ID   MURE_MESSB              Reviewed;         483 AA.
AC   Q11GS0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase;
DE            EC=6.3.2.13;
DE   AltName: Full=UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase;
DE   AltName: Full=Meso-diaminopimelate-adding enzyme;
DE   AltName: Full=Meso-A2pm-adding enzyme;
DE   AltName: Full=UDP-N-acetylmuramyl-tripeptide synthetase;
DE   AltName: Full=UDP-MurNAc-tripeptide synthetase;
GN   Name=murE; OrderedLocusNames=Meso_2012;
OS   Mesorhizobium sp. (strain BNC1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.,
RA   Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Richardson P.;
RT   "Complete sequence of chromosome of Mesorhizobium sp. BNC1.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
CC       (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanyl-D-
CC       glutamate + meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-
CC       N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diamino-
CC       heptanedioate.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Carbamoylation is probably crucial for Mg(2+) binding and,
CC       consequently, for the gamma-phosphate positioning of ATP (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the murCDEF family. MurE subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000390; ABG63405.1; -; Genomic_DNA.
DR   RefSeq; YP_674570.1; -.
DR   GeneID; 4182805; -.
DR   GenomeReviews; CP000390_GR; Meso_2012.
DR   KEGG; mes:Meso_2012; -.
DR   NMPDR; fig|266779.1.peg.607; -.
DR   HOGENOM; Q11GS0; -.
DR   OMA; Q11GS0; ERCGIVG.
DR   BioCyc; MSP266779:MESO_2012-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0008765; F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-...; IEA:EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00208; -; 1.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR000713; Mur_ligase_N.
DR   InterPro; IPR005761; UDP-N-AcMur-Glu-dNH2Pim_ligase.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   Pfam; PF01225; Mur_ligase; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 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; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN         1    483       UDP-N-acetylmuramoyl-L-alanyl-D-
FT                                glutamate--2,6-diaminopimelate ligase.
FT                                /FTId=PRO_1000012372.
FT   NP_BIND     107    113       ATP (Potential).
FT   REGION      149    150       UDP-MurNAc-L-Ala-D-Glu binding (By
FT                                similarity).
FT   REGION      404    407       Meso-diaminopimelate binding (By
FT                                similarity).
FT   MOTIF       404    407       Meso-diaminopimelate recognition motif.
FT   BINDING      29     29       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     176    176       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     182    182       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     184    184       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     380    380       Meso-diaminopimelate (By similarity).
FT   BINDING     452    452       Meso-diaminopimelate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     456    456       Meso-diaminopimelate (By similarity).
FT   MOD_RES     216    216       N6-carboxylysine (By similarity).
SQ   SEQUENCE   483 AA;  51101 MW;  A34DDB6E426467D5 CRC64;
     MKLGEFADIL PLSGSIAGET TISGLASDSR RVNAGDLFFA LQGSKADGAA YAADAAGRGA
     VAIIARPGTV GDVGVPVIEA DDPRHVLALA SARLYGAQPA TMVAVTGTSG KTSVAAFTRQ
     IWEKAGLAAA SIGTTGVVAP GRDEYGELTT PDPVSLHKLL RELADAGVTH ASMEASSHGL
     DQRRLDGVKL AAGGFTNLGR DHMDYHPTVE HYHQSKMRLF KTLLPKGAPA VIFADDPWSE
     PTEKVALAAG LQLLTVGRRG TFLTIKRVEH ERHRQRTEIE HEGMIYDIML PLAGDFQVGN
     ALVAAGLAIS TGLPADKAVA ALEHLKGASG RLELTGTTED GAQIYVDYAH KPDALENVLQ
     AVRPFTTGRV IVVFGCGGDR DPGKRPIMGE IARRLADVVI VTDDNPRSEV PAEIRRAILE
     AVPEATEIGD RREAIRTAVA MLNSGDTLIV AGKGHEIGQE IAGTKLPFSD HEEVRRALKE
     RTA
//