ID H6RW11_BLASD Unreviewed; 331 AA. AC H6RW11; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 27-MAR-2024, entry version 70. 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=ddlB {ECO:0000313|EMBL:CCG05841.1}; GN Synonyms=ddl {ECO:0000256|HAMAP-Rule:MF_00047}; GN OrderedLocusNames=BLASA_5068 {ECO:0000313|EMBL:CCG05841.1}; OS Blastococcus saxobsidens (strain DD2). OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales; OC Geodermatophilaceae; Blastococcus. OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG05841.1, ECO:0000313|Proteomes:UP000007517}; RN [1] {ECO:0000313|EMBL:CCG05841.1, ECO:0000313|Proteomes:UP000007517} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD2 {ECO:0000313|EMBL:CCG05841.1, RC ECO:0000313|Proteomes:UP000007517}; RX PubMed=22535935; DOI=10.1128/JB.00320-12; RA Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I., RA Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C., RA Gury J., Pujic P., Normand P.; RT "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting RT Bacterium."; RL J. Bacteriol. 194:2752-2753(2012). RN [2] {ECO:0000313|Proteomes:UP000007517} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517}; RA Genoscope.; RT "Complete genome sequence of Blastococcus saxobsidens strain DD2."; RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases. 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; FO117623; CCG05841.1; -; Genomic_DNA. DR RefSeq; WP_014378700.1; NC_016943.1. DR AlphaFoldDB; H6RW11; -. DR STRING; 1146883.BLASA_5068; -. DR KEGG; bsd:BLASA_5068; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_1_0_11; -. DR OrthoDB; 9813261at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000007517; 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; IPR011127; Dala_Dala_lig_N. 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 Pfam; PF01820; Dala_Dala_lig_N; 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:CCG05841.1}; 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:UP000007517}. FT DOMAIN 117..324 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT BINDING 278 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 291 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 291 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 293 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" SQ SEQUENCE 331 AA; 34138 MW; 6BECC89154866A23 CRC64; MSETAPAPDT TGGTAPHPLR AVVLAGGLTF EREVSLSSGT QVVEELTRAG LDAELRDADA ELLPGLAAAP ADAVFIALHG ATGEDGALRA VLDLAGVPYV GSPAAACRLA WDKPAAKSVV RSAAVTTPDW VALPHSTFRE LGAGAVLDLM VARLGLPLMV KPASGGSALG VQKVSRVEDL PAAMVSCFAY GDTVMVERFV EGVELAIAVV DLGDGPEALP AVEIEPESGV FDYASRYTPG LTEYHAPARI PDETAARAAE VAVRVHQVLG LADLSRTDAI VTPDGEVHFL EVNVSPGLTE TSMFPMAVEA AGHELGDVLA RLLARRASAG R //