ID DDL_BIFLO Reviewed; 428 AA. AC Q8G7C4; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 119. 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}; Synonyms=ddlA; GN OrderedLocusNames=BL0345; OS Bifidobacterium longum (strain NCC 2705). OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales; OC Bifidobacteriaceae; Bifidobacterium. OX NCBI_TaxID=206672; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCC 2705; RX PubMed=12381787; DOI=10.1073/pnas.212527599; RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.; RT "The genome sequence of Bifidobacterium longum reflects its adaptation to RT the human gastrointestinal tract."; RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002). 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; AE014295; AAN24184.1; -; Genomic_DNA. DR RefSeq; NP_695548.1; NC_004307.2. DR AlphaFoldDB; Q8G7C4; -. DR SMR; Q8G7C4; -. DR STRING; 206672.BL0345; -. DR EnsemblBacteria; AAN24184; AAN24184; BL0345. DR KEGG; blo:BL0345; -. DR PATRIC; fig|206672.9.peg.1082; -. DR HOGENOM; CLU_039268_0_0_11; -. DR OrthoDB; 9813261at2; -. DR PhylomeDB; Q8G7C4; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000439; 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: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 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..428 FT /note="D-alanine--D-alanine ligase" FT /id="PRO_0000177787" FT DOMAIN 205..424 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 237..299 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 378 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 391 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 391 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 393 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" SQ SEQUENCE 428 AA; 46045 MW; D501772E024C8F46 CRC64; MRLLCAAFRA RFGPVGGAKH RLENGCSFNK RMVMAKKRVV VLYGGRADEH SISCISTAGV LGAMDTERFE PIPVGITKDG KWIINGEDPR GWNLDGGELP TVKITPESRP VMLDPSRGQD GFFIGEPSHI NSADSGFGTS FVSMSDPEMH HVLTSLGHVD AVLPVLHGPY GEDGTVQGLL EMMGVPYVGC GVFASAACMD KHYTKVVLDA AGIPTAPGVT VDARNFTAAD VLAEIEDAGL TYPLFVKPSR AGSSFGVTKV EKADDRETQQ DRLAAAIATA GEHDWKVLVE QGIDGREIEC AVLCPKAGDE PEASWPGEIV LDHQNDDQFY DFDSKYMDAS ASHVEVPANL PVSVLEDVRD VARRAFKAVD GAGLSRVDTF VTPDGTVMVN EINTMPGFTP ISMYPKAWDA TGVSYTELIT RLIEGVLR //