GenomeNet

Database: UniProt
Entry: Q81Q29
LinkDB: Q81Q29
Original site: Q81Q29 
ID   DDL_BACAN               Reviewed;         304 AA.
AC   Q81Q29; Q6HY93; Q6KY66;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   05-DEC-2018, entry version 122.
DE   RecName: Full=D-alanine--D-alanine ligase {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 {ECO:0000255|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase {ECO:0000255|HAMAP-Rule:MF_00047};
GN   Name=ddl {ECO:0000255|HAMAP-Rule:MF_00047}; Synonyms=ddlB;
GN   OrderedLocusNames=BA_2610, GBAA_2610, BAS2435;
OS   Bacillus anthracis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1392;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames / isolate Porton;
RX   PubMed=12721629; DOI=10.1038/nature01586;
RA   Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA   Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA   Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA   Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA   DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H.,
RA   Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D.,
RA   Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F.,
RA   Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C.,
RA   Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O.,
RA   Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA   Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT   "The genome sequence of Bacillus anthracis Ames and comparison to
RT   closely related bacteria.";
RL   Nature 423:81-86(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ames ancestor;
RX   PubMed=18952800; DOI=10.1128/JB.01347-08;
RA   Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA   Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT   "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL   J. Bacteriol. 191:445-446(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sterne;
RA   Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA   Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA   Richardson P., Rubin E., Tice H.;
RT   "Complete genome sequence of Bacillus anthracis Sterne.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE016879; AAP26458.1; -; Genomic_DNA.
DR   EMBL; AE017334; AAT31727.1; -; Genomic_DNA.
DR   EMBL; AE017225; AAT54746.1; -; Genomic_DNA.
DR   RefSeq; NP_844972.1; NC_003997.3.
DR   RefSeq; WP_003157623.1; NZ_QPKQ01000001.1.
DR   RefSeq; YP_028695.1; NC_005945.1.
DR   PDB; 3R23; X-ray; 2.50 A; A/B=1-304.
DR   PDB; 3R5X; X-ray; 2.00 A; A/B/C/D=1-304.
DR   PDBsum; 3R23; -.
DR   PDBsum; 3R5X; -.
DR   ProteinModelPortal; Q81Q29; -.
DR   SMR; Q81Q29; -.
DR   STRING; 260799.BAS2435; -.
DR   DNASU; 1086552; -.
DR   EnsemblBacteria; AAP26458; AAP26458; BA_2610.
DR   EnsemblBacteria; AAT31727; AAT31727; GBAA_2610.
DR   EnsemblBacteria; AAT54746; AAT54746; BAS2435.
DR   GeneID; 1086552; -.
DR   GeneID; 2852726; -.
DR   KEGG; ban:BA_2610; -.
DR   KEGG; banh:HYU01_12950; -.
DR   KEGG; bar:GBAA_2610; -.
DR   KEGG; bat:BAS2435; -.
DR   PATRIC; fig|198094.11.peg.2589; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000427; Chromosome.
DR   Proteomes; UP000000594; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Peptidoglycan synthesis; Reference proteome.
FT   CHAIN         1    304       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000177781.
FT   DOMAIN       99    293       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     126    181       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       248    248       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       260    260       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       260    260       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       262    262       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   STRAND        1      7       {ECO:0000244|PDB:3R5X}.
FT   HELIX        11     27       {ECO:0000244|PDB:3R5X}.
FT   TURN         30     32       {ECO:0000244|PDB:3R5X}.
FT   STRAND       33     39       {ECO:0000244|PDB:3R5X}.
FT   HELIX        43     45       {ECO:0000244|PDB:3R5X}.
FT   HELIX        46     49       {ECO:0000244|PDB:3R5X}.
FT   TURN         50     52       {ECO:0000244|PDB:3R5X}.
FT   STRAND       54     58       {ECO:0000244|PDB:3R5X}.
FT   HELIX        63     66       {ECO:0000244|PDB:3R5X}.
FT   HELIX        69     77       {ECO:0000244|PDB:3R5X}.
FT   STRAND       81     84       {ECO:0000244|PDB:3R5X}.
FT   HELIX        86     93       {ECO:0000244|PDB:3R5X}.
FT   HELIX        95    104       {ECO:0000244|PDB:3R5X}.
FT   STRAND      112    119       {ECO:0000244|PDB:3R5X}.
FT   HELIX       123    129       {ECO:0000244|PDB:3R5X}.
FT   STRAND      131    137       {ECO:0000244|PDB:3R5X}.
FT   STRAND      142    144       {ECO:0000244|PDB:3R23}.
FT   STRAND      147    149       {ECO:0000244|PDB:3R5X}.
FT   HELIX       152    165       {ECO:0000244|PDB:3R5X}.
FT   STRAND      167    173       {ECO:0000244|PDB:3R5X}.
FT   STRAND      177    185       {ECO:0000244|PDB:3R5X}.
FT   STRAND      193    202       {ECO:0000244|PDB:3R5X}.
FT   STRAND      205    217       {ECO:0000244|PDB:3R5X}.
FT   HELIX       222    238       {ECO:0000244|PDB:3R5X}.
FT   STRAND      243    252       {ECO:0000244|PDB:3R5X}.
FT   STRAND      255    264       {ECO:0000244|PDB:3R5X}.
FT   HELIX       272    279       {ECO:0000244|PDB:3R5X}.
FT   HELIX       284    302       {ECO:0000244|PDB:3R5X}.
SQ   SEQUENCE   304 AA;  33852 MW;  FB85F1B59BC2B9B2 CRC64;
     MRIGVIMGGV SSEKQVSIMT GNEMIANLDK NKYEIVPITL NEKMDLIEKA KDIDFALLAL
     HGKYGEDGTV QGTLESLGIP YSGSNMLSSG ICMDKNISKK ILRYEGIETP DWIELTKMED
     LNFDELDKLG FPLVVKPNSG GSSVGVKIVY DKDELISMLE TVFEWDSEVV IEKYIKGEEI
     TCSIFDGKQL PIISIRHAAE FFDYNAKYDD ASTIEEVIEL PAELKERVNK ASLACYKALK
     CSVYARVDMM VKDGIPYVME VNTLPGMTQA SLLPKSADAA GIHYSKLLDM IIETSLRVRK
     EEGF
//
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