ID S4XJR7_SORCE Unreviewed; 349 AA.
AC S4XJR7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Alpha-L-glutamate ligase {ECO:0000313|EMBL:AGP32789.1};
GN ORFNames=SCE1572_40620 {ECO:0000313|EMBL:AGP32789.1};
OS Sorangium cellulosum So0157-2.
OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium.
OX NCBI_TaxID=1254432 {ECO:0000313|EMBL:AGP32789.1, ECO:0000313|Proteomes:UP000014803};
RN [1] {ECO:0000313|EMBL:AGP32789.1, ECO:0000313|Proteomes:UP000014803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So0157-2 {ECO:0000313|EMBL:AGP32789.1,
RC ECO:0000313|Proteomes:UP000014803};
RX PubMed=23812535; DOI=10.1038/srep02101;
RA Han K., Li Z.F., Peng R., Zhu L.P., Zhou T., Wang L.G., Li S.G.,
RA Zhang X.B., Hu W., Wu Z.H., Qin N., Li Y.Z.;
RT "Extraordinary expansion of a Sorangium cellulosum genome from an alkaline
RT milieu.";
RL Sci. Rep. 3:2101-2101(2013).
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DR EMBL; CP003969; AGP32789.1; -; Genomic_DNA.
DR RefSeq; WP_020739994.1; NC_021658.1.
DR AlphaFoldDB; S4XJR7; -.
DR STRING; 1254432.SCE1572_40620; -.
DR KEGG; scu:SCE1572_40620; -.
DR PATRIC; fig|1254432.3.peg.9179; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_054353_0_1_7; -.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000014803; Chromosome.
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:AGP32789.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 104..287
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 314..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 37467 MW; EA95726A295746E0 CRC64;
MRFLVLSRNA SLYSTSRIVL AGRARGHDVS VIDPLDFQIV VSRGRPSLLV GGSAVPRFDI
VIPRIGASIT NYGLAVVRQF DLMGVPVLNG AVSIARSRDK LRALQLLTRR KLNVPITVCA
RSPAGVEAAL SLVGGCPAIV KLQQGTQGIG TMLAETPHAV HALLETFWAM GQDIVLQEYV
RESKGRDIRV IVVGGRVVAS MRRVAKPGEF RSNLHRGGKG DRVKLPRAYR SVAIRAAKAM
GLEVAGVDML EARSGPKILE INSSPGLEGI ERASGVDVAG AIISYAERYA AEQRGLSRRT
LEARIAEVIH DERMPPTRRL SRAAENGAGA SRRKPAVLTN GRGARRAAS
//
