MURE_ALKEH
ID MURE_ALKEH Reviewed; 498 AA.
AC Q0A6J7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
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}; OrderedLocusNames=Mlg_2198;
OS Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Alkalilimnicola.
OX NCBI_TaxID=187272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL Submitted (AUG-2006) 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: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;
CC Evidence={ECO:0000255|HAMAP-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; CP000453; ABI57540.1; -; Genomic_DNA.
DR RefSeq; WP_011629934.1; NC_008340.1.
DR AlphaFoldDB; Q0A6J7; -.
DR SMR; Q0A6J7; -.
DR EnsemblBacteria; ABI57540; ABI57540; Mlg_2198.
DR KEGG; aeh:Mlg_2198; -.
DR eggNOG; COG0769; Bacteria.
DR HOGENOM; CLU_022291_4_1_6; -.
DR OMA; CFMEVSS; -.
DR OrthoDB; 1861122at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001962; 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; 3.40.1190.10; -; 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; Cell cycle; Cell division; Cell shape;
KW Cell wall biogenesis/degradation; Cytoplasm; Ligase; Magnesium;
KW Nucleotide-binding; Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..498
FT /note="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-
FT diaminopimelate ligase"
FT /id="PRO_1000058584"
FT MOTIF 416..419
FT /note="Meso-diaminopimelate recognition motif"
FT BINDING 29
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 120..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT BINDING 162..163
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 189
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 195
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 197
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 392
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT BINDING 416..419
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT BINDING 466
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT BINDING 470
FT /ligand="meso-2,6-diaminoheptanedioate"
FT /ligand_id="ChEBI:CHEBI:57791"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT MOD_RES 229
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
SQ SEQUENCE 498 AA; 52734 MW; 47C311F5CA7964C6 CRC64;
MMRLRTLLQP WLDLTDADDR PVGGLAVDSR DIEPGFVFVA LRGSRHHGLG YLGDALAAGA
GAVLWEPAGD VAPEPDERTA AERAGVPLIA VPDLGRRLGP IAARLYGDPS ARMRVVGVTG
TDGKTSVTQY LAQLLDREAH RCGLVGTLGS GFPDSLQPGT HTTPDAASVQ RTLARLHRQG
AAQVAMEVSS HALDQHRVAG VRFHTAVLTN LGRDHLDYHG DLAGYAEAKS RLFGVPGLQW
AVLNLDDAFG RQVHGALAGG TRALGYSLAG HPQAGVRGEG LVLEPQGLRL RLSTEWGEAP
VQAPLLGAFN AANVLAVAAA ALSLGVALPV IVERLAGLRP VPGRMEPFTR PGRPSVIVDY
AHTPAALRGA LAAVRAHYRG AVWLVFGCGG DRDRGKRPLM GEAAAELADR VVLTDDNPRR
EDPDRIIDDI RQGAPGRDWP VLRDRAGAIR HAVERAGPED VVLVAGKGHE TVQQIGDRCL
PFSDREAVVQ ALGEEEGA
