ID DDL_SOLUE Reviewed; 325 AA. AC Q023Q5; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 99. 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=Acid_2799; OS Solibacter usitatus (strain Ellin6076). OC Bacteria; Acidobacteriota; Terriglobia; Bryobacterales; Solibacteraceae; OC Solibacter. OX NCBI_TaxID=234267; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Ellin6076; RX PubMed=19201974; DOI=10.1128/aem.02294-08; RA Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M., RA Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B., RA Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C., RA Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S., RA Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P., RA Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q., RA Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R., RA Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.; RT "Three genomes from the phylum Acidobacteria provide insight into the RT lifestyles of these microorganisms in soils."; RL Appl. Environ. Microbiol. 75:2046-2056(2009). 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; CP000473; ABJ83785.1; -; Genomic_DNA. DR AlphaFoldDB; Q023Q5; -. DR SMR; Q023Q5; -. DR STRING; 234267.Acid_2799; -. DR KEGG; sus:Acid_2799; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_0_0_0; -. DR InParanoid; Q023Q5; -. DR OrthoDB; 9813261at2; -. DR UniPathway; UPA00219; -. 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:SF25; D-ALANINE--D-ALANINE LIGASE A; 1. DR Pfam; PF07478; Dala_Dala_lig_C; 1. DR Pfam; PF01820; Dala_Dala_lig_N; 2. 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. FT CHAIN 1..325 FT /note="D-alanine--D-alanine ligase" FT /id="PRO_1000057330" FT DOMAIN 109..309 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 136..191 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 262 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 276 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 276 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 278 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" SQ SEQUENCE 325 AA; 36542 MW; 9898F006460438CD CRC64; MKLRVAVIYG GRTGEHEVSV RSAKSILAGL DCEKYETIEY FIDQNGKWSP GPILPEPGAH ANIDVVFPVL HGTFGEDGTV QGLLELADLP YVGAGVLGSA VSMDKEMMKR VCKERMLPIV DYVTVTRQTP SIVDACRRLP FPMFVKPANL GSSVGISKAH DEQELEAAFS LAKQYDRKII VERGIEGREL ECSVLGNEAP MASLPCEILP SREFYDYEDK YLLDMARTQV PADLPGERTD EIRRLAVECY RAVECEGMAR VDFFLEHGTN RLYINEINTI PGFTSISMYP KMWEHSGIPF CTLLDQLIEF ALDRHRQKQV TRFAR //