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Database: UniProt
Entry: A0A0L0LN69_9BACT
LinkDB: A0A0L0LN69_9BACT
Original site: A0A0L0LN69_9BACT 
ID   A0A0L0LN69_9BACT        Unreviewed;       279 AA.
AC   A0A0L0LN69;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Glutathione synthase/ribosomal protein S6 modification enzyme (Glutaminyl transferase) {ECO:0000313|EMBL:KND51578.1};
GN   ORFNames=AB202_03370 {ECO:0000313|EMBL:KND51578.1};
OS   Parcubacteria bacterium C7867-007.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1659201 {ECO:0000313|EMBL:KND51578.1, ECO:0000313|Proteomes:UP000037534};
RN   [1] {ECO:0000313|EMBL:KND51578.1, ECO:0000313|Proteomes:UP000037534}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7867-007 {ECO:0000313|EMBL:KND51578.1};
RX   PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA   Nelson W.C., Stegen J.C.;
RT   "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT   symbiotic lifestyle.";
RL   Front. Microbiol. 6:713-713(2015).
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:KND51578.1}.
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DR   EMBL; LFCQ01000002; KND51578.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0LN69; -.
DR   STRING; 1659201.AB202_03370; -.
DR   Proteomes; UP000037534; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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: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   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Transferase {ECO:0000313|EMBL:KND51578.1}.
FT   DOMAIN          75..276
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   279 AA;  32091 MW;  98606024A4B0BFCA CRC64;
     MSTAGGYVNT RCVRKACDRL KIPYTVHDEY GNFVSVQKQK YFFVNASMPF NSSSLNKICS
     DKDFASRLLK DVVRMPKTLG YFDPYPKYEK YTDYIEQTNY EAITDSICSE FSFPLIIKMN
     SGQQGTNVFK CATKEDVSMA LAAIFDHNSP HYDFVALVQE YIQPKAEYRV IVFRGEVLLA
     YEKNITDATF VGNLSPLHYE NAKAIQILDL DLLKRFQECI TPIFPILNLE FTGIDIIQDE
     DDKFYVIELN SRPGFTLFEK DNGDEPLVQM YEKILSSLE
//
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