ID A0A2C5PP38_9BACI Unreviewed; 497 AA. AC A0A2C5PP38; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 29-SEP-2021, entry version 17. 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=COI65_14725 {ECO:0000313|EMBL:PHG61055.1}; OS Bacillus wiedmannii. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=1890302 {ECO:0000313|EMBL:PHG61055.1, ECO:0000313|Proteomes:UP000222503}; RN [1] {ECO:0000313|EMBL:PHG61055.1, ECO:0000313|Proteomes:UP000222503} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AFS029838 {ECO:0000313|EMBL:PHG61055.1, RC ECO:0000313|Proteomes:UP000222503}; RG Agbiome Team Llc; RA Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S., RA Shank E.A., Bowers A.; RT "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved RT roles of natural products in bacterial physiology."; RL Submitted (SEP-2017) 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:PHG61055.1}. 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; NUUQ01000020; PHG61055.1; -; Genomic_DNA. DR EnsemblBacteria; PHG61055; PHG61055; COI65_14725. DR UniPathway; UPA00219; -. DR Proteomes; UP000222503; 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:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro. 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; IPR018109; Folylpolyglutamate_synth_CS. 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. DR PROSITE; PS01011; FOLYLPOLYGLU_SYNT_1; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00208}; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP- KW Rule:MF_00208}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP- KW Rule:MF_00208}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_00208}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00208}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00208}; KW 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}. FT DOMAIN 22..84 FT /note="Mur_ligase" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 109..315 FT /note="Mur_ligase_M" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 336..421 FT /note="Mur_ligase_C" FT /evidence="ECO:0000259|Pfam:PF02875" FT NP_BIND 111..117 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT REGION 410..413 FT /note="Meso-diaminopimelate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT MOTIF 410..413 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 180 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 188 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 386 FT /note="Meso-diaminopimelate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 463 FT /note="Meso-diaminopimelate; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 467 FT /note="Meso-diaminopimelate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT MOD_RES 220 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" SQ SEQUENCE 497 AA; 55273 MW; CBD1934CBB95531D CRC64; MKLKELANLF LIKETIGDMN VEITGLEMDS RKITSGNLFI CVSGIDGFLE DRHQFVEDAV KNGAVALIVE RDVNIEIPKI IVNDARYAMA VIALHFYGDP SNKMKLIGIT GTNGKTTTSY LLEKILTDYG FQTGLMGNNG VKVGSKWYPT DINTQEPPTL QRNLQMMKNQ NVDYCVMEVT SQGLHMERVK GCNFKTAVFT NLTQDHLDYH GTFQEYKHVK GLLFSRLGND FSTIDQKIAI LNADDPSVEY FKKVTSAEVI TYGIHNGADV QAKSITLSSK GIQFLVSSFN GEIEINLNLV GRFNVYNALA AITAALVEGI PLTNISDSLY NLKSIEGRME IIDENQDFLV IVDYAHTPDA LENVLSTISE FSKGKIITVF GCGGDRDAKK RSIMGGIAGS YSDFVFITSD NPRSEDPKAI IKDIEKGFSQ NNNLNYKIEV DRELAINHAI HMASTNDIVL IAGKGHETYQ ILKDSTIHFD DKEKARQAII NKMNEFN //