ID   MURD_RICCN              Reviewed;         500 AA.
AC   Q92I60;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 130.
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=RC0560;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL03098.1; -; Genomic_DNA.
DR   PIR; H97769; H97769.
DR   RefSeq; WP_010977195.1; NC_003103.1.
DR   AlphaFoldDB; Q92I60; -.
DR   SMR; Q92I60; -.
DR   EnsemblBacteria; AAL03098; AAL03098; RC0560.
DR   KEGG; rco:RC0560; -.
DR   PATRIC; fig|272944.4.peg.639; -.
DR   HOGENOM; CLU_032540_3_0_5; -.
DR   OMA; KGMHNVE; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000816; 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   InterPro; IPR022437; RPE3.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53244; SSF53244; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
DR   TIGRFAMs; TIGR01087; murD; 1.
DR   TIGRFAMs; TIGR03775; RPE3; 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..500
FT                   /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT                   /id="PRO_0000109071"
FT   DOMAIN          260..306
FT                   /note="RPE3 insert"
FT   BINDING         111..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   500 AA;  55787 MW;  024B268F6074822C CRC64;
     MNSHTKQKIG VFGLGKTGIS VYEELQNKYD VIVYDDLKAN RDIFEELYSK TAIAALSDSR
     WQNLDTIVLS PGIPLTHEIV NIAKSFNIPI TSDIDLLFAK SKNLKFIAIT GTNGKSTTTA
     LISHILNSSG LDYPVAGNIG VSALQAKASK DGYVLELSSF QLDLVKTFTA KIAVLLNITP
     DHLDRHQDMT CYIAAKSKIF DRMDQESYAV INIDNDYCRE VFIKLQQEQR IKLIPFSVAQ
     ILENGISVVD DKISANFCDD ISFELQHNSE SFRQDEFQGE PAEPECIKIR EHRQDLQNSL
     VSSFMHYAVP FNKNLQGVHN CENIAASYAV AKIIGVEPKK ILESISSFQS LPHRMQYIGS
     INNISFYNDS KATNAISAVQ SIKALDNIYW LAGGIPKEGG IEEIKPYFSH IKKAYFYGQA
     KEIFANTAKN IVDFVICDNL EQAFDLAYKD AVGDNAEIKN ILLAPSCSSY DQFKNFEERG
     ELFIKLCSIL SLRGLITGSS