ID DDL_PSEPF Reviewed; 324 AA. AC Q3K746; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 08-NOV-2005, sequence version 1. DT 27-MAR-2024, entry version 118. 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=Pfl01_4671; OS Pseudomonas fluorescens (strain Pf0-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=205922; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Pf0-1; RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51; RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R., RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M., RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J., RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L., RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K., RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M., RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.; RT "Genomic and genetic analyses of diversity and plant interactions of RT Pseudomonas fluorescens."; RL Genome Biol. 10:R51.1-R51.16(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; CP000094; ABA76408.1; -; Genomic_DNA. DR RefSeq; WP_007956758.1; NC_007492.2. DR AlphaFoldDB; Q3K746; -. DR SMR; Q3K746; -. DR KEGG; pfo:Pfl01_4671; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_1_2_6; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000002704; 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. DR PROSITE; PS00844; DALA_DALA_LIGASE_2; 1. DR World-2DPAGE; 0008:Q3K746; -. 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..324 FT /note="D-alanine--D-alanine ligase" FT /id="PRO_1000030486" FT DOMAIN 116..311 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 142..197 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 278 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" 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" FT BINDING 280 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; 34373 MW; B86436D8182D1BC3 CRC64; MTAAYANLFS TIAPKDFGRV AVLFGGLSAE REVSLKSGNA VLTALQSAGV DAFGIDVGAD ILQRLLSEKI DRAFIILHGR GGEDGSMQGL LEVAGIPYTG SGILASALAM DKLRTKQVWH TLGIPTPRHA VLRSEADCIS AATELGFPLI VKPAHEGSSI GMAKVSSASE LIDAWKAAST YDSQVLVEQW IHGPEFTIAT LRDQVLPPIA LGTPHTFYDY DAKYIANDTQ YRIPCGLDAA KEKELMDLTA QACEALGIAG WGRADVMQDA DGKFWFLEVN TAPGMTDHSL VPMAAKAAGL DFQQLVLAIL AASVDADGKK EARG //