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UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase (EC 6.3.2.7) (L-lysine-adding enzyme) (UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase) (UDP-MurNAc-tripeptide synthetase) (UDP-N-acetylmuramyl-tripeptide synthetase)

 MURE_STRP2              Reviewed;         481 AA.
Q04JL8;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
14-NOV-2006, sequence version 1.
23-MAY-2018, entry version 79.
RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase {ECO:0000255|HAMAP-Rule:MF_00208};
EC=6.3.2.7 {ECO:0000255|HAMAP-Rule:MF_00208};
AltName: Full=L-lysine-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208};
AltName: Full=UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase {ECO:0000255|HAMAP-Rule:MF_00208};
AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
Name=murE {ECO:0000255|HAMAP-Rule:MF_00208};
OrderedLocusNames=SPD_1359;
Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
Streptococcus.
NCBI_TaxID=373153;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=D39 / NCTC 7466;
PubMed=17041037; DOI=10.1128/JB.01148-06;
Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M.,
Davidsen T.M., Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
"Genome sequence of Avery's virulent serotype 2 strain D39 of
Streptococcus pneumoniae and comparison with that of unencapsulated
laboratory strain R6.";
J. Bacteriol. 189:38-51(2007).
-!- FUNCTION: Catalyzes the addition of L-lysine to the nucleotide
precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the
biosynthesis of bacterial cell-wall peptidoglycan.
{ECO:0000255|HAMAP-Rule:MF_00208}.
-!- CATALYTIC ACTIVITY: ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-
D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetyl-alpha-D-
muramoyl-L-alanyl-gamma-D-glutamyl-L-lysine. {ECO:0000255|HAMAP-
Rule:MF_00208}.
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
{ECO:0000255|HAMAP-Rule:MF_00208}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00208}.
-!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
consequently, for the gamma-phosphate positioning of ATP.
{ECO:0000255|HAMAP-Rule:MF_00208}.
-!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
{ECO:0000255|HAMAP-Rule:MF_00208}.
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EMBL; CP000410; ABJ54578.1; -; Genomic_DNA.
RefSeq; WP_000590294.1; NC_008533.1.
ProteinModelPortal; Q04JL8; -.
STRING; 373153.SPD_1359; -.
PRIDE; Q04JL8; -.
EnsemblBacteria; ABJ54578; ABJ54578; SPD_1359.
KEGG; spd:SPD_1359; -.
eggNOG; ENOG4107EEN; Bacteria.
eggNOG; COG0769; LUCA.
HOGENOM; HOG000268121; -.
KO; K05362; -.
OMA; CFMEVSS; -.
UniPathway; UPA00219; -.
Proteomes; UP000001452; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0047482; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity; IEA:UniProtKB-EC.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
Gene3D; 3.40.1190.10; -; 1.
Gene3D; 3.90.190.20; -; 1.
HAMAP; MF_00208; MurE; 1.
InterPro; IPR036565; Mur-like_cat_sf.
InterPro; IPR004101; Mur_ligase_C.
InterPro; IPR036615; Mur_ligase_C_dom_sf.
InterPro; IPR013221; Mur_ligase_cen.
InterPro; IPR035911; MurE/MurF_N.
InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
Pfam; PF02875; Mur_ligase_C; 1.
Pfam; PF08245; Mur_ligase_M; 1.
SUPFAM; SSF53244; SSF53244; 1.
SUPFAM; SSF53623; SSF53623; 1.
SUPFAM; SSF63418; SSF63418; 1.
TIGRFAMs; TIGR01085; murE; 1.
3: Inferred from homology;
ATP-binding; Cell cycle; Cell division; Cell shape;
Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
Ligase; Nucleotide-binding; Peptidoglycan synthesis.
CHAIN 1 481 UDP-N-acetylmuramoyl-L-alanyl-D-
glutamate--L-lysine ligase.
/FTId=PRO_1000012386.
NP_BIND 118 124 ATP. {ECO:0000255|HAMAP-Rule:MF_00208}.
REGION 160 161 UDP-MurNAc-L-Ala-D-Glu binding.
{ECO:0000255|HAMAP-Rule:MF_00208}.
MOTIF 404 407 L-lysine recognition motif.
BINDING 42 42 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000255|HAMAP-Rule:MF_00208}.
BINDING 187 187 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000255|HAMAP-Rule:MF_00208}.
BINDING 195 195 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000255|HAMAP-Rule:MF_00208}.
MOD_RES 229 229 N6-carboxylysine. {ECO:0000255|HAMAP-
Rule:MF_00208}.
SEQUENCE 481 AA; 53828 MW; 9A668127E05341E5 CRC64;
MIKIETVLDI LKKDGLFREI IDQGHYHYNY SKVIFDSISY DSRKVTEDTL FFAKGAAFKK
EYLLSAITQG LAWYVAEKDY EVDIPVIIVN DIKKAMSLIA MEFYGNPQEK LKLLAFTGTK
GKTTATYFAY NILSQGHRPA MLSTMNTTLD GETFFKSALT TPESIDLFDM MNQAVQNDRT
HLIMEVSSQA YLVHRVYGLT FDVGVFLNIT PDHIGPIEHP SFEDYFYHKR LLMENSRAVI
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


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