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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)

 U6RXW5_ENTFL            Unreviewed;       516 AA.
U6RXW5;
22-JAN-2014, integrated into UniProtKB/TrEMBL.
22-JAN-2014, sequence version 1.
28-MAR-2018, entry version 29.
RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase {ECO:0000256|HAMAP-Rule:MF_00208};
EC=6.3.2.7 {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=L-lysine-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=UDP-MurNAc-L-Ala-D-Glu:L-Lys ligase {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208};
Name=murE {ECO:0000256|HAMAP-Rule:MF_00208};
ORFNames=D350_02413 {ECO:0000313|EMBL:EPI27903.1};
Enterococcus faecalis VC1B-1.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
Enterococcus.
NCBI_TaxID=1244143 {ECO:0000313|EMBL:EPI27903.1, ECO:0000313|Proteomes:UP000017833};
[1] {ECO:0000313|EMBL:EPI27903.1, ECO:0000313|Proteomes:UP000017833}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=VC1B-1 {ECO:0000313|EMBL:EPI27903.1,
ECO:0000313|Proteomes:UP000017833};
Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R.,
Courtney L., Fronick C., O'Laughlin M., Godfrey J., Wilson R.M.,
Miner T., Farmer C., Delehaunty K., Cordes M., Minx P., Tomlinson C.,
Chen J., Wollam A., Pepin K.H., Bhonagiri V., Zhang X., Warren W.,
Mitreva M., Mardis E.R., Wilson R.K.;
Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
-!- 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:0000256|HAMAP-Rule:MF_00208}.
-!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-D-
glutamate + L-lysine = ADP + phosphate + UDP-N-acetylmuramoyl-L-
alanyl-D-glutamyl-L-lysine. {ECO:0000256|HAMAP-Rule:MF_00208}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_00208};
-!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
{ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|RuleBase:RU004135}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135}.
-!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
consequently, for the gamma-phosphate positioning of ATP.
{ECO:0000256|HAMAP-Rule:MF_00208}.
-!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
{ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00569976}.
-!- CAUTION: Lacks conserved residue(s) required for the propagation
of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EPI27903.1}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; ATIZ01000070; EPI27903.1; -; Genomic_DNA.
EnsemblBacteria; EPI27903; EPI27903; D350_02413.
PATRIC; fig|1244143.4.peg.2275; -.
UniPathway; UPA00219; -.
Proteomes; UP000017833; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0047482; F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity; IEA:UniProtKB-UniRule.
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-UniRule.
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 {ECO:0000256|HAMAP-Rule:MF_00208};
Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135};
Cell division {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135};
Cell shape {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135};
Complete proteome {ECO:0000313|Proteomes:UP000017833};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208};
Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000313|EMBL:EPI27903.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135}.
DOMAIN 131 337 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
DOMAIN 357 442 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
NP_BIND 132 138 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
REGION 176 177 UDP-MurNAc-L-Ala-D-Glu binding.
{ECO:0000256|HAMAP-Rule:MF_00208}.
MOTIF 433 436 L-lysine recognition motif.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 55 55 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 203 203 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 211 211 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
MOD_RES 245 245 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_00208}.
SEQUENCE 516 AA; 56878 MW; 0C4F3100252EB020 CRC64;
MKRLEAKKVT ISLFAIRDCL EKEDLLKEFI SPEGWHLTLS DTLGQREVTA LSYDSRDVTA
ETLFFCKGLN FKEIYLENAV KDGLEIYVSE VPYEVPAQLG IIVTDIKKAM AVLSMAFYDY
PQNKLKLIGF TGTKGKTTAA YFTKYILDVA TQQKTALLST MNSTLDGKTF FKSALTTPES
LDLYRMMATA VANGMTHFIM EVSSQAYKTN RVYKLFFDVG IFLNITPDHI SPIEHPTFDD
YFYCKRQLIT HSKVIVLNHE ADYFPLLKET AQQQKVPAIV YGSQPAPEVD YSFAVSSEDS
LRFIVESPAD ALGLAGSYHL RLGGDFNKGN ALSAAIASVL VGASKEECQQ GIAATTVPGR
MESLTNTNGA TVYVDYAHNY DSLKNLLTFV REEHPDGRLI VLVGSTGDKA ISRRKDFGRV
LSELADVAVL TTDDPASEDP AKICQEIQAH ITKEMPVYTI LDRGEAIAHA LSLSTTADDA
IVLAGKGADL YQKVNGVDEP YAGDFALAEA FINKKN


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