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Database: UniProt
Entry: Q5ZSA7
LinkDB: Q5ZSA7
Original site: Q5ZSA7 
ID   DDL_LEGPH               Reviewed;         364 AA.
AC   Q5ZSA7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   05-DEC-2018, entry version 102.
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}; OrderedLocusNames=lpg2612;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 /
OS   ATCC 33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M.,
RA   Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J.,
RA   Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R.,
RA   Pampou S., Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E.,
RA   Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G.,
RA   Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J.,
RA   Ju J., Kalachikov S., Shuman H.A., Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella
RT   pneumophila.";
RL   Science 305:1966-1968(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAU28670.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE017354; AAU28670.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_096617.1; NC_002942.5.
DR   ProteinModelPortal; Q5ZSA7; -.
DR   SMR; Q5ZSA7; -.
DR   STRING; 272624.lpg2612; -.
DR   PaxDb; Q5ZSA7; -.
DR   PRIDE; Q5ZSA7; -.
DR   EnsemblBacteria; AAU28670; AAU28670; lpg2612.
DR   GeneID; 19834177; -.
DR   KEGG; lpn:lpg2612; -.
DR   PATRIC; fig|272624.6.peg.2787; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011593; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000609; 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; 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    364       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000341125.
FT   DOMAIN      134    347       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     167    222       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       300    300       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       314    314       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       314    314       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       316    316       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   364 AA;  40422 MW;  5877A15DE7E53AAD CRC64;
     MSKPVNLVLL YGGKSGEHEV SLVSAASVLK HLDSEKYHII PIAMDKSGRF HRHDYNDLLA
     CSDKLPVVTE KSTPLEGLLI NGRLAVDAKI VFPVVHGPLY EDGCLQGLLE LAGVAYVGCD
     VLSSAIGMDK DMARRLACIN GLKSARYKLL SWHANASERQ QFCHEVASEF GWPLFVKPCS
     LGSSVGIHKA NNMDELNAAV ADALRYDEEI LVEEFIVGRE IELAVLENSI PCGKPRVSMV
     GEIKVNHPDG YYSYTAKYLE SSQTDLIIPA QLNNSLEEQL KQAAANIFSY LKCKGMARVD
     FFVNDKTEEI YFNEINTLPG FTSISMYPKL WQATGIAYPD LLDELINLAM VHHNCRQHLV
     TNYL
//
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