ID   DDL_AQUAE               Reviewed;         291 AA.
AC   O66806;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JUN-2009, entry version 67.
DE   RecName: Full=D-alanine--D-alanine ligase;
DE            EC=6.3.2.4;
DE   AltName: Full=D-alanylalanine synthetase;
DE   AltName: Full=D-Ala-D-Ala ligase;
GN   Name=ddl; Synonyms=ddlA; OrderedLocusNames=aq_521;
OS   Aquifex aeolicus.
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=63363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   MEDLINE=98196666; PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC06765.1; -; Genomic_DNA.
DR   PIR; B70347; B70347.
DR   RefSeq; NP_213366.1; -.
DR   HSSP; P07862; 1IOV.
DR   GeneID; 1193224; -.
DR   GenomeReviews; AE000657_GR; aq_521.
DR   KEGG; aae:aq_521; -.
DR   NMPDR; fig|224324.1.peg.381; -.
DR   HOGENOM; O66806; -.
DR   OMA; O66806; RSDFRWD.
DR   BioCyc; AAEO224324:AQ_521-MON; -.
DR   BRENDA; 6.3.2.4; 189781.
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:UniProtKB-KW.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007047; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   HAMAP; MF_00047; -; 1.
DR   InterPro; IPR011761; ATP-grasp.
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; IPR013817; Pre-ATP_grasp.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 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    291       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000177780.
FT   DOMAIN       99    291       ATP-grasp.
FT   NP_BIND     125    179       ATP (By similarity).
FT   METAL       245    245       Magnesium or manganese 1 (By similarity).
FT   METAL       258    258       Magnesium or manganese 1 (By similarity).
FT   METAL       258    258       Magnesium or manganese 2 (By similarity).
FT   METAL       260    260       Magnesium or manganese 2 (By similarity).
SQ   SEQUENCE   291 AA;  32797 MW;  B0A892F15539C143 CRC64;
     MRVVVLMGGR SSEREISLKT GKAVAKALRE LGHEVYELDL DKELPCKLLE IKPDKVFIAL
     HGRYGEDGTV QGLLEILDIP YTGSDTIASA VSIDKDFTKR IVKSLGINTP DWETFISEGD
     VLNTEWNKFP AVVKPVREGS SVGLKIVESL EELKEYALDL LKKTERVMVE EFVEGRDMTV
     GILKGEALPV VEIIPKKGVY DYECKYTKGM SEYRILKDEK LSKKLQEISL KISKFLSLKD
     FARIDFRVTK EGKIFFLEVN TIPGMTELSL LPMAAKEKGM DFKKLISIII T
//