GenomeNet

Database: UniProt
Entry: Q89GA7
LinkDB: Q89GA7
Original site: Q89GA7 
ID   DDLA_BRADU              Reviewed;         373 AA.
AC   Q89GA7;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JAN-2019, entry version 102.
DE   RecName: Full=D-alanine--D-alanine ligase A {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 A {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthase A;
GN   Name=ddlA {ECO:0000255|HAMAP-Rule:MF_00047};
GN   OrderedLocusNames=blr6438;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC
OS   14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T.,
RA   Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K.,
RA   Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M.,
RA   Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; BA000040; BAC51703.1; -; Genomic_DNA.
DR   RefSeq; NP_773078.1; NC_004463.1.
DR   RefSeq; WP_011089178.1; NZ_CP011360.1.
DR   ProteinModelPortal; Q89GA7; -.
DR   SMR; Q89GA7; -.
DR   STRING; 224911.blr6438; -.
DR   PRIDE; Q89GA7; -.
DR   EnsemblBacteria; BAC51703; BAC51703; BAC51703.
DR   GeneID; 1047518; -.
DR   KEGG; bja:blr6438; -.
DR   PATRIC; fig|224911.44.peg.6424; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011593; -.
DR   KO; K01921; -.
DR   OMA; RTAKWIT; -.
DR   PhylomeDB; Q89GA7; -.
DR   BioCyc; BDIA224911:G1G3J-6485-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002526; 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    373       D-alanine--D-alanine ligase A.
FT                                /FTId=PRO_0000177792.
FT   DOMAIN      146    355       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     179    234       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       308    308       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       322    322       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       322    322       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       324    324       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   373 AA;  40799 MW;  896E99143E48A84C CRC64;
     MADKIRVVVL YGGRSGEHEV SLKSAASVFR HLDRTRFEVI PVSIDKTGRW QWNDLRSLDQ
     AHAAALPILP DAPEMRLARG PDGRGVLVPI TQGAAAPIAI DVVFPVIHGP LCEDGTVQGL
     LELADVAYVG SGVLASAVSM DKDVAKRLAE FAGIPVAPYR VLTRKAFVQD RVSSLAKAVE
     GLSLPVFVKP CNMGSSVGIH KVKTQDALEA ALDDAFRYDV KVLVQQGIDA REIEVAVLED
     ETLFASLASE LNPNAHHEFY SYEAKYLDPD GARVDLPARL DAAQMERVRS LATRVFAALE
     CSGFARVDFF LDRKTGEFCF NEINTLPGFT SISMYPKMME ASGVPYGELL SRLVDLALDR
     HRQRQSLERG YAS
//
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