ID   MURE_ALCBS              Reviewed;         490 AA.
AC   Q0VS07;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=ABO_0593;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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.
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; AM286690; CAL16041.1; -; Genomic_DNA.
DR   RefSeq; YP_692313.1; -.
DR   GeneID; 4211243; -.
DR   GenomeReviews; AM286690_GR; ABO_0593.
DR   KEGG; abo:ABO_0593; -.
DR   NMPDR; fig|393595.12.peg.591; -.
DR   HOGENOM; Q0VS07; -.
DR   OMA; Q0VS07; FPVIVDY.
DR   BioCyc; ABOR393595:ABO_0593-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    490       UDP-N-acetylmuramoyl-L-alanyl-D-
FT                                glutamate--2,6-diaminopimelate ligase.
FT                                /FTId=PRO_1000058583.
FT   NP_BIND     112    118       ATP (Potential).
FT   REGION      154    155       UDP-MurNAc-L-Ala-D-Glu binding (By
FT                                similarity).
FT   REGION      406    409       Meso-diaminopimelate binding (By
FT                                similarity).
FT   MOTIF       406    409       Meso-diaminopimelate recognition motif.
FT   BINDING      27     27       UDP-MurNAc-L-Ala-D-Glu; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING      29     29       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     181    181       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     187    187       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     189    189       UDP-MurNAc-L-Ala-D-Glu (By similarity).
FT   BINDING     382    382       Meso-diaminopimelate (By similarity).
FT   BINDING     457    457       Meso-diaminopimelate; via carbonyl oxygen
FT                                (By similarity).
FT   BINDING     461    461       Meso-diaminopimelate (By similarity).
FT   MOD_RES     221    221       N6-carboxylysine (By similarity).
SQ   SEQUENCE   490 AA;  51222 MW;  659B7856B35036E4 CRC64;
     MMTLQQLLPN TTLPATAAGV VLSGLQLDSR KVMPGDAFLA VQGVASDGRQ FVSQAIAAGA
     VAVLAEAETF SVQQEQAVPR VNFPGLSRSV GELAARWYGE PGSAMNVVGV TGTNGKTSIT
     WFLRDALNAL GHRCALVGTL GLGLKDNEQI TGHTTPDPIT LQAGLARVLE AGADTVAMEV
     SSHALDQHRL GPTPVSVAVF SNLSRDHLDY HGDMEAYLAA KSVLFTRDGV KLAVINCDDP
     VAYSLVGCLA DGVRCVTFGD QTGATVRCAS VAFTAEGTNA ELNVGGESFS VTLPLFGRFN
     LSNLMAVAGI LHGQGVSTDS LAGALAAITP VPGRMEPVQQ AGCPTVIVDY AHTPDGLEKA
     LQACRAHFAG RLFCIIGCGG DRDTGKRPQM AAVAERGADH VVFTSDNPRS EDPQKIIDEM
     CAGLTDTGSV QIIVERDRAV MDTVQAASDG DVILLAGKGH EDYQEVNGVR YPSDDRDLAH
     KAFNARGGAQ
//