ID DDL_AERHH Reviewed; 329 AA. AC A0KKW8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 16-JUN-2009, entry version 23. 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=AHA_2404; OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / NCIB 9240). OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales; OC Aeromonadaceae; Aeromonas. OX NCBI_TaxID=380703; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16980456; DOI=10.1128/JB.00621-06; RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., RA Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., RA Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.; RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all RT trades."; RL J. Bacteriol. 188:8272-8282(2006). 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; CP000462; ABK38135.1; -; Genomic_DNA. DR RefSeq; YP_856919.1; -. DR GeneID; 4488463; -. DR GenomeReviews; CP000462_GR; AHA_2404. DR KEGG; aha:AHA_2404; -. DR TIGR; AHA_2404; -. DR OMA; A0KKW8; GREIECG. DR GO; GO:0005618; C:cell wall; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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:0007047; P:cell wall organization; 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 Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 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 1 329 D-alanine--D-alanine ligase. FT /FTId=PRO_1000030422. FT DOMAIN 120 326 ATP-grasp. FT NP_BIND 150 205 ATP (By similarity). FT METAL 280 280 Magnesium or manganese 1 (By similarity). FT METAL 293 293 Magnesium or manganese 1 (By similarity). FT METAL 293 293 Magnesium or manganese 2 (By similarity). FT METAL 295 295 Magnesium or manganese 2 (By similarity). SQ SEQUENCE 329 AA; 36343 MW; BC5B5747304BD548 CRC64; MKNIHVLLLC GGGGSEHEVS LRSANFLEKQ LSLLPGVEVT RVEMFADRWL SADGRECKLG LDKLLSFDSV ARPVDYVVPC IHGYPGETGD LQSFLELAGL PYLGCDAEAS KICFNKISTK LWLSAIGIPN TPYLFLTEQN DAALSEAKAA LAKWGKVFIK AASQGSSVGC YSASNEADLV KGIADAFGYS EQVLIEKAVK PRELEVAVYQ YGDELVATYP GEICVPQDKF YTYEEKYSSA SHTETALRAE GLTQAQADAI HEYALKAFRQ LKLTHLSRID FFLTEEGEIL LNEINTFPGM TSISMFPKLL EHHGHRFADY LEQILRKAV //