ID   DDL_ANACE               Reviewed;         205 AA.
AC   P35660;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=D-alanine--D-alanine ligase;
DE            EC=6.3.2.4;
DE   AltName: Full=D-Ala-D-Ala ligase;
DE   AltName: Full=D-alanylalanine synthetase;
DE   Flags: Fragment;
GN   Name=ddl;
OS   Anaplasma centrale.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1540152; DOI=10.1016/0006-291x(92)91836-f;
RA   Peters J.M., Dalrymple B.P., Jorgensen W.K.;
RT   "Sequence of a putative glutathione synthetase II gene and flanking regions
RT   from Anaplasma centrale.";
RL   Biochem. Biophys. Res. Commun. 182:1040-1046(1992).
CC   -!- FUNCTION: Cell wall formation.
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   -!- 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. {ECO:0000250};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000305}.
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DR   EMBL; M80425; AAA22065.1; -; Genomic_DNA.
DR   PIR; PQ0272; PQ0272.
DR   AlphaFoldDB; P35660; -.
DR   SMR; P35660; -.
DR   UniPathway; UPA00219; -.
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-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR000291; D-Ala_lig_Van_CS.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 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; Cytoplasm;
KW   Ligase; Magnesium; Manganese; Nucleotide-binding; Peptidoglycan synthesis.
FT   CHAIN           1..>205
FT                   /note="D-alanine--D-alanine ligase"
FT                   /id="PRO_0000177778"
FT   DOMAIN          111..>205
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   BINDING         139..190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   NON_TER         205
SQ   SEQUENCE   205 AA;  21656 MW;  0FC7855DFB10A636 CRC64;
     MPVGLACNAD DVLSIAVLCG GSSPEREVSL AGGKRIADAL GRLGHRAAVV DLNRESAHQL
     LAMAPDLVYN ALHGGQGEDG CASGLLDILG LAYTHSRVAA SSVGMDKVLT KHVLKSLGID
     FPEFSVLTKE EVLSAKEVMP YPFVIKPICG GSTIGVHAIF SRSEYLDLSV HADALEGRML
     VEEYIPGQEV HTAVFLGRAI GTMEF
//