ID G2MUR7_9THEO Unreviewed; 325 AA. AC G2MUR7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 27-MAR-2024, entry version 45. DE RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975}; GN ORFNames=Thewi_0080 {ECO:0000313|EMBL:AEM77590.1}; OS Thermoanaerobacter wiegelii Rt8.B1. OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacter. OX NCBI_TaxID=697303 {ECO:0000313|EMBL:AEM77590.1, ECO:0000313|Proteomes:UP000008276}; RN [1] {ECO:0000313|EMBL:AEM77590.1, ECO:0000313|Proteomes:UP000008276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rt8.B1 {ECO:0000313|EMBL:AEM77590.1, RC ECO:0000313|Proteomes:UP000008276}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Mikhailova N., Zeytun A., Daligault H., Detter J.C., Han C., RA Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Hemme C., RA Woyke T.; RT "Complete sequence of Thermoanaerobacter wiegelii Rt8.B1."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. 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; CP002991; AEM77590.1; -; Genomic_DNA. DR AlphaFoldDB; G2MUR7; -. DR STRING; 697303.Thewi_0080; -. DR KEGG; twi:Thewi_0080; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_2866383_0_0_9; -. DR Proteomes; UP000008276; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. 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; IPR011095; Dala_Dala_lig_C. 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 SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409}; KW Ligase {ECO:0000256|ARBA:ARBA00022598}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}. FT DOMAIN 105..316 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" SQ SEQUENCE 325 AA; 37119 MW; 0C626B1A8D4F7597 CRC64; MKIGVLWRKF RNVEFQRKLT PDKVYDDAYD EAYHHYMAIK EAGFDSVLIE WKEDPLETYE TIKKEKVDLI FNASSMKEVA FLEVFNIPYV GSGLDVVATD KRMRKDIVAS HGLPTPKYVI AQNPQEIPSV DHLKFPLFAK PISGRGSAGI DEENIIYDKD KLPQVVSKIT DKIGQAALIE EFIEGKEVTV GIIGYKHPQV LPLLEVGYNN VKTNTYEHKM FDNEIIKCPM EVSKEVEEKI KETALNIYKV LNAKDFARID MILSKDNVPY FLELNTFAGL TMSSSKGEKH VHHGYMGYMA KAAGLTRGEF IRKIIESAIE RYKLK //