ID Q6WRY5_ENTFL Unreviewed; 349 AA. AC Q6WRY5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 137. DE RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047}; DE EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047}; DE AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047}; DE AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047}; GN Name=vanG {ECO:0000313|EMBL:AAQ16273.1}; GN Synonyms=ddl {ECO:0000256|HAMAP-Rule:MF_00047}; OS Enterococcus faecalis (Streptococcus faecalis). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; OC Enterococcus. OX NCBI_TaxID=1351 {ECO:0000313|EMBL:AAQ16273.1}; RN [1] {ECO:0000313|EMBL:AAQ16273.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BM4518 {ECO:0000313|EMBL:AAQ16273.1}; RX PubMed=14617152; DOI=10.1046/j.1365-2958.2003.03737.x; RA Depardieu F., Bonora M.G., Reynolds P.E., Courvalin P.; RT "The vanG glycopeptide resistance operon from Enterococcus faecalis RT revisited."; RL Mol. Microbiol. 50:931-948(2003). RN [2] {ECO:0000313|EMBL:ABA71731.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=G1-01247 {ECO:0000313|EMBL:ABA71731.1}; RX PubMed=16723588; DOI=10.1128/AAC.01541-05; RA Boyd D.A., Du T., Hizon R., Kaplen B., Murphy T., Tyler S., Brown S., RA Jamieson F., Weiss K., Mulvey M.R.; RT "VanG-type vancomycin-resistant Enterococcus faecalis strains isolated in RT Canada."; RL Antimicrob. Agents Chemother. 50:2217-2221(2006). RN [3] {ECO:0007829|PDB:4FU0} RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH ADP. RX PubMed=22969085; DOI=10.1074/jbc.M112.405522; RA Meziane-Cherif D., Saul F.A., Haouz A., Courvalin P.; RT "Structural and functional characterization of VanG D-Ala:D-Ser ligase RT associated with vancomycin resistance in Enterococcus faecalis."; RL J. Biol. Chem. 287:37583-37592(2012). CC -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) + CC phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416, CC ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00047}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR039102-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR039102-3}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000256|PIRSR:PIRSR039102-3}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00047}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047}. CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family. CC {ECO:0000256|ARBA:ARBA00010871, ECO:0000256|HAMAP-Rule:MF_00047}. 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; AY271782; AAQ16273.1; -; Genomic_DNA. DR EMBL; DQ212986; ABA71731.1; -; Genomic_DNA. DR RefSeq; WP_021418924.1; NG_048369.1. DR PDB; 4FU0; X-ray; 2.35 A; A/B=1-349. DR PDBsum; 4FU0; -. DR BioCyc; MetaCyc:MONOMER-15480; -. DR UniPathway; UPA00219; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IDA:CACAO. DR GO; GO:0046872; F:metal ion binding; 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; 3.40.50.20; -; 1. DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR HAMAP; MF_00047; Dala_Dala_lig; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR000291; D-Ala_lig_Van_CS. DR InterPro; IPR005905; D_ala_D_ala. DR InterPro; IPR011095; Dala_Dala_lig_C. DR InterPro; IPR011127; Dala_Dala_lig_N. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1. DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1. DR PANTHER; PTHR23132:SF25; D-ALANINE--D-ALANINE LIGASE A; 1. DR Pfam; PF07478; Dala_Dala_lig_C; 1. DR Pfam; PF01820; Dala_Dala_lig_N; 1. DR PIRSF; PIRSF039102; Ddl/VanB; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00843; DALA_DALA_LIGASE_1; 1. DR PROSITE; PS00844; DALA_DALA_LIGASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:4FU0}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_00047}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00047}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00047}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR039102-3}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR039102-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR039102-3}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00047}. FT DOMAIN 144..345 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT BINDING 140 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4FU0" FT BINDING 181 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4FU0" FT BINDING 183 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4FU0" FT BINDING 190 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4FU0" FT BINDING 219 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4FU0" FT BINDING 220 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4FU0" FT BINDING 222 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4FU0" FT BINDING 226 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4FU0" FT BINDING 261 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4FU0" FT BINDING 299 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 311 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0007829|PDB:4FU0" FT BINDING 312 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 312 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 314 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" SQ SEQUENCE 349 AA; 38730 MW; 458EABDDF90493FD CRC64; MQNKKIAVIF GGNSTEYEVS LQSASAVFEN INTNKFDIIP IGITRSGEWY HYTGEKEKIL NNTWFEDSKN LCPVVVSQNR SVKGFLEIAS DKYRIIKVDL VFPVLHGKNG EDGTLQGIFE LAGIPVVGCD TLSSALCMDK DRAHKLVSLA GISVPKSVTF KRFNEEAAMK EIEANLTYPL FIKPVRAGSS FGITKVIEKQ ELDAAIELAF EHDTEVIVEE TINGFEVGCA VLGIDELIVG RVDEIELSSG FFDYTEKYTL KSSKIYMPAR IDAEAEKRIQ EAAVTIYKAL GCSGFSRVDM FYTPSGEIVF NEVNTIPGFT SHSRYPNMMK GIGLSFSQML DKLIGLYVE //