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Database: UniProt
Entry: Q8FZP5
LinkDB: Q8FZP5
Original site: Q8FZP5 
ID   DDLB_BRUSU              Reviewed;         308 AA.
AC   Q8FZP5; G0KBI8;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   05-DEC-2018, entry version 100.
DE   RecName: Full=D-alanine--D-alanine ligase B {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 B {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase B {ECO:0000255|HAMAP-Rule:MF_00047};
GN   Name=ddlB {ECO:0000255|HAMAP-Rule:MF_00047}; Synonyms=ddl;
GN   OrderedLocusNames=BR1428, BS1330_I1422;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A.,
RA   Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O.,
RA   Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M.,
RA   Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between
RT   animal and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/JB.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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; AE014291; AAN30341.1; -; Genomic_DNA.
DR   EMBL; CP002997; AEM18757.1; -; Genomic_DNA.
DR   RefSeq; WP_004690987.1; NZ_KN046804.1.
DR   ProteinModelPortal; Q8FZP5; -.
DR   SMR; Q8FZP5; -.
DR   EnsemblBacteria; AAN30341; AAN30341; BR1428.
DR   EnsemblBacteria; AEM18757; AEM18757; BS1330_I1422.
DR   KEGG; bms:BR1428; -.
DR   KEGG; bsi:BS1330_I1422; -.
DR   PATRIC; fig|204722.21.peg.915; -.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000007104; 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-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    308       D-alanine--D-alanine ligase B.
FT                                /FTId=PRO_0000177797.
FT   DOMAIN      102    302       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       269    269       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       269    269       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       271    271       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   308 AA;  33378 MW;  722100E5DB7486F8 CRC64;
     MTGKHVAVLM GGFSSERSVS LSSGVACATT LEECGYRVTR IDVDRNVASI LVELKPDVVF
     NALHGPFGED GAIQGVLEYL QIPYTHSGVL ASALAMDKDR AKKVAAAAGV VVAPSRLMNR
     FDIGSQHPMK PPYVVKPVRE GSSFGVVIVK EDQPHPPQVI GSADWKYGDE VMVEGYIAGR
     ELTCAVMGDR AMDVCEIIPV GYQFYDYDSK YVAGASTHVS PAKILPNIYQ KIQTMALTAH
     RAIGCRGVSR SDFRFDDRFS EEGEVVWLEI NTQPGMTPTS LVPDIAKAAG ISFAELLSWM
     VEDASCLR
//
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