ID B9L9N9_NAUPA Unreviewed; 344 AA. AC B9L9N9; DT 24-MAR-2009, integrated into UniProtKB/TrEMBL. DT 24-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 99. DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:ACM93621.1}; DE EC=6.3.2.4 {ECO:0000313|EMBL:ACM93621.1}; GN OrderedLocusNames=NAMH_0945 {ECO:0000313|EMBL:ACM93621.1}; OS Nautilia profundicola (strain ATCC BAA-1463 / DSM 18972 / AmH). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales; OC Nautiliaceae; Nautilia. OX NCBI_TaxID=598659 {ECO:0000313|EMBL:ACM93621.1, ECO:0000313|Proteomes:UP000000448}; RN [1] {ECO:0000313|EMBL:ACM93621.1, ECO:0000313|Proteomes:UP000000448} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1463 / DSM 18972 / AmH RC {ECO:0000313|Proteomes:UP000000448}; RX PubMed=19197347; DOI=10.1371/journal.pgen.1000362; RA Campbell B.J., Smith J.L., Hanson T.E., Klotz M.G., Stein L.Y., Lee C.K., RA Wu D., Robinson J.M., Khouri H.M., Eisen J.A., Cary S.C.; RT "Adaptations to submarine hydrothermal environments exemplified by the RT genome of Nautilia profundicola."; RL PLoS Genet. 5:E1000362-E1000362(2009). CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family. CC {ECO:0000256|ARBA:ARBA00010871}. 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; CP001279; ACM93621.1; -; Genomic_DNA. DR RefSeq; WP_015902673.1; NC_012115.1. DR AlphaFoldDB; B9L9N9; -. DR STRING; 598659.NAMH_0945; -. DR KEGG; nam:NAMH_0945; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_039268_0_2_7; -. DR OrthoDB; 9813261at2; -. DR Proteomes; UP000000448; 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-EC. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW. 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 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:SF23; D-ALANINE--D-ALANINE LIGASE B; 1. DR Pfam; PF07478; Dala_Dala_lig_C; 1. DR Pfam; PF01820; Dala_Dala_lig_N; 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}; Cell shape {ECO:0000256|ARBA:ARBA00022960}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ACM93621.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}. FT DOMAIN 136..323 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" SQ SEQUENCE 344 AA; 39345 MW; B70E1338D28E2242 CRC64; MTFALLFGGN SFEHEISIVS AITLKDKIKK HTLEFIYIDQ NRNMYLVDKQ NMKSKYFASG EYKNSQKIEI TKGGFKYTKG LLKKDVFLNY DAVINLIHGK DGEDGKLAGI LEFFNIKSIT PNVEASVISY NKVLTKAYAK EIGVNVIDYE IITEPKSSFD FPIIIKPARL GSSIGVSVVK TQEEFDYAFD VAREFDDLII AEPFIEGIEE YNLAGCLAGG EFMLSNIEKV EKSDFLDFEK KYMDFSRKNV MLSDVDKDLT ERIKKTFKKI YNSTFKNAII RCDFFVKEGS VYLNEINPIP GSMANYLFDD FDDVLEKLAK NIESEKEVKI DFEYINKIQM AKGK //