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Database: UniProt
Entry: Q73IQ8
LinkDB: Q73IQ8
Original site: Q73IQ8 
ID   DDL_WOLPM               Reviewed;         315 AA.
AC   Q73IQ8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   05-DEC-2018, entry version 111.
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=WD_0095;
OS   Wolbachia pipientis wMel.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=163164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15024419; DOI=10.1371/journal.pbio.0020069;
RA   Wu M., Sun L.V., Vamathevan J.J., Riegler M., DeBoy R.T.,
RA   Brownlie J.C., McGraw E.A., Martin W., Esser C., Ahmadinejad N.,
RA   Wiegand C., Madupu R., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   Durkin A.S., Kolonay J.F., Nelson W.C., Mohamoud Y., Lee P.,
RA   Berry K.J., Young M.B., Utterback T.R., Weidman J.F., Nierman W.C.,
RA   Paulsen I.T., Nelson K.E., Tettelin H., O'Neill S.L., Eisen J.A.;
RT   "Phylogenomics of the reproductive parasite Wolbachia pipientis wMel:
RT   a streamlined genome overrun by mobile genetic elements.";
RL   PLoS Biol. 2:327-341(2004).
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; AE017196; AAS13853.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q73IQ8; -.
DR   SMR; Q73IQ8; -.
DR   STRING; 163164.WD0095; -.
DR   EnsemblBacteria; AAS13853; AAS13853; WD_0095.
DR   KEGG; wol:WD_0095; -.
DR   eggNOG; ENOG4105CPF; Bacteria.
DR   eggNOG; COG1181; LUCA.
DR   HOGENOM; HOG000011592; -.
DR   KO; K01921; -.
DR   OMA; YETKYTE; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000008215; 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.
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    315       D-alanine--D-alanine ligase.
FT                                /FTId=PRO_0000341195.
FT   DOMAIN      101    297       ATP-grasp. {ECO:0000255|HAMAP-
FT                                Rule:MF_00047}.
FT   NP_BIND     128    181       ATP. {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       249    249       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       263    263       Magnesium or manganese 1.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       263    263       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
FT   METAL       265    265       Magnesium or manganese 2.
FT                                {ECO:0000255|HAMAP-Rule:MF_00047}.
SQ   SEQUENCE   315 AA;  35482 MW;  87868BA2A031C118 CRC64;
     MIPTIAILSG GFSCEREISL MSGKAVKKAL DSLSYNAIEI DVDSNIAEKL KKINPGLAFI
     ALHGPYGEDG CIQGLLEILG IKYTHSGVMA SAVAINKVMS KHIFRSLNID TPKGYVISRE
     DVLKNNIKID YPYVLKPINE GSSIGVYIIF SHEDYLELKN NSSTIMEKMI VEEYIPGIEL
     HTAVLLDEAI GTIEVRPKNK FYDYEAKYTD GFAEHIFPAK IPDNIYKMTL EHALKIHQFL
     GCKTISRSDF RYNPKNNTLK MLEINTHPGF TELSLVPEIA KLAKGINFNE LVKIIIEDSL
     QHKNIRDLSH VEQYY
//
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