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Database: UniProt/SWISS-PROT
Entry: DDL_AZOC5
LinkDB: DDL_AZOC5
Original site: DDL_AZOC5 
ID   DDL_AZOC5               Reviewed;         306 AA.
AC   A8HZA8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   10-OCT-2018, entry version 73.
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=AZC_4561;
OS   Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 /
OS   NBRC 14845 / NCIMB 13405 / ORS 571).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 /
RC   ORS 571;
RA   Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T.,
RA   Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B.,
RA   Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M.,
RA   Oyaizu H.;
RT   "Complete genome sequence of the nitrogen-fixing bacterium
RT   Azorhizobium caulinodans ORS571.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {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; AP009384; BAF90559.1; -; Genomic_DNA.
DR   RefSeq; WP_012173080.1; NC_009937.1.
DR   ProteinModelPortal; A8HZA8; -.
DR   SMR; A8HZA8; -.
DR   STRING; 438753.AZC_4561; -.
DR   PRIDE; A8HZA8; -.
DR   EnsemblBacteria; BAF90559; BAF90559; AZC_4561.
DR   KEGG; azc:AZC_4561; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   OrthoDB; POG091H00GT; -.
DR   BioCyc; ACAU438753:G1G2W-4733-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000270; 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;
KW   Reference proteome.
FT   CHAIN         1    306       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000341057.
FT   DOMAIN      101    300       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     128    182       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       250    250       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;  32913 MW;  635CE58584325D3E CRC64;
     MAKHVAVLMG GWSPEREVSL RSGAGCAKAL EEVGYRVTRV DVDRDVAEVL ARLKPDVALN
     LLHGCPGEDG TIQGILEILR IPYSHSGVLA SALAMDKARA KVVMAAAGIP VPGGHLVTRA
     EAAKGHVLPP PYVLKPNTGG SSVGVFIVKE DQPHPPQELF RADWTFGESL MAEPFIKGLE
     LTCGVMGDRA LDVIEVEAVH GFYDYESKYA AGGSRHILPA RVLPQIYQQV RMLALEAHRA
     LGCRGISRAD FRYDDTLPDG KGLVCLEVNT QPGMTETSLV PDMAAHAGIS FGELVTWMVE
     DATLDR
//
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