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Database: UniProt/SWISS-PROT
Entry: DDL_BORPD
LinkDB: DDL_BORPD
Original site: DDL_BORPD 
ID   DDL_BORPD               Reviewed;         326 AA.
AC   A9I4V9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   22-NOV-2017, entry version 69.
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=Bpet0699;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P.,
RA   Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J.,
RA   Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N.,
RA   Larisch C., Link S., Linke B., Meyer F., Mormann S., Nakunst D.,
RA   Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J.,
RA   Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B.,
RA   Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the
RT   metabolic versatility of environmental bacteria and virulence traits
RT   of pathogenic Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
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; AM902716; CAP41031.1; -; Genomic_DNA.
DR   ProteinModelPortal; A9I4V9; -.
DR   SMR; A9I4V9; -.
DR   STRING; 340100.Bpet0699; -.
DR   EnsemblBacteria; CAP41031; CAP41031; Bpet0699.
DR   KEGG; bpt:Bpet0699; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   OrthoDB; POG091H00GT; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001225; 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-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   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    326       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000341061.
FT   DOMAIN      114    313       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     140    195       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       267    267       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       280    280       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       280    280       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       282    282       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   326 AA;  34675 MW;  A06ECB789068E9BB CRC64;
     MNQSVTRPRP DAKALGKVGV LYGGRSAERD VSLMSGKGVH QALLSAGVDA HLFDTGERTL
     AELAAAGFDR VFIALHGRYG EDGTLQGALE LLGLPYTGSG PMASSLSMDK IMTKRVWLQH
     GLRTPAFEVL DAQAELRTVP DRLGLPLILK PPHEGSTVGI TKVAGYSDMK EGYAQAAKFD
     DEVLAEQFIA GRELTVAVLG TGAAAHALPV IEIVAPGGNY DYEHKYFSDE TQYFCPADLP
     DAVAAEVADL AVRAYRALGC AGWGRIDFML DADNRPWLLE ANTSPGMTSH SLVPMAAKAI
     GMSYAELCVS IVSEAACKVH SPARNS
//
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