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Database: UniProt/SWISS-PROT
Entry: DDL_STREM
LinkDB: DDL_STREM
Original site: DDL_STREM 
ID   DDL_STREM               Reviewed;         348 AA.
AC   B4U1Z2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   23-MAY-2018, entry version 62.
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};
GN   OrderedLocusNames=Sez_0642;
OS   Streptococcus equi subsp. zooepidemicus (strain MGCS10565).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=552526;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGCS10565;
RX   PubMed=18716664; DOI=10.1371/journal.pone.0003026;
RA   Beres S.B., Sesso R., Pinto S.W.L., Hoe N.P., Porcella S.F.,
RA   Deleo F.R., Musser J.M.;
RT   "Genome sequence of a lancefield group C Streptococcus zooepidemicus
RT   strain causing epidemic nephritis: new information about an old
RT   disease.";
RL   PLoS ONE 3:E3026-E3026(2008).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000255|HAMAP-Rule:MF_00047}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {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; CP001129; ACG62009.1; -; Genomic_DNA.
DR   RefSeq; WP_012515285.1; NC_011134.1.
DR   ProteinModelPortal; B4U1Z2; -.
DR   SMR; B4U1Z2; -.
DR   PRIDE; B4U1Z2; -.
DR   EnsemblBacteria; ACG62009; ACG62009; Sez_0642.
DR   KEGG; sez:Sez_0642; -.
DR   HOGENOM; HOG000011593; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   BioCyc; SEQU552526:G1GCI-649-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001873; 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-EC.
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-UniPathway.
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    348       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_1000116639.
FT   DOMAIN      132    334       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     162    217       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       288    288       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       301    301       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       301    301       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       303    303       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   348 AA;  38789 MW;  5A1E266C7C157740 CRC64;
     MSKQTLILLY GGRSAEREVS VLSAESVMRA IDYTKFFVKT YFISQTGQFI KTQEFSSQPA
     ATERLMTNAT IRLEQQIRPS DIYEEGAVVF PVLHGPMGED GSIQGFLEVL KMPYVGTNIL
     SSSVAMDKIT TKRVLESADI PQVAYTVYIE GQDLDRCLAE TEAVLSYPVF VKPANMGSSV
     GISKAESEEE LRAAILLALT YDSRILIEQG VLAREIEVGL LGNTDVKSTL PGEVVKNVDF
     YDYQAKYIDN EITMAIPAAI DESAMTSMRT YAETAFKAIG ACGLSRCDFF LGQDGQIYLN
     ELNTMPGFTQ WSMYPLLWEH MGLSYAELIE ELVRLAQEMF EKREGHLI
//
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