ID   DDL_ARTAT               Reviewed;         378 AA.
AC   A1R7J5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 25.
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; OrderedLocusNames=AAur_2481;
OS   Arthrobacter aurescens (strain TC1).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=290340;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17194220; DOI=10.1371/journal.pgen.0020214;
RA   Mongodin E.F., Shapir N., Daugherty S.C., DeBoy R.T., Emerson J.B.,
RA   Shvartzbeyn A., Radune D., Vamathevan J., Riggs F., Grinberg V.,
RA   Khouri H.M., Wackett L.P., Nelson K.E., Sadowsky M.J.;
RT   "Secrets of soil survival revealed by the genome sequence of
RT   Arthrobacter aurescens TC1.";
RL   PLoS Genet. 2:2094-2106(2006).
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; CP000474; ABM07506.1; -; Genomic_DNA.
DR   RefSeq; YP_948207.1; -.
DR   GeneID; 4640348; -.
DR   GenomeReviews; CP000474_GR; AAur_2481.
DR   KEGG; aau:AAur_2481; -.
DR   TIGR; AAur_2481; -.
DR   OMA; A1R7J5; GREIECG.
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    378       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000341053.
FT   DOMAIN      157    368       ATP-grasp.
FT   NP_BIND     189    244       ATP (By similarity).
FT   METAL       322    322       Magnesium or manganese 1 (By similarity).
FT   METAL       335    335       Magnesium or manganese 1 (By similarity).
FT   METAL       335    335       Magnesium or manganese 2 (By similarity).
FT   METAL       337    337       Magnesium or manganese 2 (By similarity).
SQ   SEQUENCE   378 AA;  39981 MW;  912B80574B38828F CRC64;
     MVTDHSTPVT GRPRVAILFG GRSSEHAVSC VTAAGVMGAI DKNKYEVIPI GIAKSGQWVL
     ASGDTSEWSL SSAALPEVAP SGRTVTLAEV GGEHQLIVTE PNAVPQELGS VDVVFPLLHG
     PWGEDGTIQG LLELSDTRYV GAGVLASAVG MDKHFMKVVF ESAGLSVGPY VAVTDREWST
     DAEAVRKRVD KLGFPVFVKP ARAGSSMGIS KVDSMEGLDA AIDEARRHDL KLVIEAGIVG
     REIECAVLQG RGTDAPRTSM PGEIAVAVGE HQFYDFAAKY VEDGAAALSC PADMPDEAIA
     RVRELAAVAF DAVGAEGLSR VDFFYTPAGE LIINEINTMP GFTPKSMYPQ MWAASGLAYG
     DLIDELIHLA LTRKTGLR
//