ID A0A3M8SAQ9_9PROT Unreviewed; 304 AA.
AC A0A3M8SAQ9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=RimK family alpha-L-glutamate ligase {ECO:0000313|EMBL:RNF76756.1};
GN ORFNames=EC580_00520 {ECO:0000313|EMBL:RNF76756.1};
OS Acidithiobacillus sulfuriphilus.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=1867749 {ECO:0000313|EMBL:RNF76756.1, ECO:0000313|Proteomes:UP000271650};
RN [1] {ECO:0000313|EMBL:RNF76756.1, ECO:0000313|Proteomes:UP000271650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ-2 {ECO:0000313|EMBL:RNF76756.1,
RC ECO:0000313|Proteomes:UP000271650};
RA Falagan C., Moya-Beltran A., Quatrini R., Johnson D.B.;
RT "Acidithiobacillus sulfuriphilus sp. nov.: an extremely acidophilic sulfur-
RT oxidizing chemolithotroph isolated from a neutral pH environment.";
RL Submitted (OCT-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:RNF76756.1}.
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DR EMBL; RIZI01000055; RNF76756.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M8SAQ9; -.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000271650; 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:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 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:RNF76756.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000271650}.
FT DOMAIN 107..289
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 304 AA; 32112 MW; A64E67A4E9E5645A CRC64;
MTAPCIAILS RRPELYSTRR LVAAAEHLGT VPLVLDPGAC LLALDSAGSV LYHGNERVPS
CVAAIPRIGS PITRLGGRLL RHFASQGSYC LNGAAALELA RDKFAALQAL VQAGVPVPRT
VYFSNPQQRE MAMAQVGWPL VSKLLEGSQG VGVMLAESAA SARGLLDTLL HLQQEAVVQR
YLAGREDLRV IVLAGQILAS MRRRAPLDDF RSNLHRGGEA TLVGDLPAPW AAIALRATAA
LGLDFAGVDL MADGDGQALV LEVNPVPSLE GIERVSGVDV ADAIMRRVLA AALRIPHPSG
RRPG
//
