ID   MURD2_XYLFT             Reviewed;         468 AA.
AC   Q87EA7;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_02208};
DE            EC=6.3.2.53 {ECO:0000255|HAMAP-Rule:MF_02208};
DE   AltName: Full=UDP-N-acetylmuramoyl-L-alanyl-L-glutamate synthetase {ECO:0000255|HAMAP-Rule:MF_02208};
DE            Short=UDP-MurNAc-L-Ala-L-Glu synthetase {ECO:0000255|HAMAP-Rule:MF_02208};
GN   Name=murD2 {ECO:0000255|HAMAP-Rule:MF_02208}; OrderedLocusNames=PD_0410;
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=183190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Temecula1 / ATCC 700964;
RX   PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA   Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA   Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA   Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA   Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA   Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA   Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA   Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA   Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA   Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA   Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA   Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's disease
RT   and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(2003).
CC   -!- FUNCTION: Cell wall formation. Catalyzes the addition of L-glutamate to
CC       the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine.
CC       {ECO:0000255|HAMAP-Rule:MF_02208}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + UDP-N-acetyl-alpha-D-muramoyl-L-alanine =
CC         ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-
CC         glutamate; Xref=Rhea:RHEA:58816, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83898, ChEBI:CHEBI:142725, ChEBI:CHEBI:456216;
CC         EC=6.3.2.53; Evidence={ECO:0000255|HAMAP-Rule:MF_02208};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02208}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02208}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. MurD2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_02208}.
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DR   EMBL; AE009442; AAO28290.1; -; Genomic_DNA.
DR   RefSeq; WP_004090031.1; NC_004556.1.
DR   AlphaFoldDB; Q87EA7; -.
DR   SMR; Q87EA7; -.
DR   EnsemblBacteria; AAO28290; AAO28290; PD_0410.
DR   GeneID; 58015960; -.
DR   KEGG; xft:PD_0410; -.
DR   HOGENOM; CLU_032540_4_1_6; -.
DR   OMA; KGMHNVE; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002516; 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:InterPro.
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   HAMAP; MF_02208; MurD2_subfam; 1.
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; IPR043687; MurD2.
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..468
FT                   /note="UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase"
FT                   /id="PRO_0000109131"
FT   BINDING         122..128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02208"
SQ   SEQUENCE   468 AA;  49316 MW;  C40C9FFB54841FB0 CRC64;
     MRISALEGCR VALWGWGRES RAAYRAFRAA FPKQPLTLFC TIAEATEVQA LADPVLSIET
     EVSVPRLAAF DVVIKSPGIS PYSPLAVAAT AAGAHFIGGT QLWFAAHADT DGVVPGAVCV
     TGTKGKSTTT ALLAHLLRAA GHCTALAGNI GLPLLELLTP QPAPEYWAIE LSSYQTADVA
     GSGARPALAL VLNVFPEHLD WHGGEQRYIN DKLSLVTVAR PPIALLNAAD PRLASLVLPQ
     SDLRWFNQRD GWHVRGQVVY RGEQAVLDTA LIPLPGAHNG SNVCAVLATL EALGLNAVAL
     APAACNFRPL PNRLQFLGER DGILWVNDSI STTPHATLAA LDCFLGRRRV AVLVGGYDRG
     VNWECFAARI TRKVPLDIVT MGANGPHIQA LLAPLAAGRF GLHAAVDLPH AVALARTALG
     AQGGVLLLSP GAPSFGAYQD YVERGRHFAI LAGFDPEVIS SISGLGIA