ID RIMK_PECCP Reviewed; 303 AA. AC C6DEP6; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-SEP-2009, sequence version 1. DT 02-SEP-2026, entry version 85. DE RecName: Full=Probable alpha-L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01552}; DE EC=6.3.2.- {ECO:0000255|HAMAP-Rule:MF_01552}; GN Name=rimK {ECO:0000255|HAMAP-Rule:MF_01552}; GN OrderedLocusNames=PC1_1690; OS Pectobacterium carotovorum subsp. carotovorum (strain PC1). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Pectobacteriaceae; Pectobacterium. OX NCBI_TaxID=561230; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PC1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., RA Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., RA Balakrishnan V., Glasner J., Perna N.T.; RT "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01552}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01552}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000255|HAMAP-Rule:MF_01552}; CC -!- SIMILARITY: Belongs to the RimK family. {ECO:0000255|HAMAP- CC Rule:MF_01552}. 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; CP001657; ACT12731.1; -; Genomic_DNA. DR RefSeq; WP_015839948.1; NC_012917.1. DR AlphaFoldDB; C6DEP6; -. DR SMR; C6DEP6; -. DR STRING; 561230.PC1_1690; -. DR PaxDb; 561230-PC1_1690; -. DR KEGG; pct:PC1_1690; -. DR eggNOG; COG0189; Bacteria. DR HOGENOM; CLU_054353_0_1_6; -. DR OrthoDB; 3865600at2; -. DR Proteomes; UP000002736; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0018169; F:ribosomal S6-glutamic acid ligase activity; IEA:TreeGrafter. DR GO; GO:0009432; P:SOS response; IEA:TreeGrafter. DR FunFam; 3.40.50.20:FF:000004; Probable alpha-L-glutamate ligase; 1. DR FunFam; 3.30.1490.20:FF:000005; Probable alpha-L-glutamate ligase 1; 1. DR FunFam; 3.30.470.20:FF:000016; Ribosomal protein S6--L-glutamate ligase; 1. 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_01552; RimK; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013651; ATP-grasp_RimK-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR023533; RimK. DR InterPro; IPR041107; Rimk_N. DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX. DR NCBIfam; NF007764; PRK10446.1; 1. DR NCBIfam; TIGR00768; rimK_fam; 1. DR PANTHER; PTHR21621:SF7; RIBOSOMAL PROTEIN BS6--L-GLUTAMATE LIGASE; 1. DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1. DR Pfam; PF08443; RimK; 1. DR Pfam; PF18030; Rimk_N; 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; Ligase; Magnesium; Manganese; Metal-binding; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..303 FT /note="Probable alpha-L-glutamate ligase" FT /id="PRO_1000215476" FT DOMAIN 104..287 FT /note="ATP-grasp" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 141 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 178..179 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 211..213 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 248 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 248 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 260 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 260 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 260 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 260 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 262 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" FT BINDING 262 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01552" SQ SEQUENCE 303 AA; 32809 MW; B6540A5C5BEF91BE CRC64; MKIAILSRDG ALYSCKRLRE AAEARKHSVE IIDPLSCYMN INSAAPSVHY RGRRLDKYDA VIPRIGSQIT FYGTAVLRQF EMLGSYPLNN SVAVIRARDK LHSLQLLARE GIDLPITGFA HSPDDTGDLI AMVGGAPLVV KLVEGTQGIG VVLAETRQAA ESVIDAFRGL NAHILVQEYV REAQGKDIRC LVIGNRVVAA IERQAKAGEF RSNLHRGGSA NNVKITAQER AIAIKATKTL GLNVAGVDIL RADRGPLVME VNASPGLEGI ETTTGFDIAG MMIEFIEQNT QRRFATSASI SKS //