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Database: UniProt/SWISS-PROT
Entry: DDL_SINMW
LinkDB: DDL_SINMW
Original site: DDL_SINMW 
ID   DDL_SINMW               Reviewed;         308 AA.
AC   A6UB80;
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=Smed_2077;
OS   Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Rhizobiaceae;
OC   Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=366394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM419;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA   Richardson P.;
RT   "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000738; ABR60910.1; -; Genomic_DNA.
DR   RefSeq; WP_011976207.1; NC_009636.1.
DR   RefSeq; YP_001327745.1; NC_009636.1.
DR   SMR; A6UB80; -.
DR   STRING; 366394.Smed_2077; -.
DR   PRIDE; A6UB80; -.
DR   EnsemblBacteria; ABR60910; ABR60910; Smed_2077.
DR   GeneID; 45062867; -.
DR   KEGG; smd:Smed_2077; -.
DR   PATRIC; fig|366394.8.peg.5235; -.
DR   eggNOG; COG1181; Bacteria.
DR   HOGENOM; CLU_039268_1_1_5; -.
DR   KO; K01921; -.
DR   OMA; FEAKYID; -.
DR   OrthoDB; 764798at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001108; 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; Cytoplasm;
KW   Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Peptidoglycan synthesis.
FT   CHAIN           1..308
FT                   /note="D-alanine--D-alanine ligase"
FT                   /id="PRO_1000030491"
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;  33524 MW;  5F1181E88A9FC57B CRC64;
     MSSKHVAVLL GGFSSERPVS LSSGTACADA LEGEGYRVTR VDVGHDVAAV LQELRPDVVF
     NALHGPFGED GTIQGILEYL EIPYTHSGVL ASALAMDKAQ AKHVAKAAGI PVAEAVVMDR
     RSFGNQHPMK PPYVVKPVRE GSSFGVVIVK EDQSHPPQVI TSSDWRYGDR IMVERYVAGR
     EFTCGVMGDV ALGVTEIIPQ GHAFYDYDSK YVKGGSKHVI PAQVSPNIYQ KIQTLALKAH
     QAIGCRGVSR SDFRFDDRGD GEGELIWLEI NTQPGMTPTS LVPEMAQHAG LRFGEFLRWM
     VEDASCLR
//
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