ID L9Y7L4_9EURY Unreviewed; 448 AA.
AC L9Y7L4;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Alpha-L-glutamate ligase, RimK family protein {ECO:0000313|EMBL:ELY70045.1};
GN ORFNames=C489_03821 {ECO:0000313|EMBL:ELY70045.1};
OS Natrinema versiforme JCM 10478.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1227496 {ECO:0000313|EMBL:ELY70045.1, ECO:0000313|Proteomes:UP000011632};
RN [1] {ECO:0000313|EMBL:ELY70045.1, ECO:0000313|Proteomes:UP000011632}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10478 {ECO:0000313|EMBL:ELY70045.1,
RC ECO:0000313|Proteomes:UP000011632};
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:ELY70045.1}.
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DR EMBL; AOID01000013; ELY70045.1; -; Genomic_DNA.
DR RefSeq; WP_006429813.1; NZ_AOID01000013.1.
DR AlphaFoldDB; L9Y7L4; -.
DR STRING; 1227496.C489_03821; -.
DR PATRIC; fig|1227496.3.peg.766; -.
DR OrthoDB; 200216at2157; -.
DR Proteomes; UP000011632; 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:ELY70045.1};
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; 47932 MW; AC26BC3BF0026661 CRC64;
MAVADPVTVG VLSLHTSKET KAILNAVEDL GHDSEWLRAE NTSISVRDGS PVLEPDVDVI
ANRMLLSNTE QPAEELGLAN TFAQLVPTLN EPNSVLTAIH KLSTAAALAS NDVRTPDVTL
ALSGDKLNAA RDRYGEEAVY KTAIGTHGGG TWKVGPDDPI NAKVGNRYAF LQELVDQEDV
RHRDLRVYVV GGEVVAAMYR YAPDNDWRTN VALGGSVEDA TDDLPEEARE MAQRAADIID
LDYAGVDLVE GDEGWFVLEV NPTAGFKGLY EATQMSPAPY IAKLAIERAG GEVDDDRVRE
ISNVLDDSRP AAQPPEAITA DTEPAIIGYT EEVVLSGTSG SKSVLAKSDT GATRTSIDTG
LAADIGAGPI KSITRIRSGS SKQSKSRPVV DVVVGVGGNQ HTVTASVEDR SHMDYPVLLG
RDILENYQVD VSRRIDSDAA DTPEEEEE
//
