MURE_STRPN
ID MURE_STRPN Reviewed; 481 AA.
AC Q97PS1;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase;
DE EC=6.3.2.7;
DE AltName: Full=L-lysine-adding enzyme;
DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase;
DE AltName: Full=UDP-MurNAc-tripeptide synthetase;
DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase;
GN Name=murE; OrderedLocusNames=SP_1530;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP FUNCTION, AND CRYSTALLIZATION.
RC STRAIN=110K/70;
RX PubMed=14747725; DOI=10.1107/s0907444903027720;
RA Blewett A.M., Lloyd A.J., Echalier A., Fueloep V., Dowson C.G.,
RA Bugg T.D.H., Roper D.I.;
RT "Expression, purification, crystallization and preliminary characterization
RT of uridine 5'-diphospho-N-acetylmuramoyl L-alanyl-D-glutamate:lysine ligase
RT (MurE) from Streptococcus pneumoniae 110K/70.";
RL Acta Crystallogr. D 60:359-361(2004).
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.
CC {ECO:0000269|PubMed:14747725}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-lysine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-
CC alanyl-gamma-D-glutamyl-L-lysine; 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;
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and,
CC consequently, for the gamma-phosphate positioning of ATP.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC {ECO:0000305}.
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DR EMBL; AE005672; AAK75619.1; -; Genomic_DNA.
DR PIR; B95178; B95178.
DR RefSeq; WP_000590301.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97PS1; -.
DR SMR; Q97PS1; -.
DR STRING; 170187.SP_1530; -.
DR EnsemblBacteria; AAK75619; AAK75619; SP_1530.
DR KEGG; spn:SP_1530; -.
DR eggNOG; COG0769; Bacteria.
DR OMA; CFMEVSS; -.
DR PhylomeDB; Q97PS1; -.
DR BioCyc; SPNE170187:G1FZB-1548-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000585; Chromosome.
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: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 Gene3D; 3.40.1190.10; -; 1.
DR Gene3D; 3.90.190.20; -; 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 Pfam; PF02875; Mur_ligase_C; 1.
DR Pfam; PF08245; Mur_ligase_M; 1.
DR SUPFAM; SSF53244; SSF53244; 1.
DR SUPFAM; SSF53623; SSF53623; 1.
DR SUPFAM; SSF63418; SSF63418; 1.
DR TIGRFAMs; TIGR01085; murE; 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..481
FT /note="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine
FT ligase"
FT /id="PRO_0000101953"
FT MOTIF 404..407
FT /note="L-lysine recognition motif"
FT BINDING 42
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000250"
FT BINDING 118..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 160..161
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000250"
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:0000250"
FT BINDING 195
FT /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT glutamate"
FT /ligand_id="ChEBI:CHEBI:83900"
FT /evidence="ECO:0000250"
FT MOD_RES 229
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 481 AA; 53731 MW; E4374546215FBE97 CRC64;
MIKIETVLDI LKKDGLFREI IDQGHYHYNY SKVIFDSISY DSRKVTEDTL FFAKGAAFKK
EYLLSAITQG LAWYVAEKDY EVGIPVIIVN DIKKAMSLIA MEFYGNPQEK LKLLAFTGTK
GKTTAAYFAY NILSQGHRPA MLSTMNTTLD GETFFKSALT TPESIDLFDM MNQAVQNDRT
HLIMEVSSQA YLVKRVYGLT FDVGVFLNIS PDHIGPIEHP SFEDYFYHKR LLMEKSRAVI
INSDMDHFSV LKEQVEDQDH DFYGSQFDNQ IENSKAFSFS ATGKLAGDYD IQLIGNFNQE
NAVAAGLACL RLGASLEDIK KGIAATRVPG RMEVLTQKNG AKVFIDYAHN GDSLKKLINV
VETHQTGKIA LVLGSTGNKG ESRRKDFGLL LNQHPEIQVF LTADDPNYED PMAIADEISS
YINHPVEKIA DRQEAIKAAM AITNHELDAV IIAGKGADCY QIIQGKKESY PGDTAVAENY
L
