ID DDL_CAUVC Reviewed; 324 AA. AC Q9A5A9; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=D-alanine--D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00047}; DE EC=6.3.2.4 {ECO:0000255|HAMAP-Rule:MF_00047}; DE AltName: Full=D-Ala-D-Ala ligase {ECO:0000255|HAMAP-Rule:MF_00047}; DE AltName: Full=D-alanylalanine synthetase {ECO:0000255|HAMAP-Rule:MF_00047}; GN Name=ddl {ECO:0000255|HAMAP-Rule:MF_00047}; OrderedLocusNames=CC_2543; OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=190650; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 19089 / CB15; RX PubMed=11259647; DOI=10.1073/pnas.061029298; RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E., RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R., RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B., RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F., RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R., RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O., RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.; RT "Complete genome sequence of Caulobacter crescentus."; RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001). CC -!- FUNCTION: Cell wall formation. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00047}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00047}. CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family. CC {ECO:0000255|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; AE005673; AAK24514.1; -; Genomic_DNA. DR PIR; F87564; F87564. DR RefSeq; NP_421346.1; NC_002696.2. DR RefSeq; WP_010920400.1; NC_002696.2. DR AlphaFoldDB; Q9A5A9; -. DR SMR; Q9A5A9; -. DR STRING; 190650.CC_2543; -. DR EnsemblBacteria; AAK24514; AAK24514; CC_2543. DR KEGG; ccr:CC_2543; -. DR PATRIC; fig|190650.5.peg.2557; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_1_1_5; -. DR BioCyc; CAULO:CC2543-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000001816; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule. 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:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 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 3: Inferred from homology; KW ATP-binding; Cell shape; Cell wall biogenesis/degradation; Cytoplasm; KW Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; KW Peptidoglycan synthesis; Reference proteome. FT CHAIN 1..324 FT /note="D-alanine--D-alanine ligase" FT /id="PRO_0000177802" FT DOMAIN 112..312 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 139..193 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 265 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 279 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 279 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 281 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" SQ SEQUENCE 324 AA; 34110 MW; FBEA46FFED71FC2E CRC64; MTQQPQADAP LAGRHIAVLL GGPSSERKVS LVSGAACAEA LERLGAKVSR IDPGPDVAQV LAATKPDMVF NALHGEWGED GCVQGVLETL KLPYTHSGVL ASALAMDKAK AKAVLAAAGV TVPGGGLFNR HDVARDHVLQ PPYVVKPNAE GSSVGVFIIK EGANRPPEEV GAPSWTFGEE VMVEPYIQGM ELAVAVLGES NGPRALAVTD IRASTGFYDY EAKYSEGGSI HVLPAPIPNA VRDRAMRMAE LAHTALGCRG VTRSDFRYDD INDLLVLLEV NTQPGMTPTS LAPEQADHVG IPFDQLVLWI VEDAYARCSA GGTA //