ID   MURD_STRR6              Reviewed;         450 AA.
AC   Q8DQM2;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
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}; OrderedLocusNames=spr0603;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
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; AE007317; AAK99407.1; -; Genomic_DNA.
DR   PIR; C97947; C97947.
DR   RefSeq; NP_358197.1; NC_003098.1.
DR   RefSeq; WP_000863046.1; NC_003098.1.
DR   AlphaFoldDB; Q8DQM2; -.
DR   SMR; Q8DQM2; -.
DR   STRING; 171101.spr0603; -.
DR   EnsemblBacteria; AAK99407; AAK99407; spr0603.
DR   GeneID; 60233601; -.
DR   KEGG; spr:spr0603; -.
DR   PATRIC; fig|171101.6.peg.670; -.
DR   eggNOG; COG0771; Bacteria.
DR   HOGENOM; CLU_032540_0_1_9; -.
DR   OMA; CNFENYL; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000586; 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; Reference proteome.
FT   CHAIN           1..450
FT                   /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT                   /id="PRO_0000109097"
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;  48579 MW;  AF0B2DB9B7B10453 CRC64;
     MKVIDQFKNK KVLVLGLAKS GESAARLLDK LGAIVTVNDG KPFEDNPAAQ SLLEEGIKVI
     TGGHPLELLD EEFALMVKNP GIPYNNPMIE KALAKRIPVL TEVELAYLIS EAPIIGITGS
     NGKTTTTTMI GEVLTAAGQH GLLSGNIGYP ASQVAQIASD KDTLVMELSS FQLMGVQEFH
     PEIAVITNLM PTHIDYHGSF SEYVAAKWNI QNKMTAADFL VLNFNQDLAK DLTSKTEATV
     VPFSTLEKVD GAYLEDGQLY FRGEVVMAAN EIGVPGSHNV ENALATIAVA KLRDVDNQTI
     KETLSAFGGV KHRLQFVDDI KGVKFYNDSK STNILATQKA LSGFDNSKVV LIAGGLDRGN
     EFDELVPDIT GLKKMVILGQ SAERVKRAAD KAGVAYVEAT DIADATRKAY ELATQGDVVL
     LSPANASWDM YANFEVRGDL FIDTVAELKE