ID   MURD_MYCTA              Reviewed;         496 AA.
AC   A5U4I2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 2.
DT   03-AUG-2022, entry version 93.
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=MRA_2170;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
RN   [2]
RP   INTERACTION WITH PKNA, AND PHOSPHORYLATION.
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18557704; DOI=10.1042/bj20080234;
RA   Thakur M., Chakraborti P.K.;
RT   "Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase,
RT   to transphosphorylate MurD, a ligase involved in the process of
RT   peptidoglycan biosynthesis.";
RL   Biochem. J. 415:27-33(2008).
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   -!- SUBUNIT: Interacts with PknA. {ECO:0000269|PubMed:18557704}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00639}.
CC   -!- PTM: Phosphorylated by PknA. {ECO:0000269|PubMed:18557704}.
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000255|HAMAP-
CC       Rule:MF_00639}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABQ73932.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000250|UniProtKB:P9WJL5};
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DR   EMBL; CP000611; ABQ73932.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A5U4I2; -.
DR   SMR; A5U4I2; -.
DR   STRING; 419947.MRA_2170; -.
DR   EnsemblBacteria; ABQ73932; ABQ73932; MRA_2170.
DR   KEGG; mra:MRA_2170; -.
DR   eggNOG; COG0771; Bacteria.
DR   HOGENOM; CLU_032540_0_0_11; -.
DR   BRENDA; 6.3.2.9; 3445.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001988; 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   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Cell shape;
KW   Cell wall biogenesis/degradation; Cytoplasm; Ligase; Nucleotide-binding;
KW   Peptidoglycan synthesis; Phosphoprotein.
FT   CHAIN           1..496
FT                   /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT                   /id="PRO_0000301440"
FT   BINDING         130..136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00639"
SQ   SEQUENCE   496 AA;  50354 MW;  9E9F0B30A7FA358A CRC64;
     MSGLPRSVPD VLDPLGPGAP VLVAGGRVTG QAVAAVLTRF GATPTVCDDD PVMLRPHAER
     GLPTVSSSDA VQQITGYALV VASPGFSPAT PLLAAAAAAG VPIWGDVELA WRLDAAGCYG
     PPRSWLVVTG TNGKTTTTSM LHAMLIAGGR RAVLCGNIGS AVLDVLDEPA ELLAVELSSF
     QLHWAPSLRP EAGAVLNIAE DHLDWHATMA EYTAAKARVL TGGVAVAGLD DSRAAALLDG
     SPAQVRVGFR LGEPAARELG VRDAHLVDRA FSDDLTLLPV ASIPVPGPVG VLDALAAAAL
     ARSVGVPAGA IADAVTSFRV GRHRAEVVAV ADGITYVDDS KATNPHAARA SVLAYPRVVW
     IAGGLLKGAS LHAEVAAMAS RLVGAVLIGR DRAAVAEALS RHAPDVPVVQ VVAGEDTGMP
     ATVEVPVACV LDVAKDDKAG ETVGAAVMTA AVAAARRMAQ PGDTVLLAPA GASFDQFTGY
     ADRGEAFATA VRAVIR