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Database: UniProt/SWISS-PROT
Entry: DDLA_ECOLI
LinkDB: DDLA_ECOLI
Original site: DDLA_ECOLI 
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   05-DEC-2018, entry version 122.
DE   RecName: Full=D-alanine--D-alanine ligase A;
DE            EC=6.3.2.4;
DE   AltName: Full=D-Ala-D-Ala ligase A;
DE   AltName: Full=D-alanylalanine synthetase A;
GN   Name=ddlA; OrderedLocusNames=b0381, JW0372;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   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   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 277:1453-1462(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:
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000305}.
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; NP_414915.1; NC_000913.3.
DR   RefSeq; WP_000413677.1; NZ_LN832404.1.
DR   ProteinModelPortal; P0A6J8; -.
DR   SMR; P0A6J8; -.
DR   BioGrid; 4261531; 464.
DR   DIP; DIP-47939N; -.
DR   IntAct; P0A6J8; 14.
DR   STRING; 316385.ECDH10B_0338; -.
DR   DrugBank; DB00260; Cycloserine.
DR   EPD; P0A6J8; -.
DR   PaxDb; P0A6J8; -.
DR   PRIDE; P0A6J8; -.
DR   EnsemblBacteria; AAC73484; AAC73484; b0381.
DR   EnsemblBacteria; BAE76162; BAE76162; BAE76162.
DR   GeneID; 945313; -.
DR   KEGG; ecj:JW0372; -.
DR   KEGG; eco:b0381; -.
DR   PATRIC; fig|1411691.4.peg.1897; -.
DR   EchoBASE; EB0209; -.
DR   EcoGene; EG10213; ddlA.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011593; -.
DR   InParanoid; P0A6J8; -.
DR   KO; K01921; -.
DR   PhylomeDB; P0A6J8; -.
DR   BioCyc; EcoCyc:DALADALALIGA-MONOMER; -.
DR   BioCyc; MetaCyc:DALADALALIGA-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   PRO; PR:P0A6J8; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IDA:EcoCyc.
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; IBA:GO_Central.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0010165; P:response to X-ray; IMP:EcoCyc.
DR   Gene3D; 3.30.1490.20; -; 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   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   PIRSF; PIRSF039102; Ddl/VanB; 1.
DR   SUPFAM; SSF52440; SSF52440; 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;
KW   Reference proteome.
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. {ECO:0000250}.
FT   METAL       302    302       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       315    315       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       315    315       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       317    317       Magnesium or manganese 2. {ECO:0000250}.
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
//
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