ID   DDL_ARTS2               Reviewed;         382 AA.
AC   A0JXX3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 21.
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=Arth_2514;
OS   Arthrobacter sp. (strain FB24).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=290399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., Chertkov O., Thompson S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K.,
RA   Nakatsu C.H., Richardson P.;
RT   "Complete sequence of chromosome 1 of Arthrobacter sp. FB24.";
RL   Submitted (AUG-2006) 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; CP000454; ABK03893.1; -; Genomic_DNA.
DR   RefSeq; YP_831993.1; -.
DR   GeneID; 4444920; -.
DR   GenomeReviews; CP000454_GR; Arth_2514.
DR   KEGG; art:Arth_2514; -.
DR   TIGR; Arth_2514; -.
DR   OMA; A0JXX3; 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; 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   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    382       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000341054.
FT   DOMAIN      161    372       ATP-grasp.
FT   NP_BIND     193    248       ATP (By similarity).
FT   METAL       326    326       Magnesium or manganese 1 (By similarity).
FT   METAL       339    339       Magnesium or manganese 1 (By similarity).
FT   METAL       339    339       Magnesium or manganese 2 (By similarity).
FT   METAL       341    341       Magnesium or manganese 2 (By similarity).
SQ   SEQUENCE   382 AA;  40775 MW;  8D253FD6176B54FB CRC64;
     MSEEQLNKHT APGHAKPRVA VLFGGRSSEH AVSCVTAAGV LGAIDYDKYD VIPIGIAKTG
     QWVLVSGDTR QWSLSASSLP EVSPSARTVT LAEIGGEHQL IVASPNEVPQ ELGAVDVVFP
     LLHGPFGEDG TIQGLLELSD TRYVGAGVLA SAVGMDKHYM KVVFEAAGLQ VGPYIAVTDR
     QWLTDPEAIR KRVDRLGYPV FVKPARAGSS MGISKVDSLE GLDAAIAAAR EHDLKLVIEA
     GIVGREIECA VLEGRGTEPP RTSMPGEIAV APGEHEFYDF NAKYVEDDAA SLSCPADLPD
     EAIARVRELA AAAFDAVGAE GLSRVDFFYT PDGELIINEI NTMPGFTPKS MYPQMWAASG
     LGYAELIDEL IYLALNRKTG LR
//