RIMK_DESPS
ID RIMK_DESPS Reviewed; 464 AA.
AC Q6AKK4;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Probable alpha-L-glutamate ligase;
DE EC=6.3.2.-;
GN Name=rimK; OrderedLocusNames=DP2392;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: In the C-terminal section; belongs to the RimK family.
CC {ECO:0000305}.
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DR EMBL; CR522870; CAG37121.1; -; Genomic_DNA.
DR RefSeq; WP_011189633.1; NC_006138.1.
DR AlphaFoldDB; Q6AKK4; -.
DR SMR; Q6AKK4; -.
DR STRING; 177439.DP2392; -.
DR EnsemblBacteria; CAG37121; CAG37121; DP2392.
DR KEGG; dps:DP2392; -.
DR eggNOG; COG0189; Bacteria.
DR eggNOG; COG4067; Bacteria.
DR HOGENOM; CLU_045509_0_0_7; -.
DR OMA; CYMNIAS; -.
DR OrthoDB; 359914at2; -.
DR Proteomes; UP000000602; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR008503; Put_Zn_protease.
DR InterPro; IPR041107; Rimk_N.
DR InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR Pfam; PF08443; RimK; 1.
DR Pfam; PF18030; Rimk_N; 1.
DR Pfam; PF05618; Zn_protease; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR TIGRFAMs; TIGR00768; rimK_fam; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..464
FT /note="Probable alpha-L-glutamate ligase"
FT /id="PRO_0000205453"
FT DOMAIN 268..451
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT REGION 1..164
FT /note="Unknown"
FT REGION 165..464
FT /note="Alpha-L-glutamate ligase"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 342..343
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 376..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 412
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 412
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 424
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 424
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 424
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 424
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 426
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 426
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 464 AA; 50877 MW; C2C0DE91EABF4BD6 CRC64;
MSQDIAKKII GSEEWCSFPE LGIPAIKARV DSGAKTSSIH AVNIQTFQRD GEEWVSFEVH
PLRIDRRTVV RCQRPVIDKR IIKNSSGNSE TRFVIRTPLK LNKKVWDIEL TLSNRDAMGF
RMLLGREAMM DRLIIDPALQ CALGEVSKES LGKAYTKEET RKGGLKIGIL ACNESLYGNQ
RLLEAGRERG HEMLFLDIKQ CYLKLDTLEP EVHYKGRLLN DLDAVLTKIG SNITPYATAL
SRQFESMGIY TCNSSSAISQ SGDKLFSLQL LLKSGINIPI TGFANSPIDA SDLIEMVGGA
PLIIKLLEGG QGQGPILAKT KNAAESLINT FKFLRANLLV QQFIKEANGK ILRCLVINGK
VVASIERTAA SGELSSNTHQ DGKSSIVKIT PEERSLALKA AKVLGLQIAS VDIINSKAGP
LLLEVNSSPE LEGIEIATGK DIAGMVISSI EKKLQWKRPL PQQS
