ID A0A5P2FVX5_9BACT Unreviewed; 329 AA. AC A0A5P2FVX5; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 02-DEC-2020, entry version 5. 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 ORFNames=E0W69_001060 {ECO:0000313|EMBL:QES87305.1}; OS Arachidicoccus sp. B3-10. OC Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales; Chitinophagaceae; OC Arachidicoccus; unclassified Arachidicoccus. OX NCBI_TaxID=2545455 {ECO:0000313|EMBL:QES87305.1, ECO:0000313|Proteomes:UP000292424}; RN [1] {ECO:0000313|EMBL:QES87305.1, ECO:0000313|Proteomes:UP000292424} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B3-10 {ECO:0000313|EMBL:QES87305.1, RC ECO:0000313|Proteomes:UP000292424}; RA Kim H.S., Han K.-I., Suh M.K., Lee K.C., Eom M.K., Kim J.-S., Kang S.W., RA Sin Y., Lee J.-S.; RT "Complete genome sequence of Arachidicoccus sp. B3-10 isolated from apple RT orchard soil."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. 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 -!- 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|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; CP044016; QES87305.1; -; Genomic_DNA. DR KEGG; arac:E0W69_001060; -. DR UniPathway; UPA00219; -. DR Proteomes; UP000292424; 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; 3.30.1490.20; -; 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 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 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 ECO:0000313|EMBL:QES87305.1}; Magnesium {ECO:0000256|PIRSR:PIRSR039102-3}; KW Manganese {ECO:0000256|PIRSR:PIRSR039102-3}; KW Metal-binding {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:UP000292424}. FT DOMAIN 121..325 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" FT METAL 278 FT /note="Magnesium or manganese 1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT METAL 292 FT /note="Magnesium or manganese 1" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT METAL 292 FT /note="Magnesium or manganese 2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" FT METAL 294 FT /note="Magnesium or manganese 2" FT /evidence="ECO:0000256|PIRSR:PIRSR039102-3" SQ SEQUENCE 329 AA; 36614 MW; 27A123A6DBE61009 CRC64; MKKQIAFVTG GFSGEAQISY ESAKTVEQNI DRDLFDVYKI DITPDGWYYI PTEGVRLPVD KSHFTVQKEG KTVKFDAALL VIHGTPGEDG KLQGYLDLMG VPYTSCDTTT SALTFNKRFT VAVASFGGIH VAKSAILFKG QAYNIDDIKK MHFPLFVKPN NGGSSIGMSK LESKHPEDIQ AAIDKAFAVD DQVLIEEFIK GREFTIGVLK TKGEIITLPM TEILKPEGMN FFDFEAKYHG KDLEVTPADA SEHMTQKVQE TAKKVYQLLN CKGIIRIDFI YNETKDEPYL LEVNTVPGQT AASLVPQQLA AMKWSLKDFY TALIEEALV //