ID DDL_SINFN Reviewed; 306 AA.
AC C3MEM6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 10-APR-2019, entry version 66.
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=NGR_c21040;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT secretion systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP25867.1; -; Genomic_DNA.
DR RefSeq; WP_012708630.1; NC_012587.1.
DR RefSeq; YP_002826620.1; NC_012587.1.
DR ProteinModelPortal; C3MEM6; -.
DR SMR; C3MEM6; -.
DR STRING; 394.NGR_c21040; -.
DR EnsemblBacteria; ACP25867; ACP25867; NGR_c21040.
DR GeneID; 7791382; -.
DR KEGG; rhi:NGR_c21040; -.
DR PATRIC; fig|394.7.peg.4929; -.
DR eggNOG; ENOG4105CPF; Bacteria.
DR eggNOG; COG1181; LUCA.
DR HOGENOM; HOG000011592; -.
DR KO; K01921; -.
DR OMA; YETKYTE; -.
DR OrthoDB; 764798at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001054; Chromosome.
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.
FT CHAIN 1 306 D-alanine--D-alanine ligase.
FT /FTId=PRO_1000189742.
FT DOMAIN 102 300 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 267 267 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 267 267 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
FT METAL 269 269 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ SEQUENCE 306 AA; 33152 MW; 6978210213DB18D4 CRC64;
MSGKHVAVLM GGFSSERPVS LSSGAACADA LEAEGYRVSR VDVGRDVAAV LADLRPDIVF
NALHGPFGED GTIQGILEYL EIPYTHSGVL ASALAMDKAQ AKHVAKAAGI PVADALIMDR
REFGNAHPMK PPYVVKPVRE GSSFGVVIVK EDQSHPPQVI TSSEWRYGDR VMVERYIAGR
ELTCGVMGDV ALGVTEIIPQ GHAFYDYDSK YVKGGSAHVI PAQISPNIYQ KIQSLAVKAH
QAIGCRGVSR SDFRFDDRGE GELIWLEINT QPGMTPTSLV PEMAQHAGLQ FGEFLRWMVE
DASCLR
//
