ID I4BCG7_MYCCN Unreviewed; 348 AA. AC I4BCG7; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 27-MAR-2024, entry version 50. DE SubName: Full=ATP-grasp enzyme, D-alanine-D-alanine ligase {ECO:0000313|EMBL:AFM14974.1}; GN OrderedLocusNames=Mycch_0148 {ECO:0000313|EMBL:AFM14974.1}; OS Mycolicibacterium chubuense (strain NBB4) (Mycobacterium chubuense). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycolicibacterium. OX NCBI_TaxID=710421 {ECO:0000313|EMBL:AFM14974.1, ECO:0000313|Proteomes:UP000006057}; RN [1] {ECO:0000313|EMBL:AFM14974.1, ECO:0000313|Proteomes:UP000006057} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBB4 {ECO:0000313|EMBL:AFM14974.1, RC ECO:0000313|Proteomes:UP000006057}; 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., Teshima H., Detter J.C., Han C., Tapia R., RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T., RA Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.; RT "Complete sequence of chromosome of Mycobacterium chubuense NBB4."; RL Submitted (JUN-2012) 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; CP003053; AFM14974.1; -; Genomic_DNA. DR AlphaFoldDB; I4BCG7; -. DR STRING; 710421.Mycch_0148; -. DR KEGG; mcb:Mycch_0148; -. DR PATRIC; fig|710421.3.peg.140; -. DR eggNOG; COG1181; Bacteria. DR HOGENOM; CLU_796548_0_0_11; -. DR Proteomes; UP000006057; 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; 3.40.50.20; -; 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; 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; 2. 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:0000313|EMBL:AFM14974.1}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}; KW Reference proteome {ECO:0000313|Proteomes:UP000006057}. FT DOMAIN 129..341 FT /note="ATP-grasp" FT /evidence="ECO:0000259|PROSITE:PS50975" SQ SEQUENCE 348 AA; 36723 MW; E229EB34CF9FFDD4 CRC64; MAIRLGHRVV QLAGSPVDEF HAELSRLYAR DSAAVLAEHH AVQFAYVEPG GSWRFPARLD AASLAAARSV PAPAAIAHLM ALRPDVVVPQ MFCRPGMTAY RALLDVLGLP YVGNTAQVMA NTADKAVARA LVAAYGVAVP AGQLVTNASD VRLELPVVVK PARSDNSLGV SLVQDASTLA VAVAHAAELD AGVLVETYIP LGREVRCGVL EVDGELVCLP LEEYALDAQR APIRLADDKL GRTAGGDLRL VATDAGRAWI LAGDDAADDT VVDAVFDAAR TCFRALGCRH YGLFDFRIDP QGRPWFLEAG PYCSFAPSSV VAKMAEAAGL SLPALFDTVC RQARIGAS //