ID   MURD_BORAP              Reviewed;         451 AA.
AC   Q0SMS3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=BAPKO_0616;
OS   Borrelia afzelii (strain PKo).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Borrelia;
OC   Borrelia burgdorferi group.
OX   NCBI_TaxID=390236;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA   Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M.,
RA   Suehnel J., Wilske B., Platzer M.;
RT   "Comparative genome analysis: selection pressure on the Borrelia vls
RT   cassettes is essential for infectivity.";
RL   BMC Genomics 7:211-211(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; CP000395; ABH01855.1; -; Genomic_DNA.
DR   RefSeq; YP_710031.1; -.
DR   GeneID; 4227919; -.
DR   GenomeReviews; CP000395_GR; BAPKO_0616.
DR   KEGG; baf:BAPKO_0616; -.
DR   NMPDR; fig|390236.5.peg.641; -.
DR   HOGENOM; Q0SMS3; -.
DR   OMA; Q0SMS3; VSPLSFF.
DR   BioCyc; BAFZ390236:BAPKO_0616-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; 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   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    451       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000301416.
FT   NP_BIND     118    124       ATP (Potential).
SQ   SEQUENCE   451 AA;  51147 MW;  267FCDFA92509B50 CRC64;
     MRLDEIKNLN FLVMGLGLNG GGVALSRFLL KHGAKLVITD LKSEAELALS IDSLRDFDDQ
     IRYVLGKHDV NDFKKADIVV KNPSVRPNNK YLKLAKRVET DISLFLIFNK NPIIAVTGTK
     GKSTLVSLLY QALKKKYPRV KLGGNIGVSP LSFFDQLDGK SPLILELSSW QLQSLENFNP
     ILSIITNVYN DHQNYYSNFD DYIIDKSKIF VNQTSGIVII QDKAYYKYFS KFESKAKVIL
     FSEFNPCNLD QDIFYSNKGE VYFNDNLIGS FFESQVVFMI PKLIAFFVAY YLNIDLNHMF
     QILKNFKGIE HRLEFVKLVR NVMFYNDTAS TIPDSTVLSV KSLKTNDNCI NLIVGGTDKN
     LDFSSFSKII NLVKAWILIK GSATVKIINV LEKSSIQYFV FDSLRGAVNY AFEISSPGDI
     VLFSPASASF ELFNNEFDRG LQFKKLVDML G
//