GenomeNet

Database: UniProt/SWISS-PROT
Entry: DDL_BURP0
LinkDB: DDL_BURP0
Original site: DDL_BURP0 
ID   DDL_BURP0               Reviewed;         312 AA.
AC   A3NZL3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   12-SEP-2018, entry version 77.
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=BURPS1106A_3548;
OS   Burkholderia pseudomallei (strain 1106a).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=357348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1106a;
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (FEB-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; CP000572; ABN90443.1; -; Genomic_DNA.
DR   RefSeq; WP_004194254.1; NC_009076.1.
DR   PDB; 5NRH; X-ray; 1.30 A; A/B=1-312.
DR   PDB; 5NRI; X-ray; 1.50 A; A/B=1-312.
DR   PDBsum; 5NRH; -.
DR   PDBsum; 5NRI; -.
DR   ProteinModelPortal; A3NZL3; -.
DR   SMR; A3NZL3; -.
DR   EnsemblBacteria; ABN90443; ABN90443; BURPS1106A_3548.
DR   KEGG; bpl:BURPS1106A_3548; -.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000006738; Chromosome I.
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-EC.
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-UniPathway.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Peptidoglycan synthesis.
FT   CHAIN         1    312       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000341075.
FT   DOMAIN      108    308       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     138    193       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       262    262       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       275    275       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       275    275       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       277    277       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   HELIX         6      9       {ECO:0000244|PDB:5NRH}.
FT   STRAND       11     15       {ECO:0000244|PDB:5NRH}.
FT   HELIX        23     39       {ECO:0000244|PDB:5NRH}.
FT   STRAND       43     47       {ECO:0000244|PDB:5NRH}.
FT   TURN         49     51       {ECO:0000244|PDB:5NRH}.
FT   HELIX        56     59       {ECO:0000244|PDB:5NRH}.
FT   STRAND       64     67       {ECO:0000244|PDB:5NRH}.
FT   HELIX        72     74       {ECO:0000244|PDB:5NRH}.
FT   HELIX        78     85       {ECO:0000244|PDB:5NRH}.
FT   STRAND       89     92       {ECO:0000244|PDB:5NRH}.
FT   HELIX        95    101       {ECO:0000244|PDB:5NRH}.
FT   HELIX       104    114       {ECO:0000244|PDB:5NRH}.
FT   STRAND      121    125       {ECO:0000244|PDB:5NRH}.
FT   HELIX       130    141       {ECO:0000244|PDB:5NRH}.
FT   STRAND      145    151       {ECO:0000244|PDB:5NRH}.
FT   STRAND      154    156       {ECO:0000244|PDB:5NRH}.
FT   STRAND      159    161       {ECO:0000244|PDB:5NRH}.
FT   HELIX       164    166       {ECO:0000244|PDB:5NRH}.
FT   HELIX       167    177       {ECO:0000244|PDB:5NRH}.
FT   STRAND      179    185       {ECO:0000244|PDB:5NRH}.
FT   STRAND      189    198       {ECO:0000244|PDB:5NRH}.
FT   STRAND      206    209       {ECO:0000244|PDB:5NRH}.
FT   STRAND      211    215       {ECO:0000244|PDB:5NRH}.
FT   HELIX       217    221       {ECO:0000244|PDB:5NRH}.
FT   STRAND      227    231       {ECO:0000244|PDB:5NRH}.
FT   HELIX       236    252       {ECO:0000244|PDB:5NRH}.
FT   STRAND      257    266       {ECO:0000244|PDB:5NRH}.
FT   STRAND      271    279       {ECO:0000244|PDB:5NRH}.
FT   HELIX       287    293       {ECO:0000244|PDB:5NRH}.
FT   TURN        294    296       {ECO:0000244|PDB:5NRH}.
FT   HELIX       299    308       {ECO:0000244|PDB:5NRH}.
SQ   SEQUENCE   312 AA;  33341 MW;  CCD89397BEAE5E22 CRC64;
     MSGIDPKRFG KVAVLLGGDS AEREVSLNSG RLVLQGLRDA GIDAHPFDPA QRPLAALKDE
     GFVRAFNALH GGYGENGQIQ GALDFYGIRY TGSGVLGSAL GLDKFRTKLV WQQTGIPTPP
     FETVMRGDDY AARAQDIVAK LGVPLFVKPA SEGSSVAVEK VKSADALPAA LEEAAKHDKI
     VIVEKSIEGG GEYTACIAAD LDLPLIRIVP AGEFYDYHAK YIANDTQYLI PCGLDAAKEA
     EFKRIARRAF DVLGCTDWGR ADFMLDAAGN PYFLEVNTAP GMTDHSLPPK AARAVGIGYS
     ELVVKVLSLT LD
//
DBGET integrated database retrieval system