ID DDL_ACAM1 Reviewed; 352 AA. AC B0CEL5; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 86. 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=AM1_3124; OS Acaryochloris marina (strain MBIC 11017). OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales; OC Acaryochloridaceae; Acaryochloris. OX NCBI_TaxID=329726; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MBIC 11017; RX PubMed=18252824; DOI=10.1073/pnas.0709772105; RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., RA Blankenship R.E., Touchman J.W.; RT "Niche adaptation and genome expansion in the chlorophyll d-producing RT cyanobacterium Acaryochloris marina."; RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008). 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; CP000828; ABW28120.1; -; Genomic_DNA. DR RefSeq; WP_012163548.1; NC_009925.1. DR AlphaFoldDB; B0CEL5; -. DR SMR; B0CEL5; -. DR STRING; 329726.AM1_3124; -. DR KEGG; amr:AM1_3124; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_0_0_3; -. DR OrthoDB; 9813261at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000268; 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..352 FT /note="D-alanine--D-alanine ligase" FT /id="PRO_0000341042" FT DOMAIN 133..342 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 169..224 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 295 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 309 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 309 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 311 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" SQ SEQUENCE 352 AA; 38146 MW; 1C6DC84ABC2567CB CRC64; MEKLRVGLVF GGCSGEHEVS ITSAKAVCGA LQTAPNPDKY EVIPFYIHKN GCWQAGEVAN QVLEMGKPQD QAEEGSRWHF PEAAASIDVW FPILHGPNGE DGTIQGLLQL MQVPYVGSGV LGSAAGMDKI AMKTVFAAAG LPQVKYESVT REQVWSDPCV FKQVCDRIDE TIGYPNFVKP ANLGSSVGIS KVRSRLELEA ALDSAASFDR RIVVEAGVVA REVECAVLGN GRPRASVVGE ISFDSDFYDY ETKYTEGRAS LQIPAPLPAD ITEKIQEMAI NAFIAVDAAG LSRVDFFYVE STGEVLINEI NTLPGFTSTS MYPMLWSVSG VDFPKLVDRL IQLAVEYHAP AD //