ID   A0A1H9D0X0_9BACI        Unreviewed;       295 AA.
AC   A0A1H9D0X0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Ribosomal protein S6--L-glutamate ligase {ECO:0000313|EMBL:SEQ07031.1};
GN   ORFNames=SAMN05216362_10644 {ECO:0000313|EMBL:SEQ07031.1};
OS   Piscibacillus halophilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Piscibacillus.
OX   NCBI_TaxID=571933 {ECO:0000313|EMBL:SEQ07031.1, ECO:0000313|Proteomes:UP000199427};
RN   [1] {ECO:0000313|EMBL:SEQ07031.1, ECO:0000313|Proteomes:UP000199427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21633 {ECO:0000313|EMBL:SEQ07031.1,
RC   ECO:0000313|Proteomes:UP000199427};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOES01000006; SEQ07031.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9D0X0; -.
DR   STRING; 571933.SAMN05216362_10644; -.
DR   OrthoDB; 9786585at2; -.
DR   Proteomes; UP000199427; Unassembled WGS sequence.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
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:SEQ07031.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199427};
KW   Ribonucleoprotein {ECO:0000313|EMBL:SEQ07031.1};
KW   Ribosomal protein {ECO:0000313|EMBL:SEQ07031.1}.
FT   DOMAIN          103..291
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   295 AA;  33786 MW;  4C87A90DE8EBF1FE CRC64;
     MNGWIIYNGA LKFKKFHLLV ESLVAESKKK GIQLEAIPNS ELLPMFHSDG TQGLKSLRSL
     NEPDFIIFWD KDIYLAKHLE AMGYRLFNRR VAIENCDHKA YMHLQMAQDT IRVPKTIVGP
     FTFHQHELSG EYIDYIFEEL GSEVILKEVF GSFGMQVYKF NNKEDLIHKM KELDGRDFIL
     QEPIKSSFGR DIRVTIIGNQ VIGGMKREFA TDFRANITLG GRGELVELTE EQEKLALKAH
     RSLGLDFSGV DLLFDEDDRP IVCEVNSNVN YLSFEQVSGV NVSRLLLDYI VGEMP
//