MURD_ENTFA
ID MURD_ENTFA Reviewed; 456 AA.
AC O07108;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 135.
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=EF_0993;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A24836;
RX PubMed=9287029; DOI=10.1128/jb.179.17.5632-5635.1997;
RA Pucci M.J., Thanassi J.A., Discotto L.F., Kessler R.E., Dougherty T.J.;
RT "Identification and characterization of cell wall-cell division gene
RT clusters in pathogenic Gram-positive cocci.";
RL J. Bacteriol. 179:5632-5635(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U94707; AAC45635.1; -; Genomic_DNA.
DR EMBL; AE016830; AAO80799.1; -; Genomic_DNA.
DR RefSeq; NP_814729.1; NC_004668.1.
DR RefSeq; WP_002379203.1; NZ_KE136527.1.
DR AlphaFoldDB; O07108; -.
DR SMR; O07108; -.
DR STRING; 226185.EF_0993; -.
DR EnsemblBacteria; AAO80799; AAO80799; EF_0993.
DR KEGG; efa:EF0993; -.
DR PATRIC; fig|226185.45.peg.3199; -.
DR eggNOG; COG0771; Bacteria.
DR HOGENOM; CLU_032540_0_1_9; -.
DR OMA; CNFENYL; -.
DR SABIO-RK; O07108; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001415; 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 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..456
FT /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT /id="PRO_0000109010"
FT BINDING 119..125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 83
FT /note="P -> L (in Ref. 1; AAC45635)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="N -> D (in Ref. 1; AAC45635)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="A -> P (in Ref. 1; AAC45635)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="R -> K (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="T -> S (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 336
FT /note="I -> F (in Ref. 1; AAC45635)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="E -> K (in Ref. 1; AAC45635)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="A -> P (in Ref. 1; AAC45635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 456 AA; 49698 MW; DB4E0B9B5514A88D CRC64;
MKKITTYQNK KVLVLGLAKS GVSAAKLLHE LGALVTVNDA KQFDQNPDAQ DLLTLGIRVV
TGGHPIELLD EEFELIVKNP GIPYTNPLVA EALTRKIPII TEVELAGQIA ECPIVGITGT
NGKTTTTTMI GLLLNADRTA GEARLAGNIG FPASTVAQEA TAKDNLVMEL SSFQLMGIET
FHPQIAVITN IFEAHLDYHG SRKEYVAAKW AIQKNMTAED TLILNWNQVE LQTLAKTTAA
NVLPFSTKEA VEGAYLLDGK LYFNEEYIMP ADELGIPGSH NIENALAAIC VAKLKNVSNA
QIRQTLTNFS GVPHRTQFVG EVQQRRFYND SKATNILATE MALSGFDNQK LLLLAGGLDR
GNSFDELVPA LLGLKAIVLF GETKEKLAEA AKKANIETIL FAENVQTAVT IAFDYSEKDD
TILLSPACAS WDQYPNFEVR GEAFMQAVQQ LKESEM
