ID   MURE_HAEI8              Reviewed;         488 AA.
AC   Q4QLG3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 37.
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=NTHI1300;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable
RT   Haemophilus influenzae: comparative study with H. influenzae serotype
RT   d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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.
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DR   EMBL; CP000057; AAX88134.1; -; Genomic_DNA.
DR   RefSeq; YP_248794.1; -.
DR   GeneID; 3430562; -.
DR   GenomeReviews; CP000057_GR; NTHI1300.
DR   KEGG; hit:NTHI1300; -.
DR   HOGENOM; Q4QLG3; -.
DR   OMA; Q4QLG3; HTPDGIE.
DR   BioCyc; HINF281310:NTHI1300-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    488       UDP-N-acetylmuramoyl-L-alanyl-D-
FT                                glutamate--2,6-diaminopimelate ligase.
FT                                /FTId=PRO_1000012356.
FT   NP_BIND     113    119       ATP (Potential).
FT   REGION       41     43       UDP-MurNAc-L-Ala-D-Glu binding (By
FT                                similarity).
FT   REGION      155    156       UDP-MurNAc-L-Ala-D-Glu binding (By
FT                                similarity).
FT   REGION      410    413       Meso-diaminopimelate binding (By
FT                                similarity).
FT   MOTIF       410    413       Meso-diaminopimelate recognition motif.
FT   BINDING      24     24       UDP-MurNAc-L-Ala-D-Glu; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING      26     26       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     154    154       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     182    182       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     188    188       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     190    190       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     386    386       Meso-diaminopimelate (By similarity).
FT   BINDING     461    461       Meso-diaminopimelate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     465    465       Meso-diaminopimelate (By similarity).
FT   MOD_RES     222    222       N6-carboxylysine (By similarity).
SQ   SEQUENCE   488 AA;  53643 MW;  01690E772AB7D99C CRC64;
     MKKLTALFNL PELKNDIELH NMVLDSRKVK AGDLFVAIKG HQVDGNQFID SALHSGASAV
     VSETELSSEH LTVAFIRNVP VVKYYQLARH LSSLADVFYD SPSKNLTLVG VTGTNGKTTI
     SQLLAQWAEL LGHRAAVMGT IGNGLLGQIV EAKNTTGSAV EIQSSLSTFK HAGADFTSIE
     VSSHGLAQHR VEALHFKAAI FTNLTRDHLD YHQSMENYAA AKKRLFTELD TQIKVINADD
     EIGYQWLTEL PDAIAVSMNA DFKVGSHQWM KAINIHYHFK GADITFESSW GNGVLHSPLI
     GAFNVSNLLL VMTTLLSFGY PLENLLATAK SLKGVCGRME MIQYPNKPIV IVDYAHTPDA
     LEKALIAARE HCQGELWCIF GCGGDRDRGK RPLMAQVAEQ FAEKIIVTKD NPRTEPQSQI
     EADIVAGFKN MEKVGIIPDR AQAIQFAIES AVENDVILIA GKGHEHYQII GSEVVHFSDQ
     EIALDFLK
//