;
RT "Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790,
RT a model organism for the study of ion transport, bioenergetics, and copper
RT homeostasis.";
RL J. Bacteriol. 194:5126-5127(2012).
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 ECO:0000256|PIRSR:PIRSR600715-1};
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}.
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DR EMBL; CP003504; AFM69072.1; -; Genomic_DNA.
DR RefSeq; WP_010719780.1; NZ_KB946233.1.
DR AlphaFoldDB; I6SUM0; -.
DR GeneID; 56788110; -.
DR KEGG; ehr:EHR_00390; -.
DR PATRIC; fig|768486.10.peg.2293; -.
DR eggNOG; COG0472; Bacteria.
DR HOGENOM; CLU_023982_0_1_9; -.
DR OrthoDB; 9805475at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002895; Chromosome.
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 NCBIfam; TIGR00445; mraY; 1.
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 PROSITE; PS01347; MRAY_1; 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|HAMAP-Rule:MF_00038};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00038, ECO:0000256|PIRSR:PIRSR600715-
KW 1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00038};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00038,
KW ECO:0000256|PIRSR:PIRSR600715-1};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00038};
KW Reference proteome {ECO:0000313|Proteomes:UP000002895};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 49..71
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 117..133
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 145..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..218
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 225..246
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 252..273
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT TRANSMEM 302..319
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00038"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR600715-1"
SQ SEQUENCE 320 AA; 35633 MW; BF0FC4A2D1C18321 CRC64;
MEWTQALIPI VSSCAMTIAA MPLFIGYFQM KKQGQAIREE GPKWHNVKAG TPTMGGLVFL
VAAILTGIWV GAWQNQLTPT LFILLFVLAL YGVIGFLDDF IKIFKKRNMG LNSKQKLLGQ
IIGGIIFYLV YRSEGYPGTL NFFGIELPLG LFYGVFAIFW LVGFSNAVNL TDGIDGLVAG
LGTISFATYG IIAWHQQQYD VLVICLSVLG GLLGFFAYNR KPAKIFMGDV GSLALGGLLA
AISIMLNQEW TLLLVGLIYV METASVMLQV TSFKLTGKRI FKMSPIHHHF EMCGWSEWKI
DIIFWLVSIV TSLITLWFIW
//
