ID D9QA17_CORP2 Unreviewed; 363 AA. AC D9QA17; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAR-2024, entry version 78. 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 ORFNames=CPC231_04600 {ECO:0000313|EMBL:ADL10393.1}; OS Corynebacterium pseudotuberculosis (strain C231). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; OC Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL10393.1, ECO:0000313|Proteomes:UP000000276}; RN [1] {ECO:0000313|EMBL:ADL10393.1, ECO:0000313|Proteomes:UP000000276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C231 {ECO:0000313|EMBL:ADL10393.1, RC ECO:0000313|Proteomes:UP000000276}; RX PubMed=21037006; DOI=.1128/JB.01211-10; RG Consortium: Rede Paraense de Genomica e Proteomica (RPGP); RA Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T., RA Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S., RA Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F., RA de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.; RT "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a RT strain isolated from a cow in Israel with bovine mastitis."; RL J. Bacteriol. 193:323-324(2011). RN [2] {ECO:0000313|EMBL:ADL10393.1, ECO:0000313|Proteomes:UP000000276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C231 {ECO:0000313|EMBL:ADL10393.1, RC ECO:0000313|Proteomes:UP000000276}; RX PubMed=21533164; DOI=10.1371/journal.pone.0018551; RA Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R., RA Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., Turk M.Z., RA Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., Castro T.L., RA Abreu V.A., Trost E., Baumbach J., Tauch A., Schneider M.P., McCulloch J., RA Cerdeira L.T., Ramos R.T., Zerlotini A., Dominitini A., Resende D.M., RA Coser E.M., Oliveira L.M., Pedrosa A.L., Vieira C.U., Guimaraes C.T., RA Bartholomeu D.C., Oliveira D.M., Santos F.R., Rabelo E.M., Lobo F.P., RA Franco G.R., Costa A.F., Castro I.M., Dias S.R., Ferro J.A., Ortega J.M., RA Paiva L.V., Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P., RA Falcao P.R., Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C., RA Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.; RT "Evidence for reductive genome evolution and lateral acquisition of RT virulence functions in two Corynebacterium pseudotuberculosis strains."; RL PLoS ONE 6:E18551-E18551(2011). 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 -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; 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; CP001829; ADL10393.1; -; Genomic_DNA. DR RefSeq; WP_013241771.1; NC_017301.2. DR AlphaFoldDB; D9QA17; -. DR STRING; 681645.CpC231_0914; -. DR GeneID; 69459875; -. DR KEGG; cpq:CPC231_04600; -. DR PATRIC; fig|681645.3.peg.953; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_0_1_11; -. DR OrthoDB; 9813261at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000000276; 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; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW 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|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00047}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR039102-3}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR039102-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR039102-3}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00047}; Reference proteome {ECO:0000313|Proteomes:UP000000276}. FT DOMAIN 154..358 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT BINDING 313 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 325 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 325 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 327 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" SQ SEQUENCE 363 AA; 39320 MW; 07125E0F62D5499D CRC64; MCVVTQKPSP NPRVRVAVVY GGQSSEHSVS CVSAGAIMSH LDPQKYEVFP VGITRDGVWT VGESDATKLR TVDRVMPEVE FVREVKLSVN PRSAGEFRYE DGTLYAQADV IFPALHGRFG EDGTIQGMFE LSGIPYVGTG VLSSACGMDK EYTKKLLAAE GLPVGKEVIL RGDETLTESD KQMLGLPVFV KPARGGSSIG ISRVIEWDDF DAALTLAREH DTKVIVEAEI KGVEVECGVL ERADGSLIAS VPAQLEDVDE GEEGFYGFDT KYLDNIVTAT IPAPFDQQTI ALIQSLSLEA FQALNCRGLS RVDFFVTDQG PVLNEVNTMP GFTPISMYPQ VFEATGIGYA ELLSHLIDQA LAQ //