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Database: UniProt/SWISS-PROT
Entry: DDL_MICAN
LinkDB: DDL_MICAN
Original site: DDL_MICAN 
ID   DDL_MICAN               Reviewed;         352 AA.
AC   B0JHC1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 1.
DT   05-DEC-2018, entry version 70.
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=MAE_24510;
OS   Microcystis aeruginosa (strain NIES-843).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Microcystaceae; Microcystis.
OX   NCBI_TaxID=449447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-843;
RX   PubMed=18192279; DOI=10.1093/dnares/dsm026;
RA   Kaneko T., Nakajima N., Okamoto S., Suzuki I., Tanabe Y., Tamaoki M.,
RA   Nakamura Y., Kasai F., Watanabe A., Kawashima K., Kishida Y., Ono A.,
RA   Shimizu Y., Takahashi C., Minami C., Fujishiro T., Kohara M.,
RA   Katoh M., Nakazaki N., Nakayama S., Yamada M., Tabata S.,
RA   Watanabe M.M.;
RT   "Complete genomic structure of the bloom-forming toxic cyanobacterium
RT   Microcystis aeruginosa NIES-843.";
RL   DNA Res. 14:247-256(2007).
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; AP009552; BAG02273.1; -; Genomic_DNA.
DR   RefSeq; WP_012265582.1; NC_010296.1.
DR   ProteinModelPortal; B0JHC1; -.
DR   SMR; B0JHC1; -.
DR   STRING; 449447.MAE_24510; -.
DR   PaxDb; B0JHC1; -.
DR   EnsemblBacteria; BAG02273; BAG02273; MAE_24510.
DR   GeneID; 5863261; -.
DR   KEGG; mar:MAE_24510; -.
DR   PATRIC; fig|449447.4.peg.2247; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011593; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   OrthoDB; POG091H06GK; -.
DR   BioCyc; MAER449447:MAE_RS10705-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001510; 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    352       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000341135.
FT   DOMAIN      135    344       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     171    226       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       297    297       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       311    311       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       311    311       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       313    313       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   352 AA;  38821 MW;  83CD1692E170A602 CRC64;
     MDKIKVGLLF GGRSGEHEVS INSARSILQA FNYPENLDKY AVIPFYIDKN GCWHSAATAR
     QILTSGQPLA IESNIKVNIW QFPPEVREME VWFPILHGPN GEDGTLQGLL TLMRVAFVGS
     GVLGSCLGMD KIAMKTAFAA AGLPQVKYKA ITRSQVWSNP CVFPQLCDQI AEEIGYPCFI
     KPANLGSSVG ISKARNRQEL EAALDSAASY DRRIIVEAGV TAREIECAVL GNDNPQASLV
     GEITFDSDFY DYETKYTDGR SSMVIPANIP DKIANQVREM AVEAFKAVDA AGLSRVDFFY
     VENTGEVLIN EINTLPGFTN FSMYPQLWKA TGLEFDKLVD KLVQLALERQ EK
//
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