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Database: UniProt
Entry: Q87AG1
LinkDB: Q87AG1
Original site: Q87AG1 
ID   DDL_XYLFT               Reviewed;         304 AA.
AC   Q87AG1;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 1.
DT   05-DEC-2018, entry version 103.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE            EC=6.3.2.4 {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-Ala-D-Ala ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase {ECO:0000255|HAMAP-Rule:MF_00047};
GN   Name=ddl {ECO:0000255|HAMAP-Rule:MF_00047}; Synonyms=ddlB;
GN   OrderedLocusNames=PD_1864;
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=183190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Temecula1 / ATCC 700964;
RX   PubMed=12533478; DOI=10.1128/JB.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B.,
RA   Miyaki C.Y., Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H.,
RA   Takita M.A., Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R.,
RA   Goldman M.H.S., Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M.,
RA   Carrer H., Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J.,
RA   Coutinho L.L., Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E.,
RA   Marino C.L., Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M.,
RA   Baia G.S., Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V.,
RA   da Cunha A.F., Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T.,
RA   Leoni S.G., Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D.,
RA   de Souza A.A., Truffi D., Tsukumo F., Yanai G.M., Zaros L.G.,
RA   Civerolo E.L., Simpson A.J.G., Almeida N.F. Jr., Setubal J.C.,
RA   Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's
RT   disease and citrus variegated chlorosis strains of Xylella
RT   fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(2003).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00047}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00047};
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       {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00047}.
DR   EMBL; AE009442; AAO29696.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q87AG1; -.
DR   SMR; Q87AG1; -.
DR   PRIDE; Q87AG1; -.
DR   EnsemblBacteria; AAO29696; AAO29696; PD_1864.
DR   KEGG; xft:PD_1864; -.
DR   KO; K01921; -.
DR   OMA; MQGLLEC; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002516; Chromosome.
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:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
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.
FT   CHAIN         1    304       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000177911.
FT   DOMAIN      103    301       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     132    187       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       254    254       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       268    268       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       268    268       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       270    270       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   304 AA;  32890 MW;  C35DB18A0A213896 CRC64;
     MFGRVAVLLG GTSAEREVSL LSGRNVLEVL RMRGVDAQSV DGVPALAQAL VERRFDRVFN
     VLHGHNGGGE DGVVQGLMQA FGVPYTGSDV LGSALSMDKV RTKQVWLALG LPTPRYASLS
     VCATAVEVRK AVEMLGFPVI IKPAKEGSSV GVSRVFALEH LEEAVALAAR YEGELLMEQL
     IEGDELTVSI LDEMALPSIR IVPQGQWYDY NAKYLAEDTQ YVCPGLDDVA EAEIAQLALA
     AFHSVGCRGW GRVDVMRERG SGRFFLLEVN TAPGMTTHSL VPKAASQLGM GFDDLVWRIL
     EQTL
//
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