ID   MURE_STAAN              Reviewed;         494 AA.
AC   P65480; Q99V74;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 121.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase {ECO:0000255|HAMAP-Rule:MF_00208};
DE            EC=6.3.2.7 {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=L-lysine-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
GN   Name=murE {ECO:0000255|HAMAP-Rule:MF_00208}; OrderedLocusNames=SA0876;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the addition of L-lysine to the nucleotide
CC       precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the
CC       biosynthesis of bacterial cell-wall peptidoglycan. {ECO:0000255|HAMAP-
CC       Rule:MF_00208}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + L-lysine
CC         + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-L-
CC         lysine + ADP + phosphate + H(+); Xref=Rhea:RHEA:17969,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83900, ChEBI:CHEBI:83903,
CC         ChEBI:CHEBI:456216; EC=6.3.2.7; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00208};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
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DR   EMBL; BA000018; BAB42117.1; -; Genomic_DNA.
DR   PIR; B89870; B89870.
DR   RefSeq; WP_000340119.1; NC_002745.2.
DR   AlphaFoldDB; P65480; -.
DR   SMR; P65480; -.
DR   EnsemblBacteria; BAB42117; BAB42117; BAB42117.
DR   KEGG; sau:SA0876; -.
DR   HOGENOM; CLU_022291_0_1_9; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0047482; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051301; P:cell division; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR   Gene3D; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 1.
DR   HAMAP; MF_00208; MurE; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR035911; MurE/MurF_N.
DR   InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR   NCBIfam; TIGR01085; murE; 1.
DR   NCBIfam; NF001126; PRK00139.1-4; 1.
DR   NCBIfam; NF010628; PRK14022.1; 1.
DR   PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..494
FT                   /note="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine
FT                   ligase"
FT                   /id="PRO_0000101942"
FT   MOTIF           406..409
FT                   /note="L-lysine recognition motif"
FT   BINDING         30
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         110..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         152..153
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         179
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         187
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   MOD_RES         219
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
SQ   SEQUENCE   494 AA;  54233 MW;  B5BD224B23DA5A13 CRC64;
     MDASTLFKKV KVKRVLGSLE QQIDDITTDS RTAREGSIFV ASVGYTVDSH KFCQNVADQG
     CKLVVVNKEQ SLPANVTQVV VPDTLRVASI LAHTLYDYPS HQLVTFGVTG TNGKTSIATM
     IHLIQRKLQK NSAYLGTNGF QINETKTKGA NTTPETVSLT KKIKEAVDAG AESMTLEVSS
     HGLVLGRLRG VEFDVAIFSN LTQDHLDFHG TMEAYGHAKS LLFSQLGEDL SKEKYVVLNN
     DDSFSEYLRT VTPYEVFSYG IDEEAQFMAK NIQESLQGVS FDFVTPFGTY PVKSPYVGKF
     NISNIMAAMI AVWSKGTSLE TIIKAVENLE PVEGRLEVLD PSLPIDLIID YAHTADGMNK
     LIDAVQPFVK QKLIFLVGMA GERDLTKTPE MGRVACRADY VIFTPDNPAN DDPKMLTAEL
     AKGATHQNYI EFDDRAEGIK HAIDIAEPGD TVVLASKGRE PYQIMPGHIK VPHRDDLIGL
     EAAYKKFGGG PVDQ
//