ID   MURD_BACC4              Reviewed;         450 AA.
AC   B7H6P8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_00639};
DE            EC=6.3.2.9 {ECO:0000255|HAMAP-Rule:MF_00639};
DE   AltName: Full=D-glutamic acid-adding enzyme {ECO:0000255|HAMAP-Rule:MF_00639};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_00639};
GN   Name=murD {ECO:0000255|HAMAP-Rule:MF_00639};
GN   OrderedLocusNames=BCB4264_A4013;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus B4264.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC       {ECO:0000255|HAMAP-Rule:MF_00639}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC         ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-
CC         glutamate; Xref=Rhea:RHEA:16429, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29986, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83898, ChEBI:CHEBI:83900, ChEBI:CHEBI:456216; EC=6.3.2.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00639};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00639}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00639}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00639}.
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DR   EMBL; CP001176; ACK60624.1; -; Genomic_DNA.
DR   RefSeq; WP_000860116.1; NZ_VEHB01000002.1.
DR   AlphaFoldDB; B7H6P8; -.
DR   SMR; B7H6P8; -.
DR   EnsemblBacteria; ACK60624; ACK60624; BCB4264_A4013.
DR   KEGG; bcb:BCB4264_A4013; -.
DR   HOGENOM; CLU_032540_0_1_9; -.
DR   OMA; CNFENYL; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000007096; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008764; F:UDP-N-acetylmuramoylalanine-D-glutamate ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   Gene3D; 3.90.190.20; -; 1.
DR   HAMAP; MF_00639; MurD; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR004101; Mur_ligase_C.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR005762; MurD.
DR   Pfam; PF02875; Mur_ligase_C; 1.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 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; Cytoplasm; Ligase; Nucleotide-binding;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..450
FT                   /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT                   /id="PRO_1000130826"
FT   BINDING         119..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00639"
SQ   SEQUENCE   450 AA;  48940 MW;  091450240C8DC885 CRC64;
     MKTVTEFQNK NILVLGIAKS GYAAATLLQK LGANVIVNDG KPLAENVLAA ELQAKGMDVV
     CGGHPLELLE RNISLVVKNP GIPYSNPILV AAKEKQIPIV TEVELAYRIS EAPFVGITGS
     NGKTTTTMLT FEMLKEGQKH PVIAGNIGTV ACEVAQDAKE NEVVVTELSS FQLMGVELFQ
     PKIAAFLNLF EAHLDYHGTK KEYGLAKANI FKNQTENDYS VINADDADVM ALSAYSKGQK
     ILFSTTKEIE DGACIKDNAL YFKGEKVVEV SDIVLPGQHN LENILAAMSI AKLLGTSNEA
     ITVVLKRFTG VKHRLEYVTT INNRKFYNDS KATNMLATEK ALSAFTQPIV LLAGGLDRGN
     EFDDLIPYFK NVKAIVTFGQ TAPKLVRAAE KAGLDIIESV DTLDEAVVKA YAHSKDGDVV
     LLSPACASWD QFKTFEERGD IFIQAVHKLI