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Database: UniProt
Entry: Q9JSZ9
LinkDB: Q9JSZ9
Original site: Q9JSZ9 
ID   DDL_NEIMA               Reviewed;         304 AA.
AC   Q9JSZ9; A1ITP6;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   05-DEC-2018, entry version 109.
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=ddlB;
GN   OrderedLocusNames=NMA2060;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T.,
RA   Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S.,
RA   Jagels K., Leather S., Moule S., Mungall K.L., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA   Whitehead S., Spratt B.G., Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria
RT   meningitidis Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM09163.1; -; Genomic_DNA.
DR   PIR; H81776; H81776.
DR   RefSeq; WP_002236713.1; NC_003116.1.
DR   ProteinModelPortal; Q9JSZ9; -.
DR   SMR; Q9JSZ9; -.
DR   EnsemblBacteria; CAM09163; CAM09163; NMA2060.
DR   KEGG; nma:NMA2060; -.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   BioCyc; NMEN122587:NMA_RS10460-MONOMER; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000626; 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    304       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000177845.
FT   DOMAIN      103    299       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     129    184       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       253    253       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       266    266       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       266    266       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       268    268       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   304 AA;  32587 MW;  83C08DAC869EE84C CRC64;
     MQNFGKVAVL MGGFSSEREI SLDSGTAILN ALKSKGIDAY AFDPKETPLS ELKAQGFQTA
     FNILHGTYGE DGAVQGALEL LGIPYTGSGV AASAIGMDKY RCKLIWQALG LPVPEFAVLH
     DDTDFDAVEE KLGLPMFVKP AAEGSSVGVV KVKGKGRLKS VYEELKHFQG EIIAERFIGG
     GEYSCPVLNG KGLPGIHIIP ATEFYDYEAK YNRNDTIYQC PSEDLTEAEE SLMRELAVRG
     AQAIGAEGCV RVDFLKDTDG KLYLLEINTL PGMTGHSLVP KSAAVMGVGF ADLCIEILKT
     AHVG
//
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