ID A5CVB8_CLAM3 Unreviewed; 321 AA. AC A5CVB8; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 105. 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:CAN03057.1}; GN Synonyms=ddl {ECO:0000256|HAMAP-Rule:MF_00047}; GN OrderedLocusNames=CMM_2970 {ECO:0000313|EMBL:CAN03057.1}; OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae; OC Clavibacter. OX NCBI_TaxID=443906 {ECO:0000313|EMBL:CAN03057.1, ECO:0000313|Proteomes:UP000001564}; RN [1] {ECO:0000313|EMBL:CAN03057.1, ECO:0000313|Proteomes:UP000001564} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCPPB 382 {ECO:0000313|EMBL:CAN03057.1, RC ECO:0000313|Proteomes:UP000001564}; RX PubMed=18192381; DOI=10.1128/JB.01595-07; RA Gartemann K.H., Abt B., Bekel T., Burger A., Engemann J., Flugel M., RA Gaigalat L., Goesmann A., Grafen I., Kalinowski J., Kaup O., Kirchner O., RA Krause L., Linke B., McHardy A., Meyer F., Pohle S., Ruckert C., RA Schneiker S., Zellermann E.M., Puhler A., Eichenlaub R., Kaiser O., RA Bartels D.; RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter RT michiganensis subsp. michiganensis NCPPB382 reveals a large island involved RT in pathogenicity."; RL J. Bacteriol. 190:2138-2149(2008). 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; AM711867; CAN03057.1; -; Genomic_DNA. DR RefSeq; WP_012039657.1; NC_009480.1. DR AlphaFoldDB; A5CVB8; -. DR KEGG; cmi:CMM_2970; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_1_0_11; -. DR OrthoDB; 9813261at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000001564; 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:CAN03057.1}; 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}. FT DOMAIN 105..312 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT BINDING 266 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 279 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 279 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 281 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" SQ SEQUENCE 321 AA; 33111 MW; 9164F5CB177CB585 CRC64; MTAHEPLSVL VLAGGISHER DVSLRSGRRV ADALRAAGVQ ASLRDPDATL LDFLRDTPPA VVWPVLHGAS GEDGALLGLL ELAGVPYVGS SARSARLAWD KPTAKAIAES AGIRTPRSVT LPKDTFRELG AAAVLRLVTE AVPAPYAVKP ARGGSAQGVT IVTDAEALPR AMVDAYTYGD VALIEQLVEG TEVAIGILDT GDGPEALPAT EIVPTSGVYG YEARYNAGLT RFFTPARISP DANAAASAAA IGIHRALGIG QMSRVDIIID AAGEPWFIEV NVIPGLTETS LLPQGLAAAG VEVGDLYRRL AEAARGASSG P //