ID DDLA_PSEAE Reviewed; 346 AA. AC Q9HWI0; DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 128. DE RecName: Full=D-alanine--D-alanine ligase A {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 A {ECO:0000255|HAMAP-Rule:MF_00047}; DE AltName: Full=D-alanylalanine synthetase A {ECO:0000255|HAMAP-Rule:MF_00047}; GN Name=ddlA {ECO:0000255|HAMAP-Rule:MF_00047}; OrderedLocusNames=PA4201; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE004091; AAG07588.1; -; Genomic_DNA. DR PIR; E83121; E83121. DR RefSeq; NP_252890.1; NC_002516.2. DR RefSeq; WP_003114722.1; NZ_QZGE01000013.1. DR PDB; 8EVV; X-ray; 2.05 A; A/B/C/D=1-346. DR PDB; 8EVW; X-ray; 1.22 A; A/B=1-346. DR PDB; 8EVX; X-ray; 1.55 A; A/B=1-346. DR PDBsum; 8EVV; -. DR PDBsum; 8EVW; -. DR PDBsum; 8EVX; -. DR AlphaFoldDB; Q9HWI0; -. DR SMR; Q9HWI0; -. DR STRING; 208964.PA4201; -. DR PaxDb; 208964-PA4201; -. DR DNASU; 879033; -. DR GeneID; 879033; -. DR KEGG; pae:PA4201; -. DR PATRIC; fig|208964.12.peg.4401; -. DR PseudoCAP; PA4201; -. DR HOGENOM; CLU_039268_1_1_6; -. DR InParanoid; Q9HWI0; -. DR OrthoDB; 9813261at2; -. DR PhylomeDB; Q9HWI0; -. DR BioCyc; PAER208964:G1FZ6-4274-MONOMER; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IBA:GO_Central. 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; IBA:GO_Central. 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 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 NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1. 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 Pfam; PF01820; Dala_Dala_lig_N; 1. DR PIRSF; PIRSF039102; Ddl/VanB; 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. 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; Reference proteome. FT CHAIN 1..346 FT /note="D-alanine--D-alanine ligase A" FT /id="PRO_0000177855" FT DOMAIN 138..332 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 164..217 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 286 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 299 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 299 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT BINDING 301 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00047" FT STRAND 7..12 FT /evidence="ECO:0007829|PDB:8EVW" FT HELIX 19..35 FT /evidence="ECO:0007829|PDB:8EVW" FT STRAND 39..44 FT /evidence="ECO:0007829|PDB:8EVW" FT TURN 45..47 FT /evidence="ECO:0007829|PDB:8EVW" FT HELIX 52..59 FT /evidence="ECO:0007829|PDB:8EVW" FT HELIX 70..76 FT /evidence="ECO:0007829|PDB:8EVW" FT TURN 83..85 FT /evidence="ECO:0007829|PDB:8EVV" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:8EVW" FT STRAND 93..97 FT /evidence="ECO:0007829|PDB:8EVW" FT HELIX 102..105 FT /evidence="ECO:0007829|PDB:8EVW" FT HELIX 108..115 FT /evidence="ECO:0007829|PDB:8EVW" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:8EVW" FT HELIX 125..132 FT /evidence="ECO:0007829|PDB:8EVW" FT HELIX 134..143 FT /evidence="ECO:0007829|PDB:8EVW" FT STRAND 151..155 FT /evidence="ECO:0007829|PDB:8EVW" FT HELIX 158..164 FT /evidence="ECO:0007829|PDB:8EVW" FT STRAND 167..173 FT /evidence="ECO:0007829|PDB:8EVW" FT TURN 178..181 FT /evidence="ECO:0007829|PDB:8EVW" FT STRAND 183..185 FT /evidence="ECO:0007829|PDB:8EVW" FT HELIX 188..199 FT /evidence="ECO:0007829|PDB:8EVW" FT STRAND 205..209 FT /evidence="ECO:0007829|PDB:8EVW" FT STRAND 213..221 FT /evidence="ECO:0007829|PDB:8EVW" FT STRAND 229..232 FT /evidence="ECO:0007829|PDB:8EVW" FT STRAND 235..237 FT /evidence="ECO:0007829|PDB:8EVV" FT HELIX 241..245 FT /evidence="ECO:0007829|PDB:8EVW" FT STRAND 249..255 FT /evidence="ECO:0007829|PDB:8EVW" FT HELIX 260..276 FT /evidence="ECO:0007829|PDB:8EVW" FT STRAND 281..289 FT /evidence="ECO:0007829|PDB:8EVW" FT STRAND 295..303 FT /evidence="ECO:0007829|PDB:8EVW" FT HELIX 311..318 FT /evidence="ECO:0007829|PDB:8EVW" FT HELIX 323..337 FT /evidence="ECO:0007829|PDB:8EVW" SQ SEQUENCE 346 AA; 36534 MW; A66C5B0DB58F9A23 CRC64; MGQDKLKVAV LFGGSSEERD VSIASGAQVI QALRSAGHQV LAVDTASGLL GAEEERRLLA SKVKEVPPDS DSLAIIRSGK QSLLSAGELA GVDVFFLALH GGTGEDGTLQ ALLDAGGFAY TGSGHLASAM AMDKDVAKRL FLAAGVETAS WLMAPASEEE VREQLGFPLV VKPNSQGSTV GLSIVHSQAE LQPAIELAGR YGDEVMLERF VAGREVTVGV LDDQALPVGE ILLGGQEVFD YEHKYQAGAV REVFPADLPP AIAAEAQRLA LKVHRALKLS GYSRTDFRLD EQGRLWCLEV NTLPGMTATS LLPQAAAAAG IGFAELCERI CRLGIERCKG ARKARS //