ID   MURE_LEPBL              Reviewed;         500 AA.
AC   Q04Y85;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=LBL_2600;
OS   Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC   Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=355276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA   Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A.,
RA   Cullen P.A., Davis J., Johnson M., Kuczek E., Alt D.P.,
RA   Peterson-Burch B., Coppel R.L., Rood J.I., Davies J.K., Adler B.;
RT   "Genome reduction in Leptospira borgpetersenii reflects limited
RT   transmission potential.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000348; ABJ79960.1; -; Genomic_DNA.
DR   RefSeq; YP_798893.1; -.
DR   GeneID; 4407945; -.
DR   GenomeReviews; CP000348_GR; LBL_2600.
DR   KEGG; lbl:LBL_2600; -.
DR   OMA; Q04Y85; 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; 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; 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    500       UDP-N-acetylmuramoyl-L-alanyl-D-
FT                                glutamate--2,6-diaminopimelate ligase.
FT                                /FTId=PRO_1000012371.
FT   NP_BIND     118    124       ATP (Potential).
FT   REGION      160    161       UDP-MurNAc-L-Ala-D-Glu binding (By
FT                                similarity).
FT   REGION      419    422       Meso-diaminopimelate binding (By
FT                                similarity).
FT   MOTIF       419    422       Meso-diaminopimelate recognition motif.
FT   BINDING      38     38       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     187    187       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     195    195       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     395    395       Meso-diaminopimelate (By similarity).
FT   BINDING     471    471       Meso-diaminopimelate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     475    475       Meso-diaminopimelate (By similarity).
FT   MOD_RES     227    227       N6-carboxylysine (By similarity).
SQ   SEQUENCE   500 AA;  54801 MW;  7956C64A14928D2C CRC64;
     MKMKLTNLLH EFPELKLGSL PSGKNPDSVP IEYIQSDSRK TNPEDIFCVP ESIGTKKGEF
     ISNTKASVIL LHRSSNISID SSKIVLECEE DPEQLQGRIA SFLLGHPSKT LEIVAVTGTN
     GKTSLTNILF ALAKDQGKIC GLIGTIGVKF GDRSIDTGYT TPDASSLNLI LKQMKDEGVT
     TVFMEASSHG LKLGRIGGIS LKAGVFTNLT QDHLDFHSDM EDYFESKFRL FEILDVSKSP
     FAVLDYSSPG GNELHRKIRN NLPDLPIKAL DGIGGEYKVS NPFLTLQGTS YVLSLPGNRS
     QTISTNLLGS FNVRNTALAF LTGLGLGLDP KGMFSSLKEI PQIPGRFQIV YSKDRSRMAV
     VDYAHTPDAL ENIIRSVRNS RPKRLITLFG CGGDRDKTKR PKMARIAEEL SDQVILTSDN
     PRSEKPEAIL DEIQSGFSPG FTPLLREVDR ARAISEGVGI LPEGGCLLVA GKGHEEYQII
     GKEKRHFSDV EEVRKAFGLF
//