ID   MURD_ENTHR              Reviewed;         460 AA.
AC   O07669;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=UDP-N-acetylmuramoylalanine--D-glutamate ligase;
DE            EC=6.3.2.9;
DE   AltName: Full=D-glutamic acid-adding enzyme;
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase;
GN   Name=murD;
OS   Enterococcus hirae.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S185;
RX   PubMed=10520745; DOI=10.3109/10425179809072190;
RA   Duez C., Thamm I., Sapunaric F., Coyette J., Ghuysen J.-M.;
RT   "The division and cell wall gene cluster of Enterococcus hirae S185.";
RL   DNA Seq. 9:149-161(1998).
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA).
CC       {ECO:0000250}.
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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000305}.
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DR   EMBL; Y13922; CAA74234.1; -; Genomic_DNA.
DR   AlphaFoldDB; O07669; -.
DR   SMR; O07669; -.
DR   STRING; 1354.A6P53_03400; -.
DR   UniPathway; UPA00219; -.
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..460
FT                   /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT                   /id="PRO_0000109011"
FT   BINDING         123..129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   460 AA;  50282 MW;  C054CE9046A754AD CRC64;
     MTGNEKNFNH SKTKKVLVLG LAKSGFSAAK LLHELGALVT VNDGKPFDEK PEAQELLSLG
     VKVIAGSHPI ELLDEEFSLM VKNPGIPYSH PFVQKAQELG IPVITEVELA YEVAECPIIG
     ITGTNGKTTT TTMTGLLLNA GDLPGTARLA GNIGYPASSV AQEATADDKI VMELSSFQLM
     GITDFRPHVA VVTNIYEAHI DYHKTRKEYV KAKWHLQQNM TEKDYLILNW NQEELRELSK
     KTKATVLPFA TEQKLPKGAC SLDGSIYYNQ EKIMDITELG VPGSHNVENA LAAISVAKLY
     GISNEAIKNA LHHFHGVPHR TQYVGEFQGR KFYNDSKATN ILATKMALSG FQLDQLVLIA
     GGLDRGNSFD ELIPALKGIK ALITFGETQN RLEDAGKKAG IPVIKTAENA EAAVPIALEL
     SEEGDSILLS PANASWDQYP NFEIRGERFM EAVNKLTIQK