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Database: UniProt
Entry: A0A0F7JWT3_9GAMM
LinkDB: A0A0F7JWT3_9GAMM
Original site: A0A0F7JWT3_9GAMM 
ID   A0A0F7JWT3_9GAMM        Unreviewed;       303 AA.
AC   A0A0F7JWT3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Alpha-L-glutamate ligase {ECO:0000313|EMBL:AKH19260.1};
GN   ORFNames=AAY24_01655 {ECO:0000313|EMBL:AKH19260.1};
OS   Sedimenticola thiotaurini.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX   NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH19260.1, ECO:0000313|Proteomes:UP000034410};
RN   [1] {ECO:0000313|EMBL:AKH19260.1, ECO:0000313|Proteomes:UP000034410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH19260.1,
RC   ECO:0000313|Proteomes:UP000034410};
RX   PubMed=26089430;
RA   Flood B.E., Jones D.S., Bailey J.V.;
RT   "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT   Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT   Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL   Genome Announc. 3:e00671-15(2015).
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DR   EMBL; CP011412; AKH19260.1; -; Genomic_DNA.
DR   RefSeq; WP_046858199.1; NZ_CP011412.1.
DR   AlphaFoldDB; A0A0F7JWT3; -.
DR   KEGG; seds:AAY24_01655; -.
DR   PATRIC; fig|1543721.4.peg.352; -.
DR   OrthoDB; 9786585at2; -.
DR   Proteomes; UP000034410; 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   Gene3D; 3.40.50.20; -; 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; 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   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:AKH19260.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034410}.
FT   DOMAIN          108..290
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   303 AA;  33207 MW;  516F8CB6464EB4D3 CRC64;
     MTLRVAIITD DPGWHGKRLR EAFQARGVEC LFSSLQQARI ELGRTVSVVL PGFEAALPDA
     VFVRGIPGGT LQQVVFHLNV LHILKELGVR VYNDGRAIER SVDKAWTSAR LSLAEIPTPA
     TWICTDRQMT ESVVQREAAA GHALICKPLF GSQGQGIVRV TDCADLPEAD AMHHVWYLQR
     FIPQTDQLAC DWRVFVISGV AVAAMRRSTS GWLANVAQGG TCQAALPEGE LKQLAEQAVA
     CLDMDYAGVD LMRDVQGNWW VIEINSVPAW RGLQRVTAVN IADALADDLL AKVRCAEPCE
     ALR
//
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