ID I4F2H4_MODI5 Unreviewed; 373 AA. AC I4F2H4; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 02-SEP-2026, entry version 74. 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 ECO:0000313|EMBL:CCH89837.1}; GN OrderedLocusNames=MODMU_4453 {ECO:0000313|EMBL:CCH89837.1}; OS Modestobacter italicus (strain DSM 44449 / CECT 9708 / BC 501). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Geodermatophilales; OC Geodermatophilaceae; Modestobacter. OX NCBI_TaxID=2732864 {ECO:0000313|EMBL:CCH89837.1, ECO:0000313|Proteomes:UP000006461}; RN [1] {ECO:0000313|EMBL:CCH89837.1, ECO:0000313|Proteomes:UP000006461} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BC 501 {ECO:0000313|Proteomes:UP000006461}; RX PubMed=22887672; DOI=10.1128/JB.01029-12; RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L., RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A., RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.; RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501, RT a Representative Actinobacterium That Thrives on Calcareous Stone RT Surfaces."; RL J. Bacteriol. 194:4773-4774(2012). CC -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 D-alanine + ATP = D-alanyl-D-alanine + ADP + phosphate + CC H(+); Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57416, ChEBI:CHEBI:57822, CC ChEBI:CHEBI:456216; EC=6.3.2.4; Evidence={ECO:0000256|HAMAP- CC 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; FO203431; CCH89837.1; -; Genomic_DNA. DR RefSeq; WP_014742401.1; NC_017955.1. DR AlphaFoldDB; I4F2H4; -. DR STRING; 477641.MODMU_4453; -. DR KEGG; mmar:MODMU_4453; -. DR PATRIC; fig|477641.3.peg.4163; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_0_1_11; -. DR OMA; TQYRIPC; -. DR OrthoDB; 9813261at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000006461; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:InterPro. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 3.30.470.20:FF:000008; D-alanine--D-alanine ligase; 1. 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 NCBIfam; NF002378; PRK01372.1; 1. DR NCBIfam; NF002528; PRK01966.1-4; 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. 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, KW ECO:0000256|PIRSR:PIRSR039102-2}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00047}; Reference proteome {ECO:0000313|Proteomes:UP000006461}. FT DOMAIN 149..366 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT ACT_SITE 20 FT /evidence="ECO:0000256|PIRSR:PIRSR039102-1" FT ACT_SITE 200 FT /evidence="ECO:0000256|PIRSR:PIRSR039102-1" FT ACT_SITE 344 FT /evidence="ECO:0000256|PIRSR:PIRSR039102-1" FT BINDING 145 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-2" FT BINDING 192..194 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-2" FT BINDING 200..201 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-2" FT BINDING 230..237 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-2" FT BINDING 315 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 332..333 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-2" FT BINDING 333 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 333 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 335 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" SQ SEQUENCE 373 AA; 38831 MW; 9C97A59877956160 CRC64; MTGEAGKTRV AVVFGGRSAE HAISCVSAGS VLAALDPERY EVVPVGITRE GGWVLHDGGA LAIEGGRLPE VTDGTAVSLV GDPAGRGLAV LDPGQAIGRL TEVDVVFPVL HGAHGEDGTI QGLLEMSGLP YVGSGVFASA ASMDKEFTKK LLSAAGIPQG DHVVLRDASG AICPDPDVLD EAARERLGLP VFVKPSRAGS SIGITRVTDW AQFPAAVATA AAVDRKVVVE ASVPGREIEC GVLARPGGGL PEASLPAEIR LRPGTEWYDF DAKYLDDAVE FDVPADLTAE QTAAVQEISR RAFLAMDCRG LARVDFFLST DPATGADRWV VNEVNTMPGF TPISMFPRMW AATGVSYPEL VDRLVASAGL DGG //