ID A0A063YWA7_9BACI Unreviewed; 489 AA. AC A0A063YWA7; DT 03-SEP-2014, integrated into UniProtKB/TrEMBL. DT 03-SEP-2014, sequence version 1. DT 10-FEB-2021, entry version 34. DE RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208}; DE EC=6.3.2.13 {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=Meso-A2pm-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208}; DE AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000256|HAMAP-Rule:MF_00208}; GN Name=murE {ECO:0000256|HAMAP-Rule:MF_00208}; GN ORFNames=DI44_05225 {ECO:0000313|EMBL:KDE49430.1}; OS Geobacillus sp. CAMR5420. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus; OC unclassified Geobacillus. OX NCBI_TaxID=1482739 {ECO:0000313|EMBL:KDE49430.1, ECO:0000313|Proteomes:UP000027227}; RN [1] {ECO:0000313|EMBL:KDE49430.1, ECO:0000313|Proteomes:UP000027227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CAMR5420 {ECO:0000313|EMBL:KDE49430.1, RC ECO:0000313|Proteomes:UP000027227}; RA De Maayer P., Willliamson C.E., Vennard C.T., Danson M.J., Cowan D.A.; RT "The draft genomes of Geobacillus sp. CAMR5420 and CAMR12739."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the CC nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) CC in the biosynthesis of bacterial cell-wall peptidoglycan. CC {ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + meso-2,6-diaminoheptanedioate + UDP-N-acetyl-alpha-D- CC muramoyl-L-alanyl-D-glutamate = ADP + H(+) + phosphate + UDP-N- CC acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6- CC diaminoheptanedioate; Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, CC ChEBI:CHEBI:83900, ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; CC EC=6.3.2.13; Evidence={ECO:0000256|HAMAP-Rule:MF_00208}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00208}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|RuleBase:RU004135}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208, CC ECO:0000256|RuleBase:RU004135}. CC -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and, CC consequently, for the gamma-phosphate positioning of ATP. CC {ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily. CC {ECO:0000256|ARBA:ARBA00005898, ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:KDE49430.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; JHUS01000029; KDE49430.1; -; Genomic_DNA. DR RefSeq; WP_014195372.1; NZ_JHUS01000029.1. DR EnsemblBacteria; KDE49430; KDE49430; DI44_05225. DR UniPathway; UPA00219; -. DR Proteomes; UP000027227; Unassembled WGS sequence. 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:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate 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; IPR000713; Mur_ligase_N. DR InterPro; IPR035911; MurE/MurF_N. DR InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase. DR Pfam; PF01225; Mur_ligase; 1. 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00208}; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP- KW Rule:MF_00208, ECO:0000256|RuleBase:RU004135}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|RuleBase:RU004135}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000313|EMBL:KDE49430.1}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00208}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00208, ECO:0000256|RuleBase:RU004135}. FT DOMAIN 25..94 FT /note="Mur_ligase" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 106..312 FT /note="Mur_ligase_M" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 332..417 FT /note="Mur_ligase_C" FT /evidence="ECO:0000259|Pfam:PF02875" FT NP_BIND 108..114 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT REGION 150..151 FT /note="UDP-MurNAc-L-Ala-D-Glu binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT REGION 407..410 FT /note="Meso-diaminopimelate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT MOTIF 407..410 FT /note="Meso-diaminopimelate recognition motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 30 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 149 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 177 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 183 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 185 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 383 FT /note="Meso-diaminopimelate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 459 FT /note="Meso-diaminopimelate; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 463 FT /note="Meso-diaminopimelate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT MOD_RES 217 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" SQ SEQUENCE 489 AA; 53350 MW; 8381F179FE07B341 CRC64; MKLLTLLSHL PGFWVHHGGN PDIVALEMDS RRVASGSLFF CLKGFTVDGH DFAEEAVARG AAAIVAERPL SVDVPVVLVS DSRRTMAILA DAFYGRPTHR LHLIGVTGTN GKTTTTSIIE QIARKAGKKT GLIGTVHIKV GDRSYPAANT TPESLILQRM FKQMVDEGVE FVAMEVSSHA LHQGRVHGCD YDVAVFTNLT QDHLDYHGTM EEYRNAKGLL FAQLGNRYDE RRPKFAVLNH DDPVSQYYKH MTAAPIVTYG MREKSDVMAE QIRMTAGGMA FRLCTPHGSA AVETKLVGSF NVYNILAAAA ACLASGFSLE TIAAALADVE PVPGRFETVD EGQNFTIIVD YAHTPDSLEN ALKTVRQLAK RNVYVVIGCG GDRDPSKRPL MAQVAVRYAD VAIFTSDNPR SEDPKQILRD MEAGVSAEIG KHVTIPDREE AIRYAIGQAQ EGDVVLIAGK GHETYQIIGN DVIEFDDRAV ARAAVKERG //