ID DDL_ANADE Reviewed; 308 AA. AC Q2IG33; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 1. DT 25-NOV-2008, entry version 30. DE RecName: Full=D-alanine--D-alanine ligase; DE EC=6.3.2.4; DE AltName: Full=D-alanylalanine synthetase; DE AltName: Full=D-Ala-D-Ala ligase; GN Name=ddl; OrderedLocusNames=Adeh_3774; OS Anaeromyxobacter dehalogenans (strain 2CP-C). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Myxococcaceae; Anaeromyxobacter. OX NCBI_TaxID=290397; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., RA Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., RA Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cell wall formation (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D- CC alanyl-D-alanine. CC -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By CC similarity). CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000251; ABC83540.1; -; Genomic_DNA. DR RefSeq; YP_466977.1; -. DR GeneID; 3888271; -. DR GenomeReviews; CP000251_GR; Adeh_3774. DR KEGG; ade:Adeh_3774; -. DR HOGENOM; Q2IG33; -. DR BioCyc; ADEH290397:ADEH_3774-MON; -. DR GO; GO:0005618; C:cell wall; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP. DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. DR HAMAP; MF_00047; -; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013816; ATP_grasp_subdomain_2. 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; IPR013817; Pre-ATP_grasp. DR Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1. DR Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1. DR Pfam; PF07478; Dala_Dala_lig_C; 1. DR Pfam; PF01820; Dala_Dala_lig_N; 1. DR TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 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; KW Complete proteome; Cytoplasm; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Peptidoglycan synthesis. FT CHAIN 1 308 D-alanine--D-alanine ligase. FT /FTId=PRO_0000341050. FT DOMAIN 105 302 ATP-grasp. FT NP_BIND 133 188 ATP (By similarity). FT METAL 256 256 Magnesium or manganese 1 (By similarity). FT METAL 269 269 Magnesium or manganese 1 (By similarity). FT METAL 269 269 Magnesium or manganese 2 (By similarity). FT METAL 271 271 Magnesium or manganese 2 (By similarity). SQ SEQUENCE 308 AA; 32040 MW; 139E9F21B9EE075E CRC64; MSTWTGKRVA VLYGGRSSER EVSLRTGAAC AEALRQKGHD VVLVDVDLEV AARLRAERVE VAFVALHGRW GEDGSIQGLL ESMAIPYTGS GVLASAMGMD KTVSKAIFRS LGLAVADYRV FPRAAAGAIG VDDLPFGLPC VVKPAGEGSS VGVHLVNAAA ELGPACRDAA GYAGDVIVER YVKGTEVDVA VLEGKALGAI EIVPANAFYD YAAKYTAGTT KYFYPARIPE AHVRAVMEAA EAAHRGIGCS GVTRVDFIVA ADGTPYILEV NTLPGMTATS LVPKIAAGLG LSFPDLCDRI LDGAALKA //