ID   MURD_CHLMU              Reviewed;         416 AA.
AC   Q9PLG5;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 2.
DT   16-JUN-2009, entry version 58.
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=TC_0139;
OS   Chlamydia muridarum.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=83560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   MEDLINE=20150255; PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F.,
RA   White O., Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J.,
RA   Bass S., Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C.,
RA   Dodson R.J., Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F.,
RA   McClarty G., Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia
RT   pneumoniae AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39017.1; ALT_INIT; Genomic_DNA.
DR   PIR; F81736; F81736.
DR   RefSeq; NP_296518.1; -.
DR   HSSP; P14900; 1EEH.
DR   GeneID; 1245673; -.
DR   GenomeReviews; AE002160_GR; TC_0139.
DR   KEGG; cmu:TC0139; -.
DR   TIGR; TC_0139; -.
DR   HOGENOM; Q9PLG5; -.
DR   BioCyc; CMUR243161:TC_0139-MON; -.
DR   BRENDA; 6.3.2.9; 256349.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IEA:InterPro.
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   GO; GO:0006571; P:tyrosine biosynthetic process; IEA:InterPro.
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; IPR003099; Prephen_DH.
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   Pfam; PF02153; PDH; 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    416       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000108992.
FT   NP_BIND     108    114       ATP (Potential).
SQ   SEQUENCE   416 AA;  46265 MW;  0F7C4879B3EDC8D3 CRC64;
     MGLKRVVVIG LGLSGKSIAR FLARKGVYVL GVDSSIQALQ HCPYIHEKLL ETDEFPTQVD
     YVVRSPGISK DHPWVKAARA AQISVVTDIQ LAFQTKEFIE QKSFGITGTV GKTTTILFLE
     YLLRKAGIPA FAMGNVGVPI LDGMQNSGVR LVEMSSFQLA DQETSYPVLS GGMILNISDN
     HLDYHGSFLE YCQSKQNLSL CMRNPEDLWV GDQRFCGRSY WEEVQKYMRL LDKESALKPL
     YLHDKYNYCC AYLLAQAEFP IAKSLFIEAV ATFKKPSHRM EYLGEKCGVH YINDSKATTV
     RATEKALLSI GSRAIVILGG RNKGYSFVSL LPSLRRFAKS VVAMGECAQE IAQDLDGFPV
     TVVRNLHEAL LCAEEQAIPG DVVLLSPACA SFDQFRSYEE RGAIFKQLVG MEEVLL
//