ID   DDLA_CLOTE              Reviewed;         301 AA.
AC   Q897P8;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-NOV-2008, entry version 43.
DE   RecName: Full=D-alanine--D-alanine ligase A;
DE            EC=6.3.2.4;
DE   AltName: Full=D-alanylalanine synthetase A;
DE   AltName: Full=D-Ala-D-Ala ligase A;
GN   Name=ddlA; OrderedLocusNames=CTC_00683;
OS   Clostridium tetani.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88;
RX   MEDLINE=22457253; PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA   Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA   Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of
RT   tetanus disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(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; AE015927; AAO35288.1; -; Genomic_DNA.
DR   RefSeq; NP_781351.1; -.
DR   HSSP; P07862; 1IOW.
DR   GeneID; 1058953; -.
DR   GenomeReviews; AE015927_GR; CTC_00683.
DR   KEGG; ctc:CTC00683; -.
DR   NMPDR; fig|212717.1.peg.573; -.
DR   HOGENOM; Q897P8; -.
DR   BioCyc; CTET212717:CTC_00683-MON; -.
DR   GO; GO:0005618; C:cell wall; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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: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    301       D-alanine--D-alanine ligase A.
FT                                /FTId=PRO_0000177809.
FT   DOMAIN       99    293       ATP-grasp.
FT   NP_BIND     126    181       ATP (By similarity).
FT   METAL       248    248       Magnesium or manganese 1 (By similarity).
FT   METAL       260    260       Magnesium or manganese 1 (By similarity).
FT   METAL       260    260       Magnesium or manganese 2 (By similarity).
FT   METAL       262    262       Magnesium or manganese 2 (By similarity).
SQ   SEQUENCE   301 AA;  34031 MW;  AEC30BCA0618FDF5 CRC64;
     MQIGVVMGGV STEKEISNLT GKYIIENLDK SKYEILPIPI NTKFELIDKI KCLEFAFIAL
     HGNFGEDGKV QALLETMGVP YSGSGVLASS LCMDKNMSKK ILQGEGIKTP RWIMLYKNED
     IDFESIKNIG YPLVVKPNSG GSSIGITIVK KEQELIKAIE EAFKFDEEIL IEEYIKGEEI
     TCCMLDGKPL PILSIKTKEE FFNYKAKYFE GVAEEKVADL SLELKDQVEK ISNKCWKSFK
     LKVYGRIDMI IKGNEVYVIE INTLPGMTKY SLFPKSAKAY GLNFSELLDK IIELSIKEYE
     F
//