ID   MURD_BUCAP              Reviewed;         440 AA.
AC   Q8K9T2;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase;
DE            EC=6.3.2.9;
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase;
DE   AltName: Full=D-glutamic acid-adding enzyme;
GN   Name=murD; OrderedLocusNames=BUsg_212;
OS   Buchnera aphidicola subsp. Schizaphis graminum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=98794;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22084549; PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate
CC       to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA)
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + UDP-N-acetylmuramoyl-L-alanine +
CC       glutamate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-
CC       glutamate.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the murCDEF family.
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DR   EMBL; AE013218; AAM67775.1; -; Genomic_DNA.
DR   RefSeq; NP_660564.1; -.
DR   HSSP; P14900; 1E0D.
DR   GeneID; 1005411; -.
DR   GenomeReviews; AE013218_GR; BUsg_212.
DR   KEGG; bas:BUsg212; -.
DR   HOGENOM; Q8K9T2; -.
DR   OMA; Q8K9T2; LWVNDTK.
DR   BioCyc; BAPH198804:BUSG212-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate lig...; IEA:HAMAP.
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_00639; -; 1.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR005762; UDP-N-AcMur-Glu_ligase.
DR   Gene3D; G3DSA:3.90.190.20; Mur_ligase_C; 1.
DR   Gene3D; G3DSA:3.40.1190.10; Mur_ligase_cen; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   TIGRFAMs; TIGR01087; murD; 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    440       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000108986.
FT   NP_BIND     113    119       ATP (Potential).
SQ   SEQUENCE   440 AA;  49855 MW;  DD9C28B6B8E8974E CRC64;
     MSYNYFGKKI LILGLGLTGI SCINFFLKKG IQPRVIDESN KPIFLNKIPK NIEYKLGNLK
     ENWILESDLI IISPGISSFK PILMKARSLG IDIISDIELF SRETKCPIIS ITGTNGKSTV
     ATMVKKIAEK SGYKVLLGGN IGFPVLEMLN KKASLYVLEL SSFQLETTFN LKSKIAVVLN
     ITEDHLDRYP EGFEQYKKTK LSIYNKAKIC LIKLKKGEKK PFNTKSKKYI SFGTCNNNDY
     YINYEKEKAI LFHKNKKIVD TSNILLNGHH NYENILTSLA ISDQMKFDQK VSINVLKKFL
     GLPHRFQTVH INNNISWIND SKSTNVDSTK AALKNLKIKG TIWLLLGGDG KSSNFNILKK
     YFEKIKIKIY CFGKDGLNLS KLCKKKSIYT KTLKQAIILI SKKIQPGDVV LLSPGCSSKD
     QFSNFEERGN LFIKLSKEIN
//