ID   MURD_RICPR              Reviewed;         445 AA.
AC   Q9ZDC2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 129.
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; OrderedLocusNames=RP410;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(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; AJ235271; CAA14867.1; -; Genomic_DNA.
DR   PIR; A71699; A71699.
DR   RefSeq; NP_220791.1; NC_000963.1.
DR   RefSeq; WP_004597598.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZDC2; -.
DR   SMR; Q9ZDC2; -.
DR   STRING; 272947.RP410; -.
DR   EnsemblBacteria; CAA14867; CAA14867; CAA14867.
DR   GeneID; 57569535; -.
DR   KEGG; rpr:RP410; -.
DR   PATRIC; fig|272947.5.peg.423; -.
DR   eggNOG; COG0771; Bacteria.
DR   HOGENOM; CLU_032540_3_0_5; -.
DR   OMA; KGMHNVE; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004326; F:tetrahydrofolylpolyglutamate synthase activity; IEA:InterPro.
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; IPR018109; Folylpolyglutamate_synth_CS.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR036615; Mur_ligase_C_dom_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   InterPro; IPR005762; MurD.
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..445
FT                   /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT                   /id="PRO_0000109073"
FT   BINDING         111..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   445 AA;  50130 MW;  B9CCCF7437FB7AA6 CRC64;
     MNAYKKQKIG IFGLGKTGIS VYEELKNKYD LIVYDDLEAN RDIFKELFGN NLITVLSDSR
     WQDLDKIVLS PGVPLTHEVV RIAHHFNIPI ISDIDLFFEK SKNLKFIAIT GTNGKSTTTA
     LISHILNSNG LDYPVAGNIG VPALQAKASN EGYVLELSSF QLDLVKSFTV KVAVLLNITP
     DHLDRYQDMN DYIAAKAKIF DRMDKDSYAV INIDNDYCRK IFVLLQKDQS IKLIPFSVTK
     ILKNGISIVD DKIHDNDLTY KLPLNKNLQG LHNCENIAAS YAVAKIIGLE SKKILESISS
     FQSLHHRMQY IGSINNISFY NDSKATNAIS ALQSIKALDN IYWLAGGIPK EGGIEGIKPY
     FNKIKKAYFY GQAKAMFANT AKNIIDFVIC DNLEYAFNIA YKDAVSDTTE VKNILLAPSC
     SSYDQFKNFE ERGELFIKLS KRHWQ