ID RIMK_ALIFM Reviewed; 301 AA.
AC B5FBB1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 16-JAN-2019, entry version 66.
DE RecName: Full=Probable alpha-L-glutamate ligase {ECO:0000255|HAMAP-Rule:MF_01552};
DE EC=6.3.2.- {ECO:0000255|HAMAP-Rule:MF_01552};
GN Name=rimK {ECO:0000255|HAMAP-Rule:MF_01552};
GN OrderedLocusNames=VFMJ11_0676;
OS Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC Vibrionaceae; Aliivibrio.
OX NCBI_TaxID=388396;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ11;
RA Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J.,
RA Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R.,
RA Frazier M., Venter J.C.;
RT "Complete sequence of Vibrio fischeri strain MJ11.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01552};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01552};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|HAMAP-Rule:MF_01552};
CC -!- SIMILARITY: Belongs to the RimK family. {ECO:0000255|HAMAP-
CC Rule:MF_01552}.
DR EMBL; CP001139; ACH66138.1; -; Genomic_DNA.
DR RefSeq; WP_012533521.1; NC_011184.1.
DR ProteinModelPortal; B5FBB1; -.
DR SMR; B5FBB1; -.
DR EnsemblBacteria; ACH66138; ACH66138; VFMJ11_0676.
DR KEGG; vfm:VFMJ11_0676; -.
DR HOGENOM; HOG000293092; -.
DR KO; K05844; -.
DR OMA; NYLRCYM; -.
DR Proteomes; UP000001857; Chromosome I.
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:0006464; P:cellular protein modification process; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; -; 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; IPR004666; RpS6_RimK/Lys_biosynth_LsyX.
DR Pfam; PF08443; RimK; 1.
DR TIGRFAMs; TIGR00768; rimK_fam; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Ligase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1 301 Probable alpha-L-glutamate ligase.
FT /FTId=PRO_1000146953.
FT DOMAIN 104 287 ATP-grasp. {ECO:0000255|HAMAP-
FT Rule:MF_01552}.
FT NP_BIND 178 179 ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT NP_BIND 211 213 ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT METAL 248 248 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_01552}.
FT METAL 260 260 Magnesium or manganese 1.
FT {ECO:0000255|HAMAP-Rule:MF_01552}.
FT METAL 260 260 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_01552}.
FT METAL 262 262 Magnesium or manganese 2.
FT {ECO:0000255|HAMAP-Rule:MF_01552}.
FT BINDING 141 141 ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
FT BINDING 187 187 ATP. {ECO:0000255|HAMAP-Rule:MF_01552}.
SQ SEQUENCE 301 AA; 32409 MW; B0CB162A5CE6A801 CRC64;
MKIGILSRNQ SLYSTSRLIE AAESRGHEVK VIDALRCYMN INSEKPQIHF KGEELVDYDA
IIPRIGASVT FYGTAVLRQF EMMGVYPVNE SVAITRSRDK LRSMQLLSRK GIGMPITGFA
SKPDDVKDLL DMVGGAPVVI KLLEGTQGIG VVLAETRKAA ESVVEAFMGL KANIMVQEFI
KEAGGADIRC FVIGGKVIAA MKRQGAEGEF RSNLHRGGSA SLVKLTPEER KTAVAAANIM
GLNVAGVDLL RSERGPLVME VNSSPGLEGI EKATGKDVAG LIIDFIEKTA ATKRTKTRGK
G
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