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 12-AUG-2020, entry version 81.
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}; OrderedLocusNames=Oant_1747;
OS Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC
OS 15819 / NCTC 12168).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Brucellaceae;
OC 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., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT 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. {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; COG1181; Bacteria.
DR HOGENOM; CLU_039268_1_1_5; -.
DR KO; K01921; -.
DR OMA; FEAKYID; -.
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; Cytoplasm;
KW Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Peptidoglycan synthesis; Reference proteome.
FT CHAIN 1..308
FT /note="D-alanine--D-alanine ligase"
FT /id="PRO_1000030475"
FT DOMAIN 102..302
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT NP_BIND 128..183
FT /note="ATP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT METAL 252
FT /note="Magnesium or manganese 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT METAL 269
FT /note="Magnesium or manganese 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT METAL 269
FT /note="Magnesium or manganese 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT METAL 271
FT /note="Magnesium or manganese 2"
FT /evidence="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
//
