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Database: UniProt/SWISS-PROT
Entry: DDL_OCHA4
LinkDB: DDL_OCHA4
Original site: DDL_OCHA4 
ID   DDL_OCHA4               Reviewed;         308 AA.
AC   A6WZQ9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE            EC=6.3.2.4 {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-Ala-D-Ala ligase {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase {ECO:0000255|HAMAP-Rule:MF_00047};
GN   Name=ddl {ECO:0000255|HAMAP-Rule:MF_00047};
GN   OrderedLocusNames=Oant_1747;
OS   Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC
OS   15819 / NCTC 12168).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Ochrobactrum.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168;
RX   PubMed=21685287; DOI=10.1128/JB.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M.,
RA   Shin M., Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile
RT   opportunistic pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(2011).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) +
CC         phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00047};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00047}.
DR   EMBL; CP000758; ABS14463.1; -; Genomic_DNA.
DR   RefSeq; WP_012091751.1; NC_009667.1.
DR   SMR; A6WZQ9; -.
DR   STRING; 439375.Oant_1747; -.
DR   EnsemblBacteria; ABS14463; ABS14463; Oant_1747.
DR   GeneID; 5380357; -.
DR   KEGG; oan:Oant_1747; -.
DR   PATRIC; fig|439375.7.peg.1848; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   OrthoDB; 764798at2; -.
DR   BioCyc; OANT439375:G1G9F-1863-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002301; Chromosome 1.
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:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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_sf.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   PIRSF; PIRSF039102; Ddl/VanB; 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;
KW   Reference proteome.
FT   CHAIN         1    308       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_1000030475.
FT   DOMAIN      102    302       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     128    183       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       252    252       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       269    269       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       269    269       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       271    271       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   308 AA;  33280 MW;  CF12441072AA5D2F CRC64;
     MTGKHVAVLM GGFSSERPVS LSSGTACAAT LEERGYCVTR IDVDRNVASV LAELKPDVAF
     NALHGPFGED GAIQGVLEYL QIPYTHSGVL ASALAMDKDR AKKVAAAAGV AVASSLLLNR
     FEIGTEHPME PPYVVKPVRE GSSFGVVIVK EDQTHPPQII SSAEWNYGAE VLVEKYIPGR
     ELTCAVMGDR VMDVCEIIPV GHQFYDYDSK YVAGASSHVC PAKILPNIYQ KIQTMALTAH
     RAIGCRGVSR SDFRFDDRFS DDGEVIWLEI NTQPGMTPTS LVPDIAKAAG ISFGELLSWM
     VEDASCLR
//
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