ID   MURD_BAUCH              Reviewed;         446 AA.
AC   Q1LSW4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=BCI_0520;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF14267.1; -; Genomic_DNA.
DR   RefSeq; YP_588950.1; -.
DR   GeneID; 4056451; -.
DR   GenomeReviews; CP000238_GR; BCI_0520.
DR   KEGG; bci:BCI_0520; -.
DR   HOGENOM; Q1LSW4; -.
DR   OMA; Q1LSW4; SEDHLDR.
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    446       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000257166.
FT   NP_BIND     112    118       ATP (Potential).
SQ   SEQUENCE   446 AA;  49108 MW;  165EEC1D7FFE2590 CRC64;
     MTNYYGHNIV IIGLGITGIT CVNFFRSRGI TPRVMDTRYN PPQLNQLPKD IQYWLGELKI
     EWLLAATLIV ISPGISLSHP AINTAMKCGI EIIGDVELFL REVTVPVVAI TGTNGKSTVA
     KLVGTMANCA GLKVGVGGNI GYPVLSLLQQ SHQLYVLELS SFQLETTKNL KVAVATILNI
     SEDHMDRYPL GLQQYREAKL KIYKQAKIYI INDDDKLTLP ANSTNKEYCS IIKFGIKSGH
     YCLGDYQGKQ WLMAYGKPLL DCNEIKIIGR HNLLNALAAL ALAEAIAIPR QACLIALRQF
     SGLMHRFELV LERKGIRWIN DSKATNVGST KAALNELTVD GTLHLLLGGD GKLADFSSLQ
     PFVQGNNIHL YCFGKDSKKL AALNQHSATI TQTLSQAMHI INNQVKAGDV VLLSPACSSL
     DQFENFKVRG KTFTNLVFEF NDGNNN
//