ID M0D635_9EURY Unreviewed; 442 AA.
AC M0D635;
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=Alpha-L-glutamate ligase, RimK family protein {ECO:0000313|EMBL:ELZ30147.1};
GN ORFNames=C473_13554 {ECO:0000313|EMBL:ELZ30147.1};
OS Halorubrum terrestre JCM 10247.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum; Halorubrum distributum group.
OX NCBI_TaxID=1227486 {ECO:0000313|EMBL:ELZ30147.1, ECO:0000313|Proteomes:UP000011572};
RN [1] {ECO:0000313|EMBL:ELZ30147.1, ECO:0000313|Proteomes:UP000011572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10247 {ECO:0000313|EMBL:ELZ30147.1,
RC ECO:0000313|Proteomes:UP000011572};
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:ELZ30147.1}.
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DR EMBL; AOIW01000066; ELZ30147.1; -; Genomic_DNA.
DR AlphaFoldDB; M0D635; -.
DR PATRIC; fig|1227486.3.peg.2622; -.
DR Proteomes; UP000011572; 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 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 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:ELZ30147.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 95..276
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 422..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 442 AA; 47625 MW; 341009CC637208AC CRC64;
MLSLHNSKET KAICNAVEDL GHEPVWLREE NAAVSVEDGD VSVEPAVDVI ANRLLLSNTD
QPAELLGLAT TFERIRPMLN EPDAVLASIH KFATAATLAD WNIRVPDALL ALSNDRLNEG
RERFGDVGVY KTAIGTHGGG TWKVDLTERV NPKVGNRQAF LQQLIDRDDE KHRDLRVYVV
GDEIVGSMYR YAPEGDWRTN VALGGAVEDA TDDMPQEAAD TALYAAEVMG LDYAGVDLVE
GYDGWYVLEV NPTAGFKGLF EATGTSPAPH IAKLAIETVG GEVDDEAVER VAATLDDSRP
SCAPAPKPSS TEQPDIGYIE EVVVTGTSGS TQALAKSDTG ATRTSIDTQL AAEIGAGPIK
SMTRVKSGSM KGGKARPVVD LVIGIGGNQH TVTASVEDRG HMEYPLLLGR DILTDYRVDV
RRRADTDETE RDEAGEILEE EE
//
