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Database: UniProt
Entry: A8F110
LinkDB: A8F110
Original site: A8F110 
ID   DDL_RICM5               Reviewed;         321 AA.
AC   A8F110;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   05-DEC-2018, entry version 75.
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=RMA_0341;
OS   Rickettsia massiliae (strain Mtu5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=416276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mtu5;
RX   PubMed=17916642; DOI=10.1101/gr.6742107;
RA   Blanc G., Ogata H., Robert C., Audic S., Claverie J.-M., Raoult D.;
RT   "Lateral gene transfer between obligate intracellular bacteria:
RT   evidence from the Rickettsia massiliae genome.";
RL   Genome Res. 17:1657-1664(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; CP000683; ABV84596.1; -; Genomic_DNA.
DR   RefSeq; WP_012152573.1; NC_009900.1.
DR   ProteinModelPortal; A8F110; -.
DR   SMR; A8F110; -.
DR   EnsemblBacteria; ABV84596; ABV84596; RMA_0341.
DR   KEGG; rms:RMA_0341; -.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001311; 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    321       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_1000057329.
FT   DOMAIN      121    315       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     147    199       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       268    268       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       282    282       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       282    282       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       284    284       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   321 AA;  35920 MW;  3DD68EED3FE3EA73 CRC64;
     MHKYQTHWVE HSIVKILSSA GKKYIALMAG GMSAEREVSL VSSEGVSKAL IELGYSVTFI
     DMGADITVRL QEIKPDIVFN CLHGTYGEDG CLPGLLNIMR IPYTHSGMLS SALAFNKIHS
     RSWFLTNNIN MAESIVVNKS DNIKNDPMKR PYVIKPLTQG SSIGVEVIFA EDNFNFADYD
     FPYGDQVIIE QYIKGRELQV AVLNGKALGV LEIKLLKNRF YDYETKYTEG FADHLCPAPL
     PANLYEKLLI ESEKIYKTMN CKGPARAEFI LEEQTNKLYA LELNTHPGMT PLSIVPEIAA
     YAGINFTNLI EEIIKTASFE S
//
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