ID   MURD_BARHE              Reviewed;         466 AA.
AC   Q6G2Q3;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 38.
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=BH11260;
OS   Bartonella henselae (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=38323;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic
RT   derivative of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF27911.1; -; Genomic_DNA.
DR   RefSeq; YP_033898.1; -.
DR   GeneID; 2865364; -.
DR   GenomeReviews; BX897699_GR; BH11260.
DR   KEGG; bhe:BH11260; -.
DR   NMPDR; fig|283166.1.peg.1026; -.
DR   HOGENOM; Q6G2Q3; -.
DR   OMA; Q6G2Q3; SEDHLDR.
DR   BioCyc; BHEN283166:BH11260-MON; -.
DR   BRENDA; 6.3.2.9; 277357.
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    466       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000108971.
FT   NP_BIND     128    134       ATP (Potential).
SQ   SEQUENCE   466 AA;  50883 MW;  A2EF67B0883925B4 CRC64;
     MISIAFYKGK KVALFGLGKS GLATAQALIS GGADVVAWDD NPSGVQAAHR ENIPARNLQY
     ENWSEFVALI LAPGVPLTYP QPHWVVDKAR QANIEIIGDI ELFVRARNHF LQQYGFCDED
     VPFIAITGTN GKSTTTALLA HLLEQMGYDV QMGGNIGTAI LTLKPFVKKR IYVIECSSFQ
     IDLAPSLQPT IGLLLNLTPD HIDRHGSFAH YVNAKKNLVT GASQAFISVD DAACQVLYRQ
     LLHEGHHVEA VSKEHFVENG FYADGTQLFS VCQGRRHMLA DLASMAALRG SHNAQNALMA
     LATLQALKIT DPHMNKHLAS YQGLAHRMQQ VRKMGSVLFI NDSKATNAEA SAPALAAFNN
     IFWIVGGQAK EAGIVSLRGF FHKIRKAYLI GAAAEEFAGV IGSSFPFSMS LTLENAVHEA
     AVDAMRCKAK EVVVLFSPAC ASYDQFKNYE VRGEAFISFV MQLKET
//