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Database: UniProt
Entry: A0A0H3FQN4_KLEAK
LinkDB: A0A0H3FQN4_KLEAK
Original site: A0A0H3FQN4_KLEAK 
ID   A0A0H3FQN4_KLEAK        Unreviewed;       300 AA.
AC   A0A0H3FQN4;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 49.
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   OrderedLocusNames=EAE_14865 {ECO:0000313|EMBL:AEG97886.1};
OS   Klebsiella aerogenes (strain ATCC 13048 / DSM 30053 / CCUG 1429 / JCM 1235
OS   / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006 / CDC 819-56)
OS   (Enterobacter aerogenes).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=1028307 {ECO:0000313|EMBL:AEG97886.1, ECO:0000313|Proteomes:UP000008881};
RN   [1] {ECO:0000313|Proteomes:UP000008881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 /
RC   NCIMB 10102 / NCTC 10006 {ECO:0000313|Proteomes:UP000008881};
RA   Shin S.H., Kim S., Kim J.Y., Yang K.-S., Seo J.-S.;
RT   "Complete sequence of Enterobacter aerogenes KCTC 2190.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEG97886.1, ECO:0000313|Proteomes:UP000008881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 /
RC   NCIMB 10102 / NCTC 10006 {ECO:0000313|Proteomes:UP000008881};
RX   PubMed=22493190; DOI=10.1128/JB.00028-12;
RA   Shin S.H., Kim S., Kim J.Y., Lee S., Um Y., Oh M.K., Kim Y.R., Lee J.,
RA   Yang K.S.;
RT   "Complete genome sequence of Enterobacter aerogenes KCTC 2190.";
RL   J. Bacteriol. 194:2373-2374(2012).
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}.
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DR   EMBL; CP002824; AEG97886.1; -; Genomic_DNA.
DR   RefSeq; WP_015704854.1; NC_015663.1.
DR   RefSeq; YP_004593165.1; NC_015663.1.
DR   AlphaFoldDB; A0A0H3FQN4; -.
DR   KEGG; eae:EAE_14865; -.
DR   PATRIC; fig|1028307.3.peg.2970; -.
DR   eggNOG; COG0189; Bacteria.
DR   HOGENOM; CLU_054353_0_1_6; -.
DR   OrthoDB; 3865600at2; -.
DR   Proteomes; UP000008881; Chromosome.
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}.
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   300 AA;  32363 MW;  F71F427AA8D4F1C6 CRC64;
     MKIAILSRDG TLYSCRRLRE AAQKRGHQVE ILDPLSCYMS VSPVASSIHY KGRQLPHFDA
     VIPRIGTAIT YYGTAALRQF ELLGSYPLNE SVAITRARDK LRSLQLLARQ GIDLPVTGIA
     HSPDDTSDLI AMVGGAPLVV KLVEGTQGIG VVLAETRQAA ESVIDAFRGL NAHILVQEYI
     AEAKGCDIRC LVVGDEVVAA IERRAKEGDF RSNLHRGGVA TTAMLSDQER EMAIKAAQTL
     GLDVAGVDIL RAHRGPLVME VNASPGLEGI ETTTHVDIAG RMIAWIERQA TPGYCLKMGG
//
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