ID L9YLW8_9EURY Unreviewed; 448 AA.
AC L9YLW8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Alpha-L-glutamate ligase, RimK family protein {ECO:0000313|EMBL:ELY75215.1};
GN ORFNames=C486_20329 {ECO:0000313|EMBL:ELY75215.1};
OS Natrinema gari JCM 14663.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1230459 {ECO:0000313|EMBL:ELY75215.1, ECO:0000313|Proteomes:UP000011592};
RN [1] {ECO:0000313|EMBL:ELY75215.1, ECO:0000313|Proteomes:UP000011592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14663 {ECO:0000313|EMBL:ELY75215.1,
RC ECO:0000313|Proteomes:UP000011592};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:ELY75215.1}.
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DR EMBL; AOIJ01000087; ELY75215.1; -; Genomic_DNA.
DR RefSeq; WP_008459257.1; NZ_AOIJ01000087.1.
DR AlphaFoldDB; L9YLW8; -.
DR PATRIC; fig|1230459.4.peg.4033; -.
DR Proteomes; UP000011592; 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 Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 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; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR008503; Put_Zn_protease.
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; PF05618; Zn_protease; 1.
DR SUPFAM; SSF50630; Acid proteases; 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:ELY75215.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 105..286
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 448 AA; 47880 MW; 0CDAF17545DCBB66 CRC64;
MAVADPVTVG VLSLHTSKET KAILNAVEEL GHDSEWLRNE NTSISVADGS PLLEPEVDVI
ANRMLLSNTE QPAEELGLVN AFSQLVPTLN EPSAVMTAMH KLSTATALAS NDVRTPDVTL
ALSGENLNAA RERYGEEAVY KTAIGTHGGG TWKVGPDDPV NAKVGNRYAF LQELVDQEDV
RHRDLRVYVV GGEIVAAMYR YAPDNDWRTN VALGGSVEDA TEDLPAEASE MAKRAAAVVD
LDYAGVDLVE GDEGWFVLEV NPTAGFKGLY EATQVSPAPY IAKLAIERAG GEVDDDRVRD
IANVLDDSRP TAQPPESVTQ NTEPAVIGYT EEVVLSGTSG SKSVLAKSDT GATRTSIDTS
LAADIGAGPI KSITRIRSGS SKQSKSRPVV DVVVGVGGNQ HTVTASVEDR SHMDYPVLLG
RDILENYQVD VSRRIDSDAP ETPEEEEE
//
