GenomeNet

Database: UniProt
Entry: O83676
LinkDB: O83676
Original site: O83676 
ID   DDL_TREPA               Reviewed;         396 AA.
AC   O83676;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   05-DEC-2018, entry version 116.
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=ddlA;
GN   OrderedLocusNames=TP_0670;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M.,
RA   Utterback T.R., McDonald L.A., Artiach P., Bowman C., Cotton M.D.,
RA   Fujii C., Garland S.A., Hatch B., Horst K., Roberts K.M., Sandusky M.,
RA   Weidman J.F., Smith H.O., Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis
RT   spirochete.";
RL   Science 281:375-388(1998).
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; AE000520; AAC26568.1; -; Genomic_DNA.
DR   PIR; A71296; A71296.
DR   RefSeq; WP_010882115.1; NC_021490.2.
DR   ProteinModelPortal; O83676; -.
DR   SMR; O83676; -.
DR   IntAct; O83676; 2.
DR   STRING; 243276.TP0670; -.
DR   EnsemblBacteria; AAC26568; AAC26568; TP_0670.
DR   GeneID; 34331815; -.
DR   KEGG; tpa:TP_0670; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000811; 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   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    396       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000177898.
FT   DOMAIN      141    347       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     174    229       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       301    301       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   396 AA;  42728 MW;  FB5829335B6111A5 CRC64;
     MVHVTLLYGG RSAEHDVSVR SARFVARTLC LQHTVMLIGI TRRGVWYAQP ACALEQLCTG
     TVALSIQEDE KRRVCLVPGG GTAGAFVIAG MPCVTDVVFP VLHGSYGEDG TVQGLLEMLQ
     VPYVGCGVCA SALAMDKVKA KMLWQAAGLP VLPFVFFRKD AWRMHMQEFV AQLETRLGYP
     LFVKPAQAGS SVGASAVQTR APLIPAIEAA FQWDEVVLVE RYVRAREIEC ALSGNGPYTV
     HGAGEVIAQG AFYDYEEKYA DASVARVLVT APLETAQYEQ ITTLALRAYE ALGLTGLARV
     DFFLLETGEV YVNEVNTMPG FTSISLFPQI CQAAGVAPQD LMAQLLSCAR ERFAARAALS
     TDLHAHVCAP SVTAAHDPDA QGDDWDQRDS NPLPTA
//
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