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Database: UniProt
Entry: A4XJ89
LinkDB: A4XJ89
Original site: A4XJ89 
ID   DDL_CALS8               Reviewed;         364 AA.
AC   A4XJ89;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   14-MAY-2014, entry version 53.
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=Csac_1372;
OS   Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis;
OC   Caldicellulosiruptor.
OX   NCBI_TaxID=351627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43494 / DSM 8903;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA   van de Werken H.J.G., Verhaart M.R.A., VanFossen A.L., Lewis D.L.,
RA   Nichols J.D., Goorissen H.P., van Niel E.W.J., Stams F.J.M.,
RA   Willquist K.U., Ward D.E., van der Oost J., Kelly R.M., Kengen S.M.W.,
RA   Richardson P.;
RT   "Genome sequence of the thermophilic hydrogen-producing bacterium
RT   Caldicellulosiruptor saccharolyticus DSM 8903.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000679; ABP66974.1; -; Genomic_DNA.
DR   RefSeq; YP_001180165.1; NC_009437.1.
DR   ProteinModelPortal; A4XJ89; -.
DR   STRING; 351627.Csac_1372; -.
DR   EnsemblBacteria; ABP66974; ABP66974; Csac_1372.
DR   GeneID; 5087940; -.
DR   KEGG; csc:Csac_1372; -.
DR   PATRIC; 21252424; VBICalSac56748_1523.
DR   eggNOG; COG1181; -.
DR   HOGENOM; HOG000011593; -.
DR   KO; K01921; -.
DR   OMA; QIDVIFP; -.
DR   OrthoDB; EOG64BQ73; -.
DR   BioCyc; CSAC351627:GJ17-1406-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.
FT   CHAIN         1    364       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_1000030434.
FT   DOMAIN      140    346       ATP-grasp.
FT   NP_BIND     173    228       ATP (By similarity).
FT   METAL       299    299       Magnesium or manganese 1 (By similarity).
FT   METAL       313    313       Magnesium or manganese 1 (By similarity).
FT   METAL       313    313       Magnesium or manganese 2 (By similarity).
FT   METAL       315    315       Magnesium or manganese 2 (By similarity).
SQ   SEQUENCE   364 AA;  40890 MW;  7AEAA0179641995C CRC64;
     MTKLKVAVLF GGVSTEHEVS IVSAKSVMQN LDKEKYEIIP IGITKEGKWL LYTGKIEDLD
     SKWTMYSIEC FISPDRTKKA LVKIKDSEAT FIDIDVVFPV LHGLNGEDGT VQGLLELSGI
     PYVGCGVLSS ALCMDKAFAK KLALLEGIPQ GHFLVIYKDE YLSKKEYFIR RIESEFSYPV
     FVKPANSGSS VGISKAKDKD ELILAIHEAF LYDTKILIEQ AINAREIECA VLGNSEILVS
     ALGEIVPSRE FYSYEAKYID GSSELIIPAK LEKQVEDEIK ELAVKIYKLF ECSGMARIDF
     FVDKETNKVY FNEVNTIPGF TSISMYPKLM EYSGIPYPQL LDKLIQLAIE KNQQKQSIKY
     SKEG
//
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