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 01-MAY-2013, entry version 98.
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.
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; 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; LLHGPFG; -.
DR BioCyc; EFAE226185:GHI1-946-MONOMER; -.
DR UniPathway; UPA00219; -.
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:HAMAP.
DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0030145; F:manganese ion binding; IEA:HAMAP.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA: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; PreATP-grasp-like; 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
//
