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Database: UniProt
Entry: Q81D33
LinkDB: Q81D33
Original site: Q81D33 
ID   DDLA_BACCR              Reviewed;         301 AA.
AC   Q81D33;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   05-DEC-2018, entry version 107.
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 synthetase A {ECO:0000255|HAMAP-Rule:MF_00047};
GN   Name=ddlA {ECO:0000255|HAMAP-Rule:MF_00047};
GN   OrderedLocusNames=BC_2550;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 /
OS   NCIMB 9373 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL
RC   B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA   Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA   Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA   Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA   Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with
RT   Bacillus anthracis.";
RL   Nature 423:87-91(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; AE016877; AAP09509.1; -; Genomic_DNA.
DR   RefSeq; NP_832308.1; NC_004722.1.
DR   RefSeq; WP_011110115.1; NC_004722.1.
DR   ProteinModelPortal; Q81D33; -.
DR   SMR; Q81D33; -.
DR   STRING; 226900.BC2550; -.
DR   EnsemblBacteria; AAP09509; AAP09509; BC_2550.
DR   GeneID; 1204899; -.
DR   KEGG; bce:BC2550; -.
DR   PATRIC; fig|226900.8.peg.2589; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   KO; K01921; -.
DR   OMA; MQGLLEC; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001417; 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; 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    301       D-alanine--D-alanine ligase A.
FT                                /FTId=PRO_0000177782.
FT   DOMAIN       96    290       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     123    178       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       245    245       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       257    257       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       257    257       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       259    259       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   301 AA;  33595 MW;  4F3304CD90438BFE CRC64;
     MLLWAGYASE KQVSIMTGNE MIAHLDKNKY EIVPITLNEK MDLIEKAKDI DFALLALHGK
     YGEDGTVQGT LESLGIPYSG SNMLSSSICM DKNISKKILR YEGVETPDWI ELTKMEDLNL
     DELDKLGFPL VVKPNSGGSS VGVKIVYNKN ELISMLETVF EWDSEVVIEK YIKGDEITCS
     ILDGKQLPIV SIRHAAEFFD YNAKYDDTST VEEVIELPAQ IKERVNKASL TCYKALKCSV
     YARVDMMVKD GIPYVMEINT LPGMTQSSLL PKSAEAAGIS YSKLLDMIIE TSLKVRNEEG
     F
//
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