ID A0A0W1RS95_9GAMM Unreviewed; 306 AA.
AC A0A0W1RS95;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Probable alpha-L-glutamate ligase {ECO:0000256|HAMAP-Rule:MF_01552};
DE EC=6.3.2.- {ECO:0000256|HAMAP-Rule:MF_01552};
GN Name=rimK {ECO:0000256|HAMAP-Rule:MF_01552};
GN ORFNames=AUR63_03855 {ECO:0000313|EMBL:KTG16494.1};
OS Guyparkeria sp. XI15.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Thioalkalibacteraceae; Guyparkeria.
OX NCBI_TaxID=1766620 {ECO:0000313|EMBL:KTG16494.1, ECO:0000313|Proteomes:UP000053033};
RN [1] {ECO:0000313|Proteomes:UP000053033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XI15 {ECO:0000313|Proteomes:UP000053033};
RA Zhang G., Stingl U., Rashid M.;
RT "Haloferax marisrubri sp. nov., isolated from the Discovery deep brine-
RT seawater interface in the Red Sea.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01552};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01552};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000256|HAMAP-Rule:MF_01552};
CC -!- SIMILARITY: Belongs to the RimK family. {ECO:0000256|HAMAP-
CC Rule:MF_01552}.
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:KTG16494.1}.
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DR EMBL; LOPX01000015; KTG16494.1; -; Genomic_DNA.
DR RefSeq; WP_058575444.1; NZ_LOPX01000015.1.
DR AlphaFoldDB; A0A0W1RS95; -.
DR STRING; 1766620.AUR63_03855; -.
DR Proteomes; UP000053033; Unassembled WGS sequence.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR HAMAP; MF_01552; RimK; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR023533; RimK.
DR InterPro; IPR041107; Rimk_N.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR PANTHER; PTHR21621:SF7; RIBOSOMAL PROTEIN S6--L-GLUTAMATE LIGASE; 1.
DR Pfam; PF08443; RimK; 1.
DR Pfam; PF18030; Rimk_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01552};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01552};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01552};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01552};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01552};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01552};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_01552}; Reference proteome {ECO:0000313|Proteomes:UP000053033}.
FT DOMAIN 104..287
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01552"
FT BINDING 178..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01552"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01552"
FT BINDING 211..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01552"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01552"
FT BINDING 248
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01552"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01552"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01552"
FT BINDING 260
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01552"
FT BINDING 260
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01552"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01552"
FT BINDING 262
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01552"
SQ SEQUENCE 306 AA; 33404 MW; E253B3A949B8BE21 CRC64;
MKIAILSRNP KLYSTRRLIE AAEERGHEVR VLDVLRCYMN IASNNPEVHY KGEELEGFDA
VIPRIGASIT FYGTAVLRQF EMMGTAPLNE SVAISRSRDK LRSLQLLSRK GIGLPVTGFA
HRPDDVEDLI KMVGGAPLVI KLLEGTQGIG VVLAETKQAA ESVIEAFMGT KTNILVQEYI
REANGADIRC FVIGDKVVAA MKRQGAEGEF RSNLHRGGSA SLIRITPEER STAVRAAKTM
GLNVAGVDLL RSNHGAVVME VNSSPGLEGI EKATGKDIAG MQIQFIEKRL AERRTKRGLT
RTRGHG
//
