ID L9ZFP7_9EURY Unreviewed; 447 AA.
AC L9ZFP7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=RimK family alpha-L-glutamate ligase {ECO:0000313|EMBL:ELY85164.1};
GN ORFNames=C484_21422 {ECO:0000313|EMBL:ELY85164.1};
OS Natrialba taiwanensis DSM 12281.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrialba.
OX NCBI_TaxID=1230458 {ECO:0000313|EMBL:ELY85164.1, ECO:0000313|Proteomes:UP000011648};
RN [1] {ECO:0000313|EMBL:ELY85164.1, ECO:0000313|Proteomes:UP000011648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12281 {ECO:0000313|EMBL:ELY85164.1,
RC ECO:0000313|Proteomes:UP000011648};
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:ELY85164.1}.
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DR EMBL; AOIL01000069; ELY85164.1; -; Genomic_DNA.
DR RefSeq; WP_006827840.1; NZ_AOIL01000069.1.
DR AlphaFoldDB; L9ZFP7; -.
DR STRING; 1230458.C484_21422; -.
DR PATRIC; fig|1230458.4.peg.4320; -.
DR OrthoDB; 200216at2157; -.
DR Proteomes; UP000011648; 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:ELY85164.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT DOMAIN 105..286
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 447 AA; 47853 MW; CBDB1B0AD625E6F3 CRC64;
MAAAEPVTVG VLSLHTSKET KAILNAVDEL GHDTEWLRHE NTSISVTDGR VDLEPAVDVI
ANRMLLSNTE QPAEELGLAN TFAQVVPMLN DPATVLTAMH KLSTATALAT AAVQVPNVVL
ALSSDQLNAV RDRYGDEAVY KTAIGTHGGG TWKVGPGDPV NAKVGNRYAF LQELIDRDDR
RHRDVRIYVV DGTIIGAMYR YAPDNDWRTN VALGGTVEDA TDDLPEPAQR LATRAADAIG
LDYAGVDLVE SDDGWYVLEV NPTAGFKGLY EATRISPAPY IAKLAIEHAG GTVDQDRVDE
LATELDDSQP GAQPIRQTQP ETEPTVIGYT EEVILSGTSG STGVLAKSDT GATRTSIDTG
LAAEIGAGPI KSITRVKSGS SKTTRSRPVV DVVVGIGGNQ HTVTASVEDR DHMDYPVLLG
RDILSHYRVD VGRRADRNAD DLPEEEE
//
