GenomeNet

Database: UniProt
Entry: Q7NQ01
LinkDB: Q7NQ01
Original site: Q7NQ01 
ID   DDLB_CHRVO              Reviewed;         303 AA.
AC   Q7NQ01;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   16-JAN-2019, entry version 108.
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};
GN   OrderedLocusNames=CV_4341;
OS   Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 /
OS   NBRC 12614 / NCIMB 9131 / NCTC 9757).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=243365;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 /
RC   NCTC 9757;
RX   PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA   Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T.,
RA   Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R.,
RA   Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F.,
RA   Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M.,
RA   Batista J.S., Belo A., van den Berg C., Bogo M., Bonatto S.,
RA   Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A.,
RA   Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M.,
RA   Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O.,
RA   Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L.,
RA   Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A.,
RA   Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R.,
RA   Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA   Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J.,
RA   Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P.,
RA   Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S.,
RA   di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M.,
RA   Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C.,
RA   Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O.,
RA   Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P.,
RA   Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E.,
RA   Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N.,
RA   Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C.,
RA   Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L.,
RA   Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T.,
RA   Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT   "The complete genome sequence of Chromobacterium violaceum reveals
RT   remarkable and exploitable bacterial adaptability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
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; AE016825; AAQ62000.1; -; Genomic_DNA.
DR   RefSeq; WP_011137887.1; NC_005085.1.
DR   ProteinModelPortal; Q7NQ01; -.
DR   SMR; Q7NQ01; -.
DR   STRING; 243365.CV_4341; -.
DR   EnsemblBacteria; AAQ62000; AAQ62000; CV_4341.
DR   GeneID; 24947279; -.
DR   KEGG; cvi:CV_4341; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   OrthoDB; 764798at2; -.
DR   BioCyc; CVIO243365:G1G08-4376-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001424; 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    303       D-alanine--D-alanine ligase B.
FT                                /FTId=PRO_0000177806.
FT   DOMAIN      103    298       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     129    184       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       252    252       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       265    265       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       265    265       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       267    267       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   303 AA;  32785 MW;  07D31BA64C7A941F CRC64;
     MKQYGKVAVL MGGSSSEREV SLMSGAGVLS ALRSKGVDAH GFDPSEKPLS ALKEEGFDCV
     FNILHGPFGE DGTLQGALEA LGMPYTGCGV MASAIAMDKW RTKLLWKGAG LPIPAFELLD
     ENSDFDAIER QLGLPIFVKP STEGSSIGVT KVKQPGELRA AFEEARKYDK VVIAEQFIGG
     GEYTCAVIGE TAYPTIKIEP ATEYYDYQAK YFRDDTVYRC PSGLAPEVEA RARELALKAF
     KVLGCRGWSR VDFLMDEAGE IYLLEANTSP GMTSHSLVPM AARAEGIAYE DLCLKVLDTV
     HVG
//
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