ID DDL_BURP0 Reviewed; 312 AA. AC A3NZL3; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, 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=BURPS1106A_3548; OS Burkholderia pseudomallei (strain 1106a). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=357348; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1106a; RX PubMed=20333227; DOI=10.1093/gbe/evq003; RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S., RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J., RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P., RA Nierman W.C.; RT "Continuing evolution of Burkholderia mallei through genome reduction and RT large-scale rearrangements."; RL Genome Biol. Evol. 2:102-116(2010). 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; CP000572; ABN90443.1; -; Genomic_DNA. DR RefSeq; WP_004194254.1; NC_009076.1. DR PDB; 5NRH; X-ray; 1.30 A; A/B=1-312. DR PDB; 5NRI; X-ray; 1.50 A; A/B=1-312. DR PDBsum; 5NRH; -. DR PDBsum; 5NRI; -. DR AlphaFoldDB; A3NZL3; -. DR SMR; A3NZL3; -. DR GeneID; 56594282; -. DR KEGG; bpl:BURPS1106A_3548; -. DR HOGENOM; CLU_039268_1_2_4; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000006738; Chromosome I. 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. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell shape; Cell wall biogenesis/degradation; KW Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding; KW Peptidoglycan synthesis. FT CHAIN 1..312 FT /note="D-alanine--D-alanine ligase" FT /id="PRO_0000341075" FT DOMAIN 108..308 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 138..193 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 275 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 275 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 277 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT HELIX 6..9 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 11..15 FT /evidence="ECO:0007829|PDB:5NRI" FT HELIX 23..39 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 43..47 FT /evidence="ECO:0007829|PDB:5NRI" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:5NRI" FT HELIX 56..59 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:5NRI" FT HELIX 72..74 FT /evidence="ECO:0007829|PDB:5NRI" FT HELIX 78..85 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:5NRI" FT HELIX 95..101 FT /evidence="ECO:0007829|PDB:5NRI" FT HELIX 104..113 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 121..125 FT /evidence="ECO:0007829|PDB:5NRI" FT HELIX 130..141 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 145..151 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:5NRI" FT HELIX 164..166 FT /evidence="ECO:0007829|PDB:5NRI" FT HELIX 167..177 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 179..185 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 189..198 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 206..209 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 211..215 FT /evidence="ECO:0007829|PDB:5NRI" FT HELIX 217..221 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 227..231 FT /evidence="ECO:0007829|PDB:5NRI" FT HELIX 236..252 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 257..266 FT /evidence="ECO:0007829|PDB:5NRI" FT STRAND 271..279 FT /evidence="ECO:0007829|PDB:5NRI" FT HELIX 287..293 FT /evidence="ECO:0007829|PDB:5NRI" FT TURN 294..296 FT /evidence="ECO:0007829|PDB:5NRI" FT HELIX 299..308 FT /evidence="ECO:0007829|PDB:5NRI" SQ SEQUENCE 312 AA; 33341 MW; CCD89397BEAE5E22 CRC64; MSGIDPKRFG KVAVLLGGDS AEREVSLNSG RLVLQGLRDA GIDAHPFDPA QRPLAALKDE GFVRAFNALH GGYGENGQIQ GALDFYGIRY TGSGVLGSAL GLDKFRTKLV WQQTGIPTPP FETVMRGDDY AARAQDIVAK LGVPLFVKPA SEGSSVAVEK VKSADALPAA LEEAAKHDKI VIVEKSIEGG GEYTACIAAD LDLPLIRIVP AGEFYDYHAK YIANDTQYLI PCGLDAAKEA EFKRIARRAF DVLGCTDWGR ADFMLDAAGN PYFLEVNTAP GMTDHSLPPK AARAVGIGYS ELVVKVLSLT LD //