ID   MURE2_CLOAB             Reviewed;         483 AA.
AC   Q97FC1;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   02-SEP-2026, entry version 143.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=Meso-diaminopimelate-adding enzyme 2 {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase 2 {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00208};
DE   AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase 2 {ECO:0000255|HAMAP-Rule:MF_00208};
GN   Name=murE2 {ECO:0000255|HAMAP-Rule:MF_00208};
GN   OrderedLocusNames=CA_C2819;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM
OS   19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W).
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC
RC   13948 / NRRL B-527 / VKM B-1787 / 2291 / W;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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=UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-
CC         diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-
CC         D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+);
CC         Xref=Rhea:RHEA:23676, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57791, ChEBI:CHEBI:83900,
CC         ChEBI:CHEBI:83905, ChEBI:CHEBI:456216; EC=6.3.2.13;
CC         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; AE001437; AAK80763.1; -; Genomic_DNA.
DR   PIR; H97246; H97246.
DR   RefSeq; WP_010966104.1; NC_003030.1.
DR   AlphaFoldDB; Q97FC1; -.
DR   SMR; Q97FC1; -.
DR   STRING; 272562.CA_C2819; -.
DR   GeneID; 44999304; -.
DR   KEGG; cac:CA_C2819; -.
DR   PATRIC; fig|272562.8.peg.3004; -.
DR   eggNOG; COG0769; Bacteria.
DR   HOGENOM; CLU_022291_4_0_9; -.
DR   OrthoDB; 9800958at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000814; 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:0051301; P:cell division; IEA:InterPro.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
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   NCBIfam; NF001126; PRK00139.1-4; 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; Reference proteome.
FT   CHAIN           1..483
FT                   /note="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-
FT                   diaminopimelate ligase 2"
FT                   /id="PRO_0000101886"
FT   MOTIF           404..407
FT                   /note="Meso-diaminopimelate recognition motif"
FT   BINDING         30
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         111..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         156..157
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         183
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         380
FT                   /ligand="meso-2,6-diaminopimelate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         404..407
FT                   /ligand="meso-2,6-diaminopimelate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         456
FT                   /ligand="meso-2,6-diaminopimelate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         460
FT                   /ligand="meso-2,6-diaminopimelate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   MOD_RES         223
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
SQ   SEQUENCE   483 AA;  53845 MW;  5D0EAEC6F06B82E0 CRC64;
     MKLKQLLQNI DYDLIKGDIN INIEGISYNS KKVKQNYVFV SIKGARFDGH DFIKEAAQNG
     AAAVIIDEDF HDSIENTTLV KVKNSKVALA CLCNLFYEEP SRELNLVGVT GTNGKTTVIH
     YIRDMLEAFG NSTGTIGTLG YELKDKEINV EKINPTTPEA LELNQILRDF IDKGAKNAVM
     EVTSSALMKH RVDYCSFKVG VFTNLSQDHL DEHGTIENYK NEKIKLFKMC PVGVINLDDN
     IAGEIIEKGT CEFFTYGVLT NADLTASDMV YKPNSVSFNV HYKGISSKVK VNVPGEFTVY
     NVLAAIGSLL CLGIDFESIL KLVSSIKPVL GRLETINNPL NKNIIIDYAH TPDSLEKLLI
     MAREMTNGRI ITVFGCGGDR DKSKRGLMGM AVGILSDYCI ITSDNPRHEK PEDIIRDIER
     GMQTINSSYE KITDRRCAIK RGIEILKEED ILIIAGKGHE DYQIIGDNKV HFDDREVVNE
     LLG
//