ID   MURD_CHLFF              Reviewed;         419 AA.
AC   Q255W7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-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=CF0149;
OS   Chlamydophila felis (strain Fe/C-56).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydophila.
OX   NCBI_TaxID=264202;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16766509; DOI=10.1093/dnares/dsi027;
RA   Azuma Y., Hirakawa H., Yamashita A., Cai Y., Rahman M.A., Suzuki H.,
RA   Mitaku S., Toh H., Goto S., Murakami T., Sugi K., Hayashi H.,
RA   Fukushi H., Hattori M., Kuhara S., Shirai M.;
RT   "Genome sequence of the cat pathogen, Chlamydophila felis.";
RL   DNA Res. 13:15-23(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; AP006861; BAE80921.1; -; Genomic_DNA.
DR   RefSeq; YP_515066.1; -.
DR   GeneID; 3958963; -.
DR   GenomeReviews; AP006861_GR; CF0149.
DR   KEGG; cfe:CF0149; -.
DR   HOGENOM; Q255W7; -.
DR   OMA; Q255W7; DSKATNF.
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    419       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000257177.
FT   NP_BIND     109    115       ATP (Potential).
SQ   SEQUENCE   419 AA;  46307 MW;  DB7119E7EB30DD30 CRC64;
     MNHQRVVVLG AGVTGKSAAE FLHKKGDFVI GIDGSWDALI SCNFFHQRYL DKTENFPEDV
     DLFVRSPGIK TSHPLVIEAK RRDIPIVTDV QLAFQSPEFY QYPSLGITGS TGKTTTVLFL
     VHLLHSLGIS AFAMGNIGFP ILQAMYQKGV RVVEISSFQL TEQEQKIPVL SGAAILNISE
     NHLDYHQTLH AYSEAKMNIA KCLQWPDSLW SGEGVSSGRS YLEYTEEIDS VLDKGGALKP
     LYLHDRNNYC AAYALAKEVT SVPLEAFLQA VQTFEKPPHR IEYLGEKDGV RYINDSKATT
     MSSVEKALMA VKENVIVIMG GRNKESNFTS LIPVLTQTVK HIVAMGECRK EIAQALSSSL
     PLTQARDLQE AVSIAQSIAQ PGDVILLSPG CASFDQFRSF EERGDCFRQL VGDMEALKI
//