MURD_STAAU
ID MURD_STAAU Reviewed; 449 AA.
AC P0A091; O07323; O33595;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R27;
RX PubMed=9524242; DOI=10.1016/s0378-1119(98)00059-6;
RA El-Sherbeini M., Geissler W.M., Pittman J., Yuan X., Wong K.K.,
RA Pompliano D.L.;
RT "Cloning and expression of Staphylococcus aureus and Streptococcus pyogenes
RT murD genes encoding uridine diphosphate N-acetylmuramoyl-L-alanine:D-
RT glutamate ligases.";
RL Gene 210:117-125(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8325-4;
RA Pucci M.J., Thanassi J.A., Discotto L.F., Kessler R.E., Dougherty T.J.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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; AF009671; AAC46291.1; -; Genomic_DNA.
DR EMBL; U94706; AAC45626.1; -; Genomic_DNA.
DR PIR; JC6560; JC6560.
DR RefSeq; WP_000935991.1; NZ_WYDB01000002.1.
DR AlphaFoldDB; P0A091; -.
DR SMR; P0A091; -.
DR BindingDB; P0A091; -.
DR ChEMBL; CHEMBL4841; -.
DR OMA; CNFENYL; -.
DR BioCyc; MetaCyc:MON-12256; -.
DR BRENDA; 6.3.2.9; 3352.
DR SABIO-RK; P0A091; -.
DR UniPathway; UPA00219; -.
DR PRO; PR:P0A091; -.
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.
FT CHAIN 1..449
FT /note="UDP-N-acetylmuramoylalanine--D-glutamate ligase"
FT /id="PRO_0000109083"
FT BINDING 118..124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 370..385
FT /note="RAMVVFGQTKAKFAKL -> SREWLYSDSRKLSLLNY (in Ref. 2;
FT AAC45626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 449 AA; 49844 MW; 071BEEE9CF74F985 CRC64;
MLNYTGLENK NVLVVGLAKS GYEAAKLLSK LGANVTVNDG KDLSQDAHAK DLESMGISVV
SGSHPLTLLD NNPIIVKNPG IPYTVSIIDE AVKRGLKILT EVELSYLISE APIIAVTGTN
GKTTVTSLIG DMFKKSRLTG RLSGNIGYVA SKVAQEVKPT DYLVTELSSF QLLGIEKYKP
HIAIITNIYS AHLDYHENLE NYQNAKKQIY KNQTEEDYLI CNYHQRQVIE SEELKAKTLY
FSTQQEVDGI YIKDGFIVYK GVRIINTEDL VLPGEHNLEN ILAAVLACIL AGVPIKAIID
SLTTFSGIEH RLQYVGTNRT NKYYNDSKAT NTLATQFALN SFNQPIIWLC GGLDRGNEFD
ELIPYMENVR AMVVFGQTKA KFAKLGNSQG KSVIEANNVE DAVDKVQDII EPNDVVLLSP
ACASWDQYST FEERGEKFIE RFRAHLPSY