ID   MURE_LAWIP              Reviewed;         482 AA.
AC   Q1MPC4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-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=LI1099;
OS   Lawsonia intracellularis (strain PHE/MN1-00).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Lawsonia.
OX   NCBI_TaxID=363253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA   Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT   "The complete genome sequence of Lawsonia intracellularis: the
RT   causative agent of proliferative enteropathy.";
RL   Submitted (NOV-2005) 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.
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DR   EMBL; AM180252; CAJ55153.1; -; Genomic_DNA.
DR   RefSeq; YP_595474.1; -.
DR   GeneID; 4060077; -.
DR   GenomeReviews; AM180252_GR; LI1099.
DR   KEGG; lip:LI1099; -.
DR   HOGENOM; Q1MPC4; -.
DR   OMA; Q1MPC4; HTPDGIE.
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    482       UDP-N-acetylmuramoyl-L-alanyl-D-
FT                                glutamate--2,6-diaminopimelate ligase.
FT                                /FTId=PRO_1000012369.
FT   NP_BIND     105    111       ATP (Potential).
FT   REGION      147    148       UDP-MurNAc-L-Ala-D-Glu binding (By
FT                                similarity).
FT   REGION      402    405       Meso-diaminopimelate binding (By
FT                                similarity).
FT   MOTIF       402    405       Meso-diaminopimelate recognition motif.
FT   BINDING      24     24       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     174    174       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     180    180       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     182    182       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     378    378       Meso-diaminopimelate (By similarity).
FT   BINDING     453    453       Meso-diaminopimelate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     457    457       Meso-diaminopimelate (By similarity).
FT   MOD_RES     214    214       N6-carboxylysine (By similarity).
SQ   SEQUENCE   482 AA;  53605 MW;  6B4DB5FF5EBE96C3 CRC64;
     MNRYPLKALE SELEKKHMLI CIDSRKVEKG CVFVALPGSS VDGGLFIPDA VSRGAAYIVC
     RHNEVEYCGS AIPIVVDDPR YTLGRLARIF YNTGNLSMPI IGVTGTNGKT TITYLLEYLF
     RAKGNRTGVI GTIAYRWPGF SKEAPLTTPQ CLDLHAMLAQ MQVDKTEIVF MEVSSHALDQ
     RRIAGISFKG VIFTNLTQDH LDYHKDMKEY FHAKARLFFE YPSKNKIMVA SMDNQWGRKL
     AKLVPEIIGF GFKNKPTQVS NYLFGKILSS SRAGLHLQMS FKDKVWELCT PLVGVHNAEN
     LLAVQAISLQ LGLAPEDFCC FEKFTGVPGR LERIVNKKQL DIFVDYAHTP DALINVLSAL
     RDVGFKRIIT VFGCGGNRDK AKRPLMGKAV AKLSDVAVLT SDNPRNEDPE LIMADVLPGL
     KKAKQIITEP DREKAIRQAI ELVSPGDALL VAGKGHECTQ QIGFMKYPFS DQSVIRKILG
     CD
//