ID DDLA_ECOLI Reviewed; 364 AA. AC P0A6J8; P23844; Q2MC44; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 1. DT 16-JUN-2009, entry version 49. DE RecName: Full=D-alanine--D-alanine ligase A; DE EC=6.3.2.4; DE AltName: Full=D-alanylalanine synthetase A; DE AltName: Full=D-Ala-D-Ala ligase A; GN Name=ddlA; OrderedLocusNames=b0381, JW0372; OS Escherichia coli (strain K12). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91129242; PubMed=1993184; DOI=10.1021/bi00220a033; RA Zawadzke L.E., Bugg T.D., Walsh C.T.; RT "Existence of two D-alanine:D-alanine ligases in Escherichia coli: RT cloning and sequencing of the ddlA gene and purification and RT characterization of the DdlA and DdlB enzymes."; RL Biochemistry 30:1673-1682(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains RT MG1655 and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). CC -!- FUNCTION: Cell wall formation. 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. 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; M58467; AAA23671.1; -; Genomic_DNA. DR EMBL; U73857; AAB18104.1; -; Genomic_DNA. DR EMBL; U00096; AAC73484.1; -; Genomic_DNA. DR EMBL; AP009048; BAE76162.1; -; Genomic_DNA. DR PIR; A39182; CEECDA. DR RefSeq; AP_001032.1; -. DR RefSeq; NP_414915.1; -. DR HSSP; P25051; 1E4E. DR GeneID; 945313; -. DR GenomeReviews; AP009048_GR; JW0372. DR GenomeReviews; U00096_GR; b0381. DR KEGG; ecj:JW0372; -. DR KEGG; eco:b0381; -. DR EchoBASE; EB0209; -. DR EcoGene; EG10213; ddlA. DR HOGENOM; P0A6J8; -. DR OMA; P0A6J8; GREIECG. DR BioCyc; EcoCyc:DALADALALIGA-MON; -. DR BioCyc; MetaCyc:DALADALALIGA-MON; -. DR DrugBank; DB00260; Cycloserine. 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 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 1 364 D-alanine--D-alanine ligase A. FT /FTId=PRO_0000177815. FT DOMAIN 145 348 ATP-grasp. FT NP_BIND 175 230 ATP (By similarity). FT METAL 302 302 Magnesium or manganese 1 (By similarity). FT METAL 315 315 Magnesium or manganese 1 (By similarity). FT METAL 315 315 Magnesium or manganese 2 (By similarity). FT METAL 317 317 Magnesium or manganese 2 (By similarity). SQ SEQUENCE 364 AA; 39316 MW; C7FDBEC353AC1320 CRC64; MEKLRVGIVF GGKSAEHEVS LQSAKNIVDA IDKSRFDVVL LGIDKQGQWH VSDASNYLLN ADDPAHIALR PSATSLAQVP GKHEHQLIDA QNGQPLPTVD VIFPIVHGTL GEDGSLQGML RVANLPFVGS DVLASAACMD KDVTKRLLRD AGLNIAPFIT LTRANRHNIS FAEVESKLGL PLFVKPANQG SSVGVSKVTS EEQYAIAVDL AFEFDHKVIV EQGIKGREIE CAVLGNDNPQ ASTCGEIVLT SDFYAYDTKY IDEDGAKVVV PAAIAPEIND KIRAIAVQAY QTLGCAGMAR VDVFLTPENE VVINEINTLP GFTNISMYPK LWQASGLGYT DLITRLIELA LERHAADNAL KTTM //