DDL_ACIBC
ID DDL_ACIBC Reviewed; 308 AA.
AC B2I1J3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=ACICU_03532;
OS Acinetobacter baumannii (strain ACICU).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=405416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACICU;
RX PubMed=18411315; DOI=10.1128/aac.01643-07;
RA Iacono M., Villa L., Fortini D., Bordoni R., Imperi F., Bonnal R.J.,
RA Sicheritz-Ponten T., De Bellis G., Visca P., Cassone A., Carattoli A.;
RT "Whole-genome pyrosequencing of an epidemic multidrug-resistant
RT Acinetobacter baumannii strain belonging to the European clone II group.";
RL Antimicrob. Agents Chemother. 52:2616-2625(2008).
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. {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}.
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DR EMBL; CP000863; ACC58841.1; -; Genomic_DNA.
DR RefSeq; WP_000063661.1; NZ_CP031380.1.
DR PDB; 5D8D; X-ray; 2.19 A; A/B/C/D/E/F=1-308.
DR PDB; 5DMX; X-ray; 2.81 A; A/B/C/D/E/F=1-308.
DR PDBsum; 5D8D; -.
DR PDBsum; 5DMX; -.
DR AlphaFoldDB; B2I1J3; -.
DR SMR; B2I1J3; -.
DR GeneID; 60877879; -.
DR GeneID; 66395481; -.
DR KEGG; abc:ACICU_03532; -.
DR HOGENOM; CLU_039268_1_2_6; -.
DR OMA; MQGLLEC; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008839; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell shape; Cell wall biogenesis/degradation;
KW Cytoplasm; Ligase; Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Peptidoglycan synthesis.
FT CHAIN 1..308
FT /note="D-alanine--D-alanine ligase"
FT /id="PRO_1000091154"
FT DOMAIN 104..301
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT BINDING 130..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047"
FT HELIX 3..7
FT /evidence="ECO:0007829|PDB:5D8D"
FT STRAND 9..13
FT /evidence="ECO:0007829|PDB:5D8D"
FT HELIX 21..37
FT /evidence="ECO:0007829|PDB:5D8D"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:5D8D"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:5D8D"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:5D8D"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:5D8D"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:5D8D"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:5D8D"
FT HELIX 74..81
FT /evidence="ECO:0007829|PDB:5D8D"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:5D8D"
FT HELIX 91..97
FT /evidence="ECO:0007829|PDB:5D8D"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:5D8D"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:5D8D"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:5D8D"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:5D8D"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:5D8D"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:5D8D"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5D8D"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:5D8D"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:5D8D"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:5D8D"
FT HELIX 229..245
FT /evidence="ECO:0007829|PDB:5D8D"
FT STRAND 250..259
FT /evidence="ECO:0007829|PDB:5D8D"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:5D8D"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:5D8D"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:5D8D"
FT HELIX 292..301
FT /evidence="ECO:0007829|PDB:5D8D"
SQ SEQUENCE 308 AA; 33361 MW; 2FAC21CB07A75F19 CRC64;
MSNATKFGKV AVLLGGKSAE RAVSLDSGQA VLDALLRSGV QAEAFDPQDR SVTELVNYDR
AFIVLHGRGG EDGQIQGVLE WLNIPYTGTG VQGSAIGMDK VKTKQIWQGS DLPTAPYRII
TKETDLDSVI AELGLPVIIK PVHEGSSVGM SKVEKAEDFA AAIEKATQHD AVVMAEKWIT
GREFTISFLN GQPLPVIRLQ PPADVAFYDY EAKYQRNDVE YGIPCGLSET EEKKLQALCL
RAFQAVGAEG WGRIDAMQDE QGNFWLLEVN TVPGMTSHSL VPKAAKAVGY SFDELCVAIL
EQTLEGTA
