ID C7R3N7_JONDD Unreviewed; 319 AA. AC C7R3N7; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 27-MAR-2024, entry version 83. DE RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047}; DE EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047}; DE AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047}; DE AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047}; GN Name=ddl {ECO:0000256|HAMAP-Rule:MF_00047}; GN OrderedLocusNames=Jden_2550 {ECO:0000313|EMBL:ACV10182.1}; OS Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / BCRC 15368 / CIP OS 55.134 / JCM 11481 / NBRC 15587 / NCTC 10816 / Prevot 55134) (Listeria OS denitrificans). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Jonesiaceae; OC Jonesia. OX NCBI_TaxID=471856 {ECO:0000313|EMBL:ACV10182.1, ECO:0000313|Proteomes:UP000000628}; RN [1] {ECO:0000313|EMBL:ACV10182.1, ECO:0000313|Proteomes:UP000000628} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 14870 / DSM 20603 / BCRC 15368 / CIP 55.134 / JCM 11481 / RC NBRC 15587 / NCTC 10816 / Prevot 55134 RC {ECO:0000313|Proteomes:UP000000628}; RX PubMed=21304666; DOI=10.4056/sigs.41646; RA Pukall R., Gehrich-Schroter G., Lapidus A., Nolan M., Glavina Del Rio T., RA Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F., Copeland A., RA Saunders E., Brettin T., Detter J.C., Bruce D., Goodwin L., Pati A., RA Ivanova N., Mavromatis K., Ovchinnikova G., Chen A., Palaniappan K., RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Goker M., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Han C.; RT "Complete genome sequence of Jonesia denitrificans type strain (Prevot RT 55134)."; RL Stand. Genomic Sci. 1:262-269(2009). CC -!- FUNCTION: Cell wall formation. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00047}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR039102-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR039102-3}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000256|PIRSR:PIRSR039102-3}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00047}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047}. CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family. CC {ECO:0000256|ARBA:ARBA00010871, ECO:0000256|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; CP001706; ACV10182.1; -; Genomic_DNA. DR RefSeq; WP_015772793.1; NC_013174.1. DR AlphaFoldDB; C7R3N7; -. DR STRING; 471856.Jden_2550; -. DR KEGG; jde:Jden_2550; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_1_0_11; -. DR OrthoDB; 9813261at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000628; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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; IPR005905; D_ala_D_ala. DR InterPro; IPR011095; Dala_Dala_lig_C. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1. DR PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1. DR Pfam; PF07478; Dala_Dala_lig_C; 1. DR PIRSF; PIRSF039102; Ddl/VanB; 2. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF52440; PreATP-grasp domain; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409}; KW Cell shape {ECO:0000256|HAMAP-Rule:MF_00047}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00047}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000313|EMBL:ACV10182.1}; KW Magnesium {ECO:0000256|PIRSR:PIRSR039102-3}; KW Manganese {ECO:0000256|PIRSR:PIRSR039102-3}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR039102-3}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}; KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00047}; KW Reference proteome {ECO:0000313|Proteomes:UP000000628}. FT DOMAIN 103..308 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT BINDING 262 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 275 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 275 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 277 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" SQ SEQUENCE 319 AA; 33829 MW; 020344C07DE0B491 CRC64; MSSHPFVVIL AGGLSHERDV SLRSGRRVAE ALRSTGMTVS VVDVDAQLLP RLQSHRPDLV WPLLHGASGE DGSIRDVLEL LDLPYLGTRP RESRVAWNKP VAKAVLAAAG VLTPSYVTLP QSLFRELGAR SVMEPVTAKL GLPLVVKPAQ GGSALGVTLV TSAEQLPQAL VDCFAYGDLA LIEEAITGTE VSVSVVESPD VTALPAVEII TDGPYDYDAR YNPGRTQYFT PARLDPEIAD AAARVALTAH TTLGLRHVSR SDLIIDGKGQ VWFLEVNVAP GMTETSLLPQ AVVASGQSLP DAYSSWVRAA LVVADSAAQ //