ID   MURD2_XANC8             Reviewed;         468 AA.
AC   Q4UWX9;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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=XC_1375;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA   Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA   Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
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; CP000050; AAY48444.1; -; Genomic_DNA.
DR   RefSeq; WP_011037868.1; NC_007086.1.
DR   AlphaFoldDB; Q4UWX9; -.
DR   SMR; Q4UWX9; -.
DR   EnsemblBacteria; AAY48444; AAY48444; XC_1375.
DR   KEGG; xcb:XC_1375; -.
DR   HOGENOM; CLU_032540_4_1_6; -.
DR   OMA; KGMHNVE; -.
DR   OrthoDB; 1093223at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000420; 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: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; 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; 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_0000109128"
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;  49585 MW;  4DAA13293AC32B25 CRC64;
     MRISQLEGKA VALWGWAREG RAAYRALRQQ LPAQPLTVFC NAEEARDVAA LADPALQVQT
     EASAQALAAF EVVIKSPGIS PYREEARAAA AQGARFIGGT ALWFAEHAQP DGYVPGAICV
     TGTKGKSTTT ALLAHLLRAD GHRTALVGNI GQPLLEVLSP QPPPAYWAIE LSSYQTGEVG
     RSGARPELAL VLNLFPEHLD WHGSEAAYVR DKLALVTDGR PRIALLNAAD PHLAQLQLPE
     SEVRWFNHPD GWHLRGDVVY RGQQPIFDTA NVPLPGEHNR RNLCAVLAAV EALGLDAAAL
     APAALTFRPL PNRLQWLGSV DGIAYVNDSI STTPHASLAA LACFAQQRVA LLVGGHDRGL
     DWQEFAAHMA QQAPLEIVTM GANGPRIHAL LAPLAQSAGF GLHAADDLAH AMQLARSALG
     AQGGVLLLSP GAPSFGVYSD YVARGRHFAQ LAGFDPAAIS AIPGLGVQ