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Database: UniProt
Entry: Q9ZBR9
LinkDB: Q9ZBR9
Original site: Q9ZBR9 
ID   DDL_STRCO               Reviewed;         389 AA.
AC   Q9ZBR9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JAN-2019, entry version 126.
DE   RecName: Full=D-alanine--D-alanine ligase;
DE            EC=6.3.2.4;
DE   AltName: Full=D-Ala-D-Ala ligase;
DE   AltName: Full=D-alanylalanine synthetase;
GN   Name=ddl; Synonyms=ddlA; OrderedLocusNames=SCO5560; ORFNames=SC7A1.04;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000250}.
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   -!- 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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000305}.
DR   EMBL; AL939124; CAA22403.1; -; Genomic_DNA.
DR   PIR; T35644; T35644.
DR   RefSeq; NP_629695.1; NC_003888.3.
DR   RefSeq; WP_003973434.1; NC_003888.3.
DR   ProteinModelPortal; Q9ZBR9; -.
DR   SMR; Q9ZBR9; -.
DR   STRING; 100226.SCO5560; -.
DR   EnsemblBacteria; CAA22403; CAA22403; CAA22403.
DR   GeneID; 1101001; -.
DR   KEGG; sco:SCO5560; -.
DR   PATRIC; fig|100226.15.peg.5649; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011593; -.
DR   InParanoid; Q9ZBR9; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   PhylomeDB; Q9ZBR9; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IBA:GO_Central.
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; IBA:GO_Central.
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    389       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000177885.
FT   DOMAIN      169    379       ATP-grasp.
FT   NP_BIND     205    260       ATP. {ECO:0000250}.
FT   METAL       333    333       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       346    346       Magnesium or manganese 1. {ECO:0000250}.
FT   METAL       346    346       Magnesium or manganese 2. {ECO:0000250}.
FT   METAL       348    348       Magnesium or manganese 2. {ECO:0000250}.
SQ   SEQUENCE   389 AA;  42273 MW;  9F25CE27B761DF49 CRC64;
     MSTENLPQNP EQSPRRPPRK PRVAVVFGGR SSEHGISVVT AGAVLAAIDR TRYDVLPIGI
     TRDGRWALTA DEPERMAITE RRTPDVEELA ESTEGGVLLP VDPANREVVY SEPGSVPKAL
     GEVDVVFPVL HGPYGEDGTL QGLLELSGVP YVGAGVLASA VGQDKEYMKA VFTSYGLKVG
     PYAVIRPREW EQDRSGARKK IVDFAGEHGW PLFVKPARAG SSIGITKVDD LAGLDEAIEE
     ARRHDPKILV EAALRGREIE CGVLEFEDGP RASVPAEIPP PSEHAYYDFE AKYIDSTPGI
     VPAPLTAEET AEVQRLAVAA FDAASCEGLV RADFFLTEDD EFVINEINTM PGFTPISMYP
     QMWQASGVSY PELVDRLVQA ALRRPTGLR
//
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