ID   MURE_TRIV2              Reviewed;         496 AA.
AC   Q3ME15;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_00208};
DE            EC=6.3.2.13 {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=Meso-A2pm-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=Meso-diaminopimelate-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase {ECO:0000255|HAMAP-Rule:MF_00208};
GN   Name=murE {ECO:0000255|HAMAP-Rule:MF_00208};
GN   OrderedLocusNames=Ava_1147;
OS   Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29413 / PCC 7937;
RX   PubMed=25197444; DOI=10.4056/sigs.3899418;
RA   Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA   Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT   "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL   Stand. Genomic Sci. 9:562-573(2014).
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:0000255|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:0000255|HAMAP-Rule:MF_00208};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00208};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- PTM: Carboxylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurE subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00208}.
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DR   EMBL; CP000117; ABA20771.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3ME15; -.
DR   SMR; Q3ME15; -.
DR   STRING; 240292.Ava_1147; -.
DR   KEGG; ava:Ava_1147; -.
DR   eggNOG; COG0769; Bacteria.
DR   HOGENOM; CLU_022291_4_1_3; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002533; Chromosome.
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; 3.90.190.20; Mur ligase, C-terminal domain; 1.
DR   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   Gene3D; 3.40.1390.10; MurE/MurF, N-terminal domain; 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   NCBIfam; TIGR01085; murE; 1.
DR   PANTHER; PTHR23135; MUR LIGASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR23135:SF4; UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   SUPFAM; SSF53244; MurD-like peptide ligases, peptide-binding domain; 1.
DR   SUPFAM; SSF63418; MurE/MurF N-terminal domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Magnesium;
KW   Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN           1..496
FT                   /note="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-
FT                   diaminopimelate ligase"
FT                   /id="PRO_1000012335"
FT   MOTIF           413..416
FT                   /note="Meso-diaminopimelate recognition motif"
FT   BINDING         32
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         116..122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         158..159
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         185
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         191
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         193
FT                   /ligand="UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
FT                   glutamate"
FT                   /ligand_id="ChEBI:CHEBI:83900"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         389
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         413..416
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         464
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         468
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   MOD_RES         225
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
SQ   SEQUENCE   496 AA;  53416 MW;  DCDF7907B96B79BA CRC64;
     MKLRELLATV DSVENLPPVL ADTEVKGIKT NSHACGAGDL FIGMPGTRVD GGEFWPSAIA
     SGAIAAIVSP QAVEKNPPSD EAVVISSNNM TKACAAIAAA FYGYPGQKLK LVGVTGTNGK
     TTTTHLIEFF LTKAQLSTAL MGTLYTRWPG FEQTATHTTP FAVELQQQLA QAVNAGCEFG
     VMEVSSHALA QGRVLGCPFE VGVFSNLTQD HLDYHSDMED YFAAKALLFS PDYLKGRAII
     NADDTYGQRL IKALSPEKVW SYSVNDSSAD LWMSDLSYEP NGVTGTIHTP EGDVSFRSPL
     VGQYNLENLL ASVGAVLHLG LDLQLIANAI PEFPGVPGRM ERVQINPDQD ISVIVDYAHT
     PDSLENLLKA ARPFIPGRMI CVFGCGGDRD RTKRPKMGKI AAELADLAFV TSDNPRTEDP
     EKILDDILAG IPDTVQPTVI GDRAIAIRTA ILQAQPGDGV LLAGKGHEDY QILGTEKIHF
     DDREHARAAL TEREKL
//