ID DDL_POLAQ Reviewed; 337 AA. AC A4SV76; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 27-MAR-2024, entry version 102. 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}; GN OrderedLocusNames=Pnuc_0169; OS Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 / OS QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Polynucleobacter. OX NCBI_TaxID=312153; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1; RX PubMed=22675600; DOI=10.4056/sigs.2395367; RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G., RA Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D., RA Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T., RA Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M., RA Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.; RT "Complete genome sequence of Polynucleobacter necessarius subsp. RT asymbioticus type strain (QLW-P1DMWA-1(T))."; RL Stand. Genomic Sci. 6:74-83(2012). 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; CP000655; ABP33390.1; -; Genomic_DNA. DR RefSeq; WP_011902015.1; NC_009379.1. DR AlphaFoldDB; A4SV76; -. DR SMR; A4SV76; -. DR GeneID; 31480518; -. DR KEGG; pnu:Pnuc_0169; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_1_2_4; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000231; 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:SF23; D-ALANINE--D-ALANINE LIGASE B; 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. 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..337 FT /note="D-alanine--D-alanine ligase" FT /id="PRO_0000341152" FT DOMAIN 126..326 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 152..207 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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 293 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 293 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 295 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" SQ SEQUENCE 337 AA; 36228 MW; A117462B500868D3 CRC64; MSKQEELLIQ WGDRVKACLA NLDIKSLGRV GVLLGGRSGE REISLMSGNG VLQALLSKGV DAHGFDPGLR NPTELATEKF DRIFISLHGR FGEDGTIQGL LELLELPYTG SGVLASALAI DKIATKQIWI SNGLSTPEYE ELTAKSDWNA VVKHLGLPLI VKPAHEGSSL GLTKVKSVEE LPAAYQLAAG LDKKVIAETC IVGDELTCPL VGQGNSAEAL PVIKIIPPQA NYDFHNKYFS DETQYLCPTG LTAEINAAVQ DLALAAYQTL GCRTWGRADV MLDKKTGKPY LLEMNTSPGM TSHSLVPMAA KAAGVEYADL VLWLLSQTLL QKEGART //