ID M0JY67_9EURY Unreviewed; 450 AA.
AC M0JY67;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=RimK family alpha-L-glutamate ligase {ECO:0000313|EMBL:QUJ73102.1};
GN ORFNames=C436_08352 {ECO:0000313|EMBL:EMA13936.1}, KDQ40_04955
GN {ECO:0000313|EMBL:QUJ73102.1};
OS Haloarcula sinaiiensis ATCC 33800.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=662476 {ECO:0000313|EMBL:EMA13936.1, ECO:0000313|Proteomes:UP000011659};
RN [1] {ECO:0000313|EMBL:EMA13936.1, ECO:0000313|Proteomes:UP000011659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33800 {ECO:0000313|EMBL:EMA13936.1,
RC ECO:0000313|Proteomes:UP000011659};
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).
RN [2] {ECO:0000313|EMBL:QUJ73102.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 33800 {ECO:0000313|EMBL:QUJ73102.1};
RA Fomenkov A., DasSarma P., DasSarma S., Roberts R.J.;
RT "Complete Genome sequence and Methylome Analysis of the Haloarchaeon
RT Haloarcula sinaiiensis.";
RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AOLR01000016; EMA13936.1; -; Genomic_DNA.
DR EMBL; CP073366; QUJ73102.1; -; Genomic_DNA.
DR RefSeq; WP_004961009.1; NZ_CP073366.1.
DR AlphaFoldDB; M0JY67; -.
DR GeneID; 64822281; -.
DR KEGG; hsin:KDQ40_04955; -.
DR PATRIC; fig|662476.7.peg.1663; -.
DR OrthoDB; 200216at2157; -.
DR Proteomes; UP000011659; Unassembled WGS sequence.
DR Proteomes; UP000682967; 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; 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:QUJ73102.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 104..285
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 431..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 450 AA; 48485 MW; 68AC5E0B3C860E4E CRC64;
MSDQDLTVGV LSLHSSKESK AILNAVDEMG YDTEWLRAEN TAISVSDGEM TLDPRVDVVA
NRLLLSSDEH PAEGIGLGMT ISRLAPTLNE PMAATTALHK FASAAALADA GVPVPDALLA
LSSDMLNEER DRFGDRAVYK TAIGTHGGGT WMVDLENQVN AQVGGRYAFL QEYMEHDEQR
HHDLRVYVVG DQIVGAMNRY APEGEWRTNV ALGGEVEDMT GELPERVREI ALDSVDAIGL
DYAGVDIVQS DDGYYVLEVN PTAGFRGLFK ASGVSPAPYI AQLAIERAGG SVDHETVERL
SDRLDDSKPA CTPKKPQPKA QENVVVGYIE EVVVTGTQGT KSVLAKSDTG ATRTSIDAKL
AAEIGTGPIL DIVKIKSGSL KSGRSRPVVD LVVGVGGTQH TVTASVEDRG HMDYPLLLGR
DILKHYQVDV TRRADDESDV ETEEEEQSEE
//
