ID A0A417HSY0_9CLOT Unreviewed; 477 AA. AC A0A417HSY0; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 03-JUL-2019, entry version 3. 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=DW742_07290 {ECO:0000313|EMBL:RHT76235.1}; OS Butyricicoccus sp. AM28-25. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae; OC Butyricicoccus. OX NCBI_TaxID=2292294 {ECO:0000313|EMBL:RHT76235.1, ECO:0000313|Proteomes:UP000283242}; RN [1] {ECO:0000313|EMBL:RHT76235.1, ECO:0000313|Proteomes:UP000283242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AM28-25 {ECO:0000313|EMBL:RHT76235.1, RC ECO:0000313|Proteomes:UP000283242}; RA Zou Y., Xue W., Luo G.; RT "A genome reference for cultivated species of the human gut RT microbiota."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to CC the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate CC (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. CC {ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + meso-2,6-diaminopimelate + 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- CC diaminopimelate; 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; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00208}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|RuleBase:RU004135, CC ECO:0000256|SAAS:SAAS00031714}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208, CC ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00354145}. CC -!- PTM: Carbamoylation 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|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00569976}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00208}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:RHT76235.1}. 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; QUJL01000006; RHT76235.1; -; Genomic_DNA. DR UniPathway; UPA00219; -. DR Proteomes; UP000283242; 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|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00431804}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00031739}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00431829}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00431889}; KW Complete proteome {ECO:0000313|Proteomes:UP000283242}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|SAAS:SAAS00431837}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000313|EMBL:RHT76235.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00208}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00431817}. FT DOMAIN 23 91 Mur_ligase. {ECO:0000259|Pfam:PF01225}. FT DOMAIN 105 302 Mur_ligase_M. {ECO:0000259|Pfam:PF08245}. FT DOMAIN 323 409 Mur_ligase_C. {ECO:0000259|Pfam:PF02875}. FT NP_BIND 107 113 ATP. {ECO:0000256|HAMAP-Rule:MF_00208}. FT REGION 149 150 UDP-MurNAc-L-Ala-D-Glu binding. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT REGION 398 401 Meso-diaminopimelate binding. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT MOTIF 398 401 Meso-diaminopimelate recognition motif. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 30 30 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 176 176 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 184 184 UDP-MurNAc-L-Ala-D-Glu. FT {ECO:0000256|HAMAP-Rule:MF_00208}. FT BINDING 374 374 Meso-diaminopimelate. {ECO:0000256|HAMAP- FT Rule:MF_00208}. FT BINDING 450 450 Meso-diaminopimelate; via carbonyl FT oxygen. {ECO:0000256|HAMAP-Rule: FT MF_00208}. FT BINDING 454 454 Meso-diaminopimelate. {ECO:0000256|HAMAP- FT Rule:MF_00208}. FT MOD_RES 216 216 N6-carboxylysine. {ECO:0000256|HAMAP- FT Rule:MF_00208}. SQ SEQUENCE 477 AA; 51813 MW; 41048883E8BE34A1 CRC64; MKLQELLKNV AVKNSTAAQD IDIKEVRYDS RAVQPGDLFV AIRGYATDGH KYIAKAMEQG AAAVVCEEAP EGVPAVVVEN SRIALAEIAA NRFGHPAESM VMLGVTGTNG KTTTTYLVKH MLEDAGHKVG LIGTNQNLIG DEVIETERTT PESYELHALF ARMRDAGCTH VIMEVSSHSL VLDRVHGIPF AVGAFTNLTQ DHLDFHKTME EYRKAKALLF SISKKGVINL DDAAAEKMLA DAKCPCMTFS CGKPEADLEA TDLQLHADGV EFTAQYQGEK ADVKLPIPGH FSVENALTAL GIVLQLGMPL AAAAKSMATA TGVKGRVEVV PTDTDYTVLI DYAHSPDGVE NVLKAVRGFA KGRVVALFGC GGDRDRTKRP KMGKIAADLA DFCVVTSDNP RTEEPKAIID DILEGMKDSD TPMQVIVDRP EAIHWALAHA QKDDIIVLMG KGHETYQEVN HVKHHMDERE IVAEYFA //