ID   MURD_BACTN              Reviewed;         444 AA.
AC   Q8A256;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   16-JUN-2009, entry version 51.
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=BT_3450;
OS   Bacteroides thetaiotaomicron.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=818;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX   MEDLINE=22550858; PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA   Chiang H.C., Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO78556.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_812362.1; -.
DR   HSSP; P14900; 1EEH.
DR   GeneID; 1074391; -.
DR   GenomeReviews; AE015928_GR; BT_3450.
DR   KEGG; bth:BT_3450; -.
DR   NMPDR; fig|226186.1.peg.3449; -.
DR   HOGENOM; Q8A256; -.
DR   BioCyc; BTHE226186:BT_3450-MON; -.
DR   BRENDA; 6.3.2.9; 21018.
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    444       UDP-N-acetylmuramoylalanine--D-glutamate
FT                                ligase.
FT                                /FTId=PRO_0000108970.
FT   NP_BIND     109    115       ATP (Potential).
SQ   SEQUENCE   444 AA;  49492 MW;  541FED7F141F0770 CRC64;
     MKRIVILGAG ESGAGAAVLA KVKGFETFVS DMSAIKDKYK DLLDSHHIAW EEGHHTEELI
     LNADEVIKSP GIPNDAPLIL KLKAQGTPVI SEIEFAGRYT DAKMICITGS NGKTTTTSLI
     YHIFKSADLN VGLAGNIGKS LALQVAEEHH DYYIIELSSF QLDNMYNFRA NIAVLMNITP
     DHLDRYDHCM QNYIDAKFRI TQNQTTDDAF IFWNDDPIIK QELAKHGLKA HLYPFAAVKE
     DGAIAYVEDH EVKITEPIAF NMEQEELALT GQHNLYNSLA AGISANLAGI TKENIRKALS
     DFKGVEHRLE KVARVRGIDF INDSKATNVN SCWYALQSMT TKTVLILGGK DKGNDYTEIE
     DLVREKCSAL VYLGLHNEKL HAFFDRFGLP VADVQTGMKD AVEAAYKLAK KGETVLLSPC
     CASFDLFKSY EDRGDQFKKY VREL
//