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Database: UniProt
Entry: Q5HEB7
LinkDB: Q5HEB7
Original site: Q5HEB7 
ID   DDL_STAAC               Reviewed;         356 AA.
AC   Q5HEB7;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   05-DEC-2018, entry version 97.
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=SACOL2074;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
RX   PubMed=15774886; DOI=10.1128/JB.187.7.2426-2438.2005;
RA   Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T.,
RA   Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J.,
RA   Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S.,
RA   Haft D.H., Vamathevan J.J., Khouri H., Utterback T.R., Lee C.,
RA   Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H.,
RA   Hance I.R., Nelson K.E., Fraser C.M.;
RT   "Insights on evolution of virulence and resistance from the complete
RT   genome analysis of an early methicillin-resistant Staphylococcus
RT   aureus strain and a biofilm-producing methicillin-resistant
RT   Staphylococcus epidermidis strain.";
RL   J. Bacteriol. 187:2426-2438(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; CP000046; AAW37036.1; -; Genomic_DNA.
DR   RefSeq; WP_000159631.1; NC_002951.2.
DR   PDB; 2I80; X-ray; 2.19 A; A/B=1-356.
DR   PDB; 2I87; X-ray; 2.00 A; A/B=1-356.
DR   PDB; 2I8C; X-ray; 2.46 A; A/B=1-356.
DR   PDB; 3N8D; X-ray; 2.30 A; A/B=1-356.
DR   PDBsum; 2I80; -.
DR   PDBsum; 2I87; -.
DR   PDBsum; 2I8C; -.
DR   PDBsum; 3N8D; -.
DR   ProteinModelPortal; Q5HEB7; -.
DR   SMR; Q5HEB7; -.
DR   STRING; 93062.SACOL2074; -.
DR   EnsemblBacteria; AAW37036; AAW37036; SACOL2074.
DR   KEGG; sac:SACOL2074; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011593; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   BioCyc; MetaCyc:MONOMER-15463; -.
DR   BioCyc; SAUR93062:G1G4B-2280-MONOMER; -.
DR   BRENDA; 6.3.2.4; 3352.
DR   UniPathway; UPA00219; -.
DR   EvolutionaryTrace; Q5HEB7; -.
DR   Proteomes; UP000000530; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cell shape;
KW   Cell wall biogenesis/degradation; Complete proteome; Cytoplasm;
KW   Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW   Peptidoglycan synthesis.
FT   CHAIN         1    356       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000177874.
FT   DOMAIN      134    339       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     167    222       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       293    293       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       306    306       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       306    306       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       308    308       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   STRAND        4     11       {ECO:0000244|PDB:2I87}.
FT   STRAND       13     15       {ECO:0000244|PDB:2I87}.
FT   HELIX        17     29       {ECO:0000244|PDB:2I87}.
FT   TURN         33     35       {ECO:0000244|PDB:2I87}.
FT   STRAND       36     43       {ECO:0000244|PDB:2I87}.
FT   STRAND       49     52       {ECO:0000244|PDB:2I87}.
FT   HELIX        62     64       {ECO:0000244|PDB:2I87}.
FT   HELIX        67     69       {ECO:0000244|PDB:2I87}.
FT   STRAND       70     73       {ECO:0000244|PDB:2I87}.
FT   HELIX        77     80       {ECO:0000244|PDB:2I87}.
FT   STRAND       85     87       {ECO:0000244|PDB:2I87}.
FT   STRAND       89     94       {ECO:0000244|PDB:2I87}.
FT   STRAND       98    100       {ECO:0000244|PDB:2I87}.
FT   HELIX       104    112       {ECO:0000244|PDB:2I87}.
FT   STRAND      116    118       {ECO:0000244|PDB:2I87}.
FT   HELIX       121    128       {ECO:0000244|PDB:2I87}.
FT   HELIX       130    140       {ECO:0000244|PDB:2I87}.
FT   STRAND      147    151       {ECO:0000244|PDB:2I87}.
FT   HELIX       152    169       {ECO:0000244|PDB:2I87}.
FT   STRAND      172    180       {ECO:0000244|PDB:2I87}.
FT   STRAND      182    184       {ECO:0000244|PDB:3N8D}.
FT   STRAND      188    192       {ECO:0000244|PDB:2I87}.
FT   HELIX       193    204       {ECO:0000244|PDB:2I87}.
FT   STRAND      208    214       {ECO:0000244|PDB:2I87}.
FT   STRAND      219    230       {ECO:0000244|PDB:2I87}.
FT   STRAND      237    239       {ECO:0000244|PDB:2I87}.
FT   STRAND      259    262       {ECO:0000244|PDB:2I87}.
FT   HELIX       267    283       {ECO:0000244|PDB:2I87}.
FT   STRAND      288    296       {ECO:0000244|PDB:2I87}.
FT   STRAND      302    310       {ECO:0000244|PDB:2I87}.
FT   HELIX       318    325       {ECO:0000244|PDB:2I87}.
FT   HELIX       330    356       {ECO:0000244|PDB:2I87}.
SQ   SEQUENCE   356 AA;  40231 MW;  65822883958DC645 CRC64;
     MTKENICIVF GGKSAEHEVS ILTAQNVLNA IDKDKYHVDI IYITNDGDWR KQNNITAEIK
     STDELHLENG EALEISQLLK ESSSGQPYDA VFPLLHGPNG EDGTIQGLFE VLDVPYVGNG
     VLSAASSMDK LVMKQLFEHR GLPQLPYISF LRSEYEKYEH NILKLVNDKL NYPVFVKPAN
     LGSSVGISKC NNEAELKEGI KEAFQFDRKL VIEQGVNARE IEVAVLGNDY PEATWPGEVV
     KDVAFYDYKS KYKDGKVQLQ IPADLDEDVQ LTLRNMALEA FKATDCSGLV RADFFVTEDN
     QIYINETNAM PGFTAFSMYP KLWENMGLSY PELITKLIEL AKERHQDKQK NKYKID
//
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