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Database: UniProt
Entry: Q47758
LinkDB: Q47758
Original site: Q47758 
ID   DDL_ENTFA               Reviewed;         348 AA.
AC   Q47758;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   19-FEB-2014, entry version 102.
DE   RecName: Full=D-alanine--D-alanine ligase;
DE            EC=6.3.2.4;
DE   AltName: Full=D-Ala-D-Ala ligase;
DE   AltName: Full=D-alanylalanine synthetase;
GN   Name=ddl; OrderedLocusNames=EF_0843;
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=8125347; DOI=10.1016/0378-1119(94)90737-4;
RA   Evers S., Reynolds P.E., Courvalin P.;
RT   "Sequence of the vanB and ddl genes encoding D-alanine:D-lactate and
RT   D-alanine:D-alanine ligases in vancomycin-resistant Enterococcus
RT   faecalis V583.";
RL   Gene 140:97-102(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F.,
RA   Tettelin H., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J.,
RA   Khouri H.M., Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A.,
RA   Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant
RT   Enterococcus faecalis.";
RL   Science 299:2071-2074(2003).
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.
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DR   EMBL; U00457; AAC43218.2; -; Genomic_DNA.
DR   EMBL; AE016830; AAO80655.1; -; Genomic_DNA.
DR   RefSeq; NP_814585.1; NC_004668.1.
DR   ProteinModelPortal; Q47758; -.
DR   STRING; 226185.EF0843; -.
DR   EnsemblBacteria; AAO80655; AAO80655; EF_0843.
DR   GeneID; 1199736; -.
DR   KEGG; efa:EF0843; -.
DR   PATRIC; 21852066; VBIEntFae7065_0782.
DR   eggNOG; COG1181; -.
DR   KO; K01921; -.
DR   OMA; MDKIAMK; -.
DR   OrthoDB; EOG64BQ73; -.
DR   BioCyc; EFAE226185:GHI1-824-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   Gene3D; 3.30.470.20; -; 2.
DR   Gene3D; 3.40.50.20; -; 1.
DR   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR016185; PreATP-grasp_dom.
DR   PANTHER; PTHR23132; PTHR23132; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 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    348       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000177821.
FT   DOMAIN      136    341       ATP-grasp.
FT   NP_BIND     169    224       ATP (By similarity).
FT   METAL       295    295       Magnesium or manganese 1 (By similarity).
FT   METAL       308    308       Magnesium or manganese 1 (By similarity).
FT   METAL       308    308       Magnesium or manganese 2 (By similarity).
FT   METAL       310    310       Magnesium or manganese 2 (By similarity).
FT   CONFLICT    127    127       A -> V (in Ref. 1; AAC43218).
SQ   SEQUENCE   348 AA;  39340 MW;  4A690F4E4FEDBF75 CRC64;
     MKIILLYGGR SEEHDVSVLS AYSVLNAIYY KYYQVQLVFI SKDGQWVKGP LLSERPQNKE
     VLHLTWAQTP EETGEFSGKR ISPSEIYEEE AIVFPVLHGP NGEDGTIQGF METINMPYVG
     AGVLASANAM DKIMTKYLLQ TVGIPQVPFV PVLRSDWKGN PKEVFEKCEG SLIYPVFVKP
     ANMGSSVGIS KVENREELQE ALEEAFRYDA RAIVEQGIEA REIEVAILGN EDVRTTLPGE
     VVKDVAFYDY DAKYINNTIE MQIPAHVPEE VAHQAQEYAK KAYIMLDGSG LSRCDFFLTS
     KNELFLNELN TMPGFTDFSM YPLLWENMGL KYSDLIEELI QLALNRFK
//
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