ID A0A5C7FBC6_9BACI Unreviewed; 490 AA. AC A0A5C7FBC6; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 11-DEC-2019, entry version 2. 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=FTX54_01565 {ECO:0000313|EMBL:TXF87433.1}; OS Alkalicoccus halolimnae. OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalicoccus. OX NCBI_TaxID=1667239 {ECO:0000313|EMBL:TXF87433.1, ECO:0000313|Proteomes:UP000321816}; RN [1] {ECO:0000313|EMBL:TXF87433.1, ECO:0000313|Proteomes:UP000321816} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BZ-SZ-XJ29 {ECO:0000313|EMBL:TXF87433.1, RC ECO:0000313|Proteomes:UP000321816}; RA Zhao B.; RT "Alkalicoccus halolimnae sp. nov., isolated from a salt lake close to RT Xinjiang Uyghur Autonomous Region of China."; RL Submitted (AUG-2019) 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-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; 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 ECO:0000256|SAAS:SAAS00951514}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208, CC ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951526}. 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|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00569976}. 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:TXF87433.1}. 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; VPFE01000001; TXF87433.1; -; Genomic_DNA. DR UniPathway; UPA00219; -. DR Proteomes; UP000321816; Unassembled WGS sequence. DR GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity; IEA:UniProtKB-EC. 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|HAMAP-Rule:MF_00208, KW ECO:0000256|SAAS:SAAS00951530}; KW Cell cycle {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00951553}; KW Cell division {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951537}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|RuleBase:RU004135, KW ECO:0000256|SAAS:SAAS00951545}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951523}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00951519}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00208, ECO:0000256|SAAS:SAAS00951534, KW ECO:0000313|EMBL:TXF87433.1}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00208}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|SAAS:SAAS00951542}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00208, KW ECO:0000256|RuleBase:RU004135, ECO:0000256|SAAS:SAAS00951548}. FT DOMAIN 25..96 FT /note="Mur_ligase" FT /evidence="ECO:0000259|Pfam:PF01225" FT DOMAIN 108..313 FT /note="Mur_ligase_M" FT /evidence="ECO:0000259|Pfam:PF08245" FT DOMAIN 334..420 FT /note="Mur_ligase_C" FT /evidence="ECO:0000259|Pfam:PF02875" FT NP_BIND 110..116 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT REGION 152..153 FT /note="UDP-MurNAc-L-Ala-D-Glu binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT REGION 409..412 FT /note="Meso-diaminopimelate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT COILED 159..179 FT /evidence="ECO:0000256|SAM:Coils" FT MOTIF 409..412 FT /note="Meso-diaminopimelate recognition motif" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 32 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 151 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 179 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 187 FT /note="UDP-MurNAc-L-Ala-D-Glu" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" FT BINDING 385 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 219 FT /note="N6-carboxylysine" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00208" SQ SEQUENCE 490 AA; 54358 MW; D8E2A6F40A2B97B0 CRC64; MMSLKEIVSL LPVCEVSGFE EKTIIETISM DSRLIEKKSL FFCVPGFTVD GHDFAQEAVE AGAAALVTDR PIQMSVPVIQ VPDVRRAMAL ISARFYEYPS QELKMIGVTG TNGKTSVTHF LEQMLELLEV ETGIIGTMYT KYAGKEISSN NTTPESIVLQ KILRDMRDAE TEAAAMEVSS HALSNGRIHG TRFDIAVYTN LSQDHLDYHA TMEDYARAKS LLFAQLGSGF VKERQPYSVI NVDDPYSEIM MEASAAPLIT YGLSKHAAVR AEEVELSGGR SNFYFCAPGI RDHVTLNLPG RFSIYNALAA ASALYAYGWR WQEIIPLIPL LKGVRGRFEP VFSSAPVHAL VDYAHTPDSL ENVLQTIKDA AEGKIITVIG CGGDRDRKKR PLMAAIAEKY SSFTYLTSDN PRTEKPEAII EEMKSGMSGI RYNVIVDREE AINEAVRKAK PGDVVLIAGK GHETYQEIGR DRIYFDDKKA AEKALKEWVE //