ID D6XT10_BACIE Unreviewed; 310 AA.
AC D6XT10;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=Alpha-L-glutamate ligase, RimK family {ECO:0000313|EMBL:ADH98946.1};
GN OrderedLocusNames=Bsel_1434 {ECO:0000313|EMBL:ADH98946.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH98946.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH98946.1, ECO:0000313|Proteomes:UP000000271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC {ECO:0000313|Proteomes:UP000000271};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001791; ADH98946.1; -; Genomic_DNA.
DR RefSeq; WP_013172370.1; NC_014219.1.
DR AlphaFoldDB; D6XT10; -.
DR STRING; 439292.Bsel_1434; -.
DR KEGG; bse:Bsel_1434; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_054353_0_2_9; -.
DR OrthoDB; 9786585at2; -.
DR Proteomes; UP000000271; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0036211; P:protein modification process; 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; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF08443; RimK; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADH98946.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 108..296
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 310 AA; 33593 MW; 3FCAFE798E96F841 CRC64;
MTTTRSPVLL ILGNGHMQTA KFLDYQDWIH NAADKAGFTA ITATNLDFLA GNIGEAPLCT
GEEKMPAIDA VLFADKDLPL ARAFEASGIP VFNNSQAVGV CDHKGQMHER LAASGLPTPD
TVFAPFLYQK PKEMDLRFLD AVIHRLGLPI VVKEAYGSFG EQVHLAQSRE ELEALTLSLA
GKPFLFQAFI KESRGEDLRL NVIGGEVIAA MRRTSETDFR ANVTAGGKTA PHEPTEAERA
LAIAASRAVC ADFAGVDLLR TNDGPVICEV NTNPHIRSIH EATGIDIAPH MMAWIDKKIR
QSVQVEGGPR
//