ID F0RPD4_DEIPM Unreviewed; 360 AA. AC F0RPD4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 27-MAR-2024, entry version 79. 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}; GN Name=ddl {ECO:0000256|HAMAP-Rule:MF_00047}; GN OrderedLocusNames=Deipr_1328 {ECO:0000313|EMBL:ADY26477.1}; OS Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 / NBRC OS 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP). OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae; OC Deinococcus. OX NCBI_TaxID=693977 {ECO:0000313|EMBL:ADY26477.1, ECO:0000313|Proteomes:UP000007718}; RN [1] {ECO:0000313|Proteomes:UP000007718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G., RA Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K., RA Brambilla E., Klenk H.-P., Eisen J.A.; RT "The complete sequence of chromosome of Deinococcus proteolyticus DSM RT 20540."; RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADY26477.1, ECO:0000313|Proteomes:UP000007718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 / RC VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718}; RX PubMed=22768367; DOI=10.4056/sigs.2756060; RA Copeland A., Zeytun A., Yassawong M., Nolan M., Lucas S., Hammon N., RA Deshpande S., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S., RA Mavromatis K., Liolios K., Pagani I., Ivanova N., Mikhailova N., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Brambilla E.M., RA Rohde M., Sikorski J., Pukall R., Goker M., Detter J.C., Woyke T., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Lapidus A.; RT "Complete genome sequence of the orange-red pigmented, radioresistant RT Deinococcus proteolyticus type strain (MRP(T))."; RL Stand. Genomic Sci. 6:240-250(2012). 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; CP002536; ADY26477.1; -; Genomic_DNA. DR AlphaFoldDB; F0RPD4; -. DR STRING; 693977.Deipr_1328; -. DR KEGG; dpt:Deipr_1328; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_0_0_0; -. DR OrthoDB; 9813261at2; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000007718; 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}; Reference proteome {ECO:0000313|Proteomes:UP000007718}. FT DOMAIN 147..354 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 307 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 321 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 321 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT BINDING 323 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" SQ SEQUENCE 360 AA; 38483 MW; AFF7C8CD00661327 CRC64; MSDLTPAQPQ SPSESPSAPR QPRRRVLLLA GGQSEEHEVS LSSARSVLAA LPQDRFEVTA VVISKQGRWL PPAETAQALG AGAAESGGEP MLQRVSDTAG YDVVFPLLHG PMGEDGTVQG LLTLAGLPFV GSGVLGSSVG MDKIMTKRVL EAAGIPQVAW REASRAEWRR DPQGVQSRAA ELGFPLFVKP ANMGSSVGVS RVTGAGELAE ALELAFGHDR RVIVEAAAGA KPREVEVGIL GNDDPVASPV GELRFDTDFY DYDTKYTGGR AEMLIPAPLP EGVSERIQEL ALRAYQALDC AGLSRVDFFY VEETGELLLN EINTMPGFTT TSMYPSLLQA HGLSYPELVT RLIELALEER //