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Entry: DDL_ENTFA S0PHI1_ENTFA
LinkDB: DDL_ENTFA S0PHI1_ENTFA
Original site: DDL_ENTFA S0PHI1_ENTFA 
tr:S0PHI1_ENTFA : No such data.

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   13-SEP-2023, entry version 138.
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; Bacillota; 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 D-
RT   alanine:D-alanine ligases in vancomycin-resistant Enterococcus faecalis
RT   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., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000250}.
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. {ECO:0000250};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000305}.
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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   RefSeq; WP_010774177.1; NZ_KE136527.1.
DR   AlphaFoldDB; Q47758; -.
DR   SMR; Q47758; -.
DR   STRING; 226185.EF_0843; -.
DR   BindingDB; Q47758; -.
DR   ChEMBL; CHEMBL4523951; -.
DR   EnsemblBacteria; AAO80655; AAO80655; EF_0843.
DR   KEGG; efa:EF0843; -.
DR   PATRIC; fig|226185.46.peg.1249; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_0_0_9; -.
DR   OMA; NTTPGMT; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001415; 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; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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   NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF25; D-ALANINE--D-ALANINE LIGASE A; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   PIRSF; PIRSF039102; Ddl/VanB; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 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; Cytoplasm;
KW   Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN           1..348
FT                   /note="D-alanine--D-alanine ligase"
FT                   /id="PRO_0000177821"
FT   DOMAIN          136..341
FT                   /note="ATP-grasp"
FT   BINDING         169..224
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         308
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         310
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        127
FT                   /note="A -> V (in Ref. 1; AAC43218)"
FT                   /evidence="ECO:0000305"
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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