ID A0A3D8N1L1_9DELT Unreviewed; 317 AA.
AC A0A3D8N1L1;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=RimK family alpha-L-glutamate ligase {ECO:0000313|EMBL:RDV40092.1};
GN ORFNames=DV096_05910 {ECO:0000313|EMBL:RDV40092.1};
OS Bradymonadaceae bacterium TMQ3.
OC Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae.
OX NCBI_TaxID=2283320 {ECO:0000313|EMBL:RDV40092.1, ECO:0000313|Proteomes:UP000256871};
RN [1] {ECO:0000313|EMBL:RDV40092.1, ECO:0000313|Proteomes:UP000256871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMQ3 {ECO:0000313|EMBL:RDV40092.1,
RC ECO:0000313|Proteomes:UP000256871};
RA Wang S.;
RT "Lujinxingia celare sp. nov., isolated from a marine island.";
RL Submitted (AUG-2018) 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:RDV40092.1}.
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DR EMBL; QRGZ01000001; RDV40092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8N1L1; -.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000256871; Unassembled WGS sequence.
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 GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
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; IPR041107; Rimk_N.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR PANTHER; PTHR21621:SF7; RIBOSOMAL PROTEIN S6--L-GLUTAMATE LIGASE; 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 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:RDV40092.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 129..312
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 317 AA; 33872 MW; 9CD0D6DA3B82415E CRC64;
MYLCGTADFS DCAGDLFRPE LGRPAVKLAL ISTNRNLYST RRLWEAARKA GHDVRFLHPR
RCTTGVDLKG TLISTDGLRM EGFDAAIPRF GASQTRAGLV LLDLLQARGV VTLNTSAAIE
RCRDKLRSIQ HLAIADLPVP PTVSLYDAER LDETVDQLGG LPIIIKLIKG SHGVGVIRCD
TIETLRSTVE TLWSLNEEVL LQRYIGESAG KDLRVFVVAG EVVGAMERRA GPGEFRANLH
RGGSAQAVDL SDELREIALG AAKALGLGIA GVDLLMSADG PLILEVNASP GLEGIEAATG
KDIARQIIRA TAALSSS
//