ID A0A1F2PGR3_9FIRM Unreviewed; 307 AA.
AC A0A1F2PGR3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Ribosomal protein S6--L-glutamate ligase {ECO:0000313|EMBL:OFV69906.1};
DE EC=6.3.2.- {ECO:0000313|EMBL:OFV69906.1};
GN Name=rimK_1 {ECO:0000313|EMBL:OFV69906.1};
GN ORFNames=ACWI_25480 {ECO:0000313|EMBL:OFV69906.1};
OS Acetobacterium wieringae.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=52694 {ECO:0000313|EMBL:OFV69906.1, ECO:0000313|Proteomes:UP000176244};
RN [1] {ECO:0000313|EMBL:OFV69906.1, ECO:0000313|Proteomes:UP000176244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1911 {ECO:0000313|EMBL:OFV69906.1,
RC ECO:0000313|Proteomes:UP000176244};
RA Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT "Genome sequence of Acetobacterium wieringae DSM 1911.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OFV69906.1}.
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DR EMBL; LKEU01000035; OFV69906.1; -; Genomic_DNA.
DR RefSeq; WP_070371821.1; NZ_LKEU01000035.1.
DR AlphaFoldDB; A0A1F2PGR3; -.
DR STRING; 52694.ACWI_25480; -.
DR OrthoDB; 9786585at2; -.
DR Proteomes; UP000176244; 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 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 PANTHER; PTHR21621:SF2; COENZYME GAMMA-F420-2:ALPHA-L-GLUTAMATE LIGASE; 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:OFV69906.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ribonucleoprotein {ECO:0000313|EMBL:OFV69906.1};
KW Ribosomal protein {ECO:0000313|EMBL:OFV69906.1}.
FT DOMAIN 109..293
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 307 AA; 34292 MW; 4715C9DE6D331360 CRC64;
MKGWLLRNPG KLEDPSIVKI MKVVEELHVD LTVVDPLTIH VVCDHDFDGK LYVGDEIMEV
PDYVVAAFFT EKNYHTAAAL RMLESLGVLC INSYDAIKNV DDKLLTFQLV AESIEAVCFP
KTLLVTEYTE ASFVSKLFDY PVVMKVMHGS KGKGVVLVNN EKELDNLISM STASEIGDQI
IIQECIKASS GRDLRMILAN GKFVKSFIRQ NEKSFRSNLA KGGHIVEYTP PAAVIEAAEK
VAQLLKINMG SVDFLFGEND TFYLCEANAM PGVAFDIKVM FADLMKQVKD RPEPLWKKRL
REGGKTC
//
