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MURE_PROM1
ID   MURE_PROM1              Reviewed;         509 AA.
AC   A2C0L8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=NATL1_04641;
OS   Prochlorococcus marinus (strain NATL1A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL1A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000553; ABM75028.1; -; Genomic_DNA.
DR   RefSeq; WP_011823215.1; NC_008819.1.
DR   AlphaFoldDB; A2C0L8; -.
DR   SMR; A2C0L8; -.
DR   STRING; 167555.NATL1_04641; -.
DR   EnsemblBacteria; ABM75028; ABM75028; NATL1_04641.
DR   KEGG; pme:NATL1_04641; -.
DR   eggNOG; COG0769; Bacteria.
DR   HOGENOM; CLU_022291_4_1_3; -.
DR   OMA; CFMEVSS; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002592; 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.
FT   CHAIN           1..509
FT                   /note="UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-
FT                   diaminopimelate ligase"
FT                   /id="PRO_1000012374"
FT   MOTIF           425..428
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         117..123
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         159..160
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         186
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         192
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         194
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         401
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         425..428
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         476
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   BINDING         480
FT                   /ligand="meso-2,6-diaminoheptanedioate"
FT                   /ligand_id="ChEBI:CHEBI:57791"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
FT   MOD_RES         226
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00208"
SQ   SEQUENCE   509 AA;  56281 MW;  D98BD6E69F8DEDFB CRC64;
     MSRYLHTLLK AIDLQVRSGL ANPEIKNLST DSREIEKGDL FLGLDGEKVD GGTFWAKAIE
     RGACAAIISK KASLLNPPTN EDPVVILPEP VSLFMGKLAA DFWGKPSSEI CLIGITGTNG
     KTTTSFLIEF LTTSLGHPSA LFGTLINRWP NYEETSKYTT TFAVPLQAKL RKAVQAGVEY
     GAMEVSSHAL SQNRVAGCDF NGAIFTNLSR DHLDYHDSME SYFEAKASLF RSHLIDDDGP
     RSVINIDDKW GSILAKELNK KCWTCSLKEN SQIREKPDLY ISNLQIMQDG YMGKLHTPFG
     VGNFISPLIG EFNLMNMLQA IGILVQRGLP LNDLLEALNK FPGVPGRMQL INMDGFKVKD
     GYPLVIVDYA HTPDGLQNAL IASRSLTKKR LICVFGCGGD RDKGKRSKMG EVAAKFADYI
     VVTSDNPRQE DPIEIIKDIQ KGITIDSEIS VEPERSIAIQ FAIAKAKKND VVLIAGKGHE
     DYQILKDQTI YFDDREQARK ALSLRTDVI
 
 
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