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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)

 H8E2R3_9MICO            Unreviewed;       548 AA.
H8E2R3;
16-MAY-2012, integrated into UniProtKB/TrEMBL.
16-MAY-2012, sequence version 1.
16-JAN-2019, entry version 43.
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=OR221_1141 {ECO:0000313|EMBL:EIC08793.1};
Microbacterium laevaniformans OR221.
Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae;
Microbacterium.
NCBI_TaxID=1160710 {ECO:0000313|EMBL:EIC08793.1, ECO:0000313|Proteomes:UP000004547};
[1] {ECO:0000313|EMBL:EIC08793.1, ECO:0000313|Proteomes:UP000004547}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=OR221 {ECO:0000313|EMBL:EIC08793.1,
ECO:0000313|Proteomes:UP000004547};
PubMed=22628508; DOI=10.1128/JB.00474-12;
Brown S.D., Palumbo A.V., Panikov N., Ariyawansa T., Klingeman D.M.,
Johnson C.M., Land M.L., Utturkar S.M., Epstein S.S.;
"Draft Genome Sequence for Microbacterium laevaniformans Strain OR221,
a Bacterium Tolerant to Metals, Nitrate, and Low pH.";
J. Bacteriol. 194:3279-3280(2012).
-!- 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:
Reaction=ATP + L-lysine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-
D-glutamate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-
muramoyl-L-alanyl-gamma-D-glutamyl-L-lysine;
Xref=Rhea:RHEA:17969, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:32551, ChEBI:CHEBI:43474, ChEBI:CHEBI:83900,
ChEBI:CHEBI:83903, ChEBI:CHEBI:456216; EC=6.3.2.7;
Evidence={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,
ECO:0000256|SAAS:SAAS00951514}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951526}.
-!- 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:EIC08793.1}.
-----------------------------------------------------------------------
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EMBL; AJGR01000115; EIC08793.1; -; Genomic_DNA.
EnsemblBacteria; EIC08793; EIC08793; OR221_1141.
PATRIC; fig|1160710.3.peg.689; -.
UniPathway; UPA00219; -.
Proteomes; UP000004547; 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; IPR000713; Mur_ligase_N.
InterPro; IPR035911; MurE/MurF_N.
InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
Pfam; PF01225; Mur_ligase; 1.
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,
ECO:0000256|SAAS:SAAS00951530};
Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951537};
Cell division {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951537};
Cell shape {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951548};
Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951523};
Complete proteome {ECO:0000313|Proteomes:UP000004547};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|SAAS:SAAS00951519};
Ligase {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|SAAS:SAAS00951534, ECO:0000313|EMBL:EIC08793.1};
Magnesium {ECO:0000256|HAMAP-Rule:MF_00208};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|SAAS:SAAS00951530};
Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208,
ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951548};
Reference proteome {ECO:0000313|Proteomes:UP000004547}.
DOMAIN 77 157 Mur_ligase. {ECO:0000259|Pfam:PF01225}.
DOMAIN 169 367 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}.
DOMAIN 388 471 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}.
NP_BIND 171 177 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}.
REGION 211 212 UDP-MurNAc-L-Ala-D-Glu binding.
{ECO:0000256|HAMAP-Rule:MF_00208}.
MOTIF 463 466 L-lysine recognition motif.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 81 81 UDP-MurNAc-L-Ala-D-Glu; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_00208}.
BINDING 83 83 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 238 238 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
BINDING 246 246 UDP-MurNAc-L-Ala-D-Glu.
{ECO:0000256|HAMAP-Rule:MF_00208}.
MOD_RES 278 278 N6-carboxylysine. {ECO:0000256|HAMAP-
Rule:MF_00208}.
SEQUENCE 548 AA; 58036 MW; 8969DB47F44BACBD CRC64;
MAREVGLCTA MLTVVFPGVC YRRRVSIEQS SPSDPSELET GAAQRAANRP QKVISRSLAD
IADQVDATSV LGDAFVTGIA LSTASTQPGD LFFAQPGARD HGAHYLADAV RAGAVAVLTD
AAGADIIDVT PGVSALPRIV VDGHPRRVLG GLAAWFYDQP ARALKTIGIT GTQGKTSTTY
LVDAARQSRH TGVIGSMGTR IDGVAVPSTL TTPEAPQMHA LMALMRERGV EVVTSEVSSH
AITMGRVEGL RFDVGIFLNL GHDHRDFHGT QQAYLLAKRQ LLTPAMSAVA LVNVDDGAGR
RLHADAELNT QSFSVTGRDA DWRAVDIDLR LDGSSFRVIG PDGQTARFTT PLVGEFNVSN
ILAAVAALDI VGHPLAASVA GISSFAGVEG RVQFVPVDAE FQVVIDAGHK PEAINALLRA
MRPLTPGRII TVIGSNGNRD AHKRPLMGRF SAMASDIVIV TDDNPADEDP ETIRRAVVAG
TRGSRAEVFD VGGRAEAIHK AVELAREGDL IAIVGKGDER HQIMRDGVIV PHSDPDEVEW
ALRQRAGS


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