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Database: UniProt
Entry: P0CB57
LinkDB: P0CB57
Original site: P0CB57 
ID   DDL_STRPN               Reviewed;         347 AA.
AC   P0CB57; O54631;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 1.
DT   05-DEC-2018, entry version 55.
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=SP_1671;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T.,
RA   Hickey E.K., Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C.,
RA   Dougherty B.A., Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 155-300.
RA   Zhi-Yuan S., Enright M.C., Wilkinson P., Spratt B.G.;
RT   "Identification of three major clones of multiply antibiotic resistant
RT   Streptococcus pneumoniae in Taiwanese hospitals using multilocus
RT   sequence typing.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 155-301.
RC   STRAIN=Various strains;
RA   Coffey T.J., Enright M.C., Daniels M., Wilkinson P., Berron S.,
RA   Fenoll A., Spratt B.G.;
RT   "Recombinational exchanges at the capsular polysaccharide biosynthetic
RT   locus lead to frequent serotype changes among natural isolates of
RT   Streptococcus pneumoniae.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 155-301.
RC   STRAIN=Various strains;
RX   PubMed=9846740; DOI=10.1099/00221287-144-11-3049;
RA   Enright M.C., Spratt B.G.;
RT   "A multilocus sequence typing scheme for Streptococcus pneumoniae:
RT   identification of clones associated with serious invasive disease.";
RL   Microbiology 144:3049-3060(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; AE005672; AAK75750.1; -; Genomic_DNA.
DR   EMBL; AJ233887; CAA13580.1; -; Genomic_DNA.
DR   EMBL; Z99894; CAB17019.1; -; Genomic_DNA.
DR   EMBL; Z99837; CAB16962.1; -; Genomic_DNA.
DR   EMBL; Z99844; CAB16969.1; -; Genomic_DNA.
DR   EMBL; Z99845; CAB16970.1; -; Genomic_DNA.
DR   EMBL; Z99878; CAB17003.1; -; Genomic_DNA.
DR   EMBL; Z99893; CAB17018.1; -; Genomic_DNA.
DR   EMBL; AJ232272; CAA13275.1; -; Genomic_DNA.
DR   EMBL; AJ232245; CAA13248.1; -; Genomic_DNA.
DR   EMBL; AJ232254; CAA13257.1; -; Genomic_DNA.
DR   EMBL; AJ232260; CAA13263.1; -; Genomic_DNA.
DR   EMBL; AJ232267; CAA13270.1; -; Genomic_DNA.
DR   EMBL; AJ232268; CAA13271.1; -; Genomic_DNA.
DR   PIR; E95194; E95194.
DR   ProteinModelPortal; P0CB57; -.
DR   SMR; P0CB57; -.
DR   EnsemblBacteria; AAK75750; AAK75750; SP_1671.
DR   KEGG; spn:SP_1671; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011593; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000585; 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.
FT   CHAIN         1    347       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000177887.
FT   DOMAIN      131    333       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     161    216       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       287    287       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       300    300       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       300    300       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       302    302       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   CONFLICT    250    250       K -> N (in Ref. 1; AAK75750).
FT                                {ECO:0000305}.
SQ   SEQUENCE   347 AA;  38717 MW;  AFCF7AB1E53F9289 CRC64;
     MKQTIILLYG GRSAEREVSV LSAESVMRAV DYDRFTVKTF FISQSGDFIK TQEFSHAPGQ
     EDRLMTNETI DWDKKVAPSA IYEEGAVVFP VLHGPMGEDG SVQGFLEVLK MPYVGCNILS
     SSLAMDKITT KRVLESAGIA QVPYVAIVEG DDVTAKIAEV EEKLAYPVFT KPSNMGSSVG
     ISKSENQEEL RQALKLAFRY DSRVLVEQGV NAREIEVGLL GNYDVKSTLP GEVVKDVAFY
     DYDAKYIDNK ITMDIPAKIS DDVVAVMRQN AETAFRAIGG LGLSRCDFFY TDKGEIFLNE
     LNTMPGFTQW SMYPLLWDNM GISYPKLIER LVDLAKESFD KREAHLI
//
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