ID F0M548_PSEPM Unreviewed; 382 AA. AC F0M548; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 78. DE RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047}; DE EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047}; DE AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047}; DE AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047}; DE Flags: Precursor; GN Name=ddl {ECO:0000256|HAMAP-Rule:MF_00047}; GN OrderedLocusNames=Asphe3_23780 {ECO:0000313|EMBL:ADX73512.1}; OS Pseudarthrobacter phenanthrenivorans (strain DSM 18606 / JCM 16027 / LMG OS 23796 / Sphe3) (Arthrobacter phenanthrenivorans). OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae; OC Pseudarthrobacter. OX NCBI_TaxID=930171 {ECO:0000313|EMBL:ADX73512.1, ECO:0000313|Proteomes:UP000008639}; RN [1] {ECO:0000313|EMBL:ADX73512.1, ECO:0000313|Proteomes:UP000008639} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 18606 / JCM 16027 / LMG 23796 / Sphe3 RC {ECO:0000313|Proteomes:UP000008639}; RX PubMed=21677849; DOI=10.4056/sigs.1393494; RA Kallimanis A., Labutti K.M., Lapidus A., Clum A., Lykidis A., RA Mavromatis K., Pagani I., Liolios K., Ivanova N., Goodwin L., Pitluck S., RA Chen A., Palaniappan K., Markowitz V., Bristow J., Velentzas A.D., RA Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.; RT "Complete genome sequence of Arthrobacter phenanthrenivorans type strain RT (Sphe3)."; RL Stand. Genomic Sci. 4:123-130(2011). CC -!- FUNCTION: Cell wall formation. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00047}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR039102-3}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR039102-3}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000256|PIRSR:PIRSR039102-3}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00047}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047}. CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family. CC {ECO:0000256|ARBA:ARBA00010871, ECO:0000256|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; CP002379; ADX73512.1; -; Genomic_DNA. DR RefSeq; WP_013601425.1; NC_015145.1. DR AlphaFoldDB; F0M548; -. DR STRING; 930171.Asphe3_23780; -. DR KEGG; apn:Asphe3_23780; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_0_0_11; -. DR OrthoDB; 9813261at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000008639; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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; 3.40.50.20; -; 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:SF25; D-ALANINE--D-ALANINE LIGASE A; 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP- KW Rule:MF_00047}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_00047}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00047}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR039102-3}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR039102-3}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR039102-3}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00409}; KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP- KW Rule:MF_00047}. FT DOMAIN 161..372 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT BINDING 326 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 339 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 339 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 341 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" SQ SEQUENCE 382 AA; 40611 MW; AB15614B3519AE79 CRC64; MSHDKLAAGE SVNRAKPRVA VLFGGRSSEH AVSCVTAAGV LGAINKDKYE VIPIGIAKSG QWVLVSADTA QWSLAATSLP EVAPSAKSVT LAEIGGEHQL IVAAPNEVPQ ELGTVDVVFP LLHGPFGEDG TIQGLLELSD TRYVGAGVLA SAVGMDKHFM KVVFESAGLQ VGPYVAVTDR QWRKDPESVR KQVDRLGFPV FVKPARAGSS MGISKVESMA ELDAAIEEAR RHDLKLVIEA GITGREIECA VLEGRGTDAP RTSMPGEISV AGGTHEFYDF NAKYVEDGAA ALSCPADIPE EAIARVRELA AAAFDAVGAE GLSRVDFFYT PAGELIINEI NTMPGFTPKS MYPQMWAASG LDYADLIDEL IYLALNRKTG LR //