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Database: UniProt
Entry: Q4JUX6
LinkDB: Q4JUX6
Original site: Q4JUX6 
ID   DDL_CORJK               Reviewed;         373 AA.
AC   Q4JUX6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JAN-2019, entry version 93.
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}; OrderedLocusNames=jk1217;
OS   Corynebacterium jeikeium (strain K411).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=306537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K411;
RX   PubMed=15968079; DOI=10.1128/JB.187.13.4671-4682.2005;
RA   Tauch A., Kaiser O., Hain T., Goesmann A., Weisshaar B.,
RA   Albersmeier A., Bekel T., Bischoff N., Brune I., Chakraborty T.,
RA   Kalinowski J., Meyer F., Rupp O., Schneiker S., Viehoever P.,
RA   Puehler A.;
RT   "Complete genome sequence and analysis of the multiresistant
RT   nosocomial pathogen Corynebacterium jeikeium K411, a lipid-requiring
RT   bacterium of the human skin flora.";
RL   J. Bacteriol. 187:4671-4682(2005).
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; CR931997; CAI37381.1; -; Genomic_DNA.
DR   RefSeq; WP_011273733.1; NC_007164.1.
DR   ProteinModelPortal; Q4JUX6; -.
DR   SMR; Q4JUX6; -.
DR   STRING; 306537.jk1217; -.
DR   EnsemblBacteria; CAI37381; CAI37381; jk1217.
DR   GeneID; 3433693; -.
DR   KEGG; cjk:jk1217; -.
DR   PATRIC; fig|306537.10.peg.1232; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011593; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   OrthoDB; 764798at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000545; 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   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   InterPro; IPR011761; ATP-grasp.
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    373       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000341086.
FT   DOMAIN      165    369       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     192    247       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       324    324       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       336    336       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       336    336       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       338    338       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   373 AA;  38958 MW;  CE68144B565BE606 CRC64;
     MSNEAKKHAR TTVAVLYGGQ STEHSVSCIS AGAVIDHLDP EIYEVVPVGI TEAGAWVPGT
     TDTSRLRADG RDMPRVEDGG VHVQLTFGGA GTAGSAGSGA AGEMRYVTGP QAGEVFAQVD
     VVFPVLHGVN GEDGTVQGVL DLAGVRYVGN GVLASAAGMD KDFTKRLARE AGIPVGEELI
     LFQPRELTAE EKERLGLPVF VKPARGGSSI GISKVDSWEE FDAAIDLAFS NDNKVIVEAM
     IHGAEVECGV LQHADGSIVS SVPAMLNGTE DGAEGFYGFD AKYVDSTVSA TIPAPLPAET
     IKEIRQLAIR TFNALGCDGI ARVDFFATEN GPVLNEINTM PGFTPISMYP KMFAAEGVSF
     GDLVSALIAR ALA
//
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