ID I1XJ53_METNJ Unreviewed; 301 AA.
AC I1XJ53;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 73.
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=Q7A_1598 {ECO:0000313|EMBL:AFI84422.1};
GN ORFNames=CDW43_07795 {ECO:0000313|EMBL:AUZ84489.1};
OS Methylophaga nitratireducenticrescens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI84422.1, ECO:0000313|Proteomes:UP000009144};
RN [1] {ECO:0000313|EMBL:AFI84422.1, ECO:0000313|Proteomes:UP000009144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI84422.1,
RC ECO:0000313|Proteomes:UP000009144};
RX PubMed=22815445; DOI=10.1128/JB.00726-12;
RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT sp. strain JAM7.";
RL J. Bacteriol. 194:4126-4127(2012).
RN [2] {ECO:0000313|EMBL:AFI84422.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI84422.1};
RX PubMed=23148104; DOI=10.1099/ijs.0.044545-0;
RA Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT "Methylophaga nitratireducenticrescens sp. nov. and Methylophaga frappieri
RT sp. nov., isolated from the biofilm of the methanol-fed denitrification
RT system treating the seawater at the Montreal Biodome.";
RL Int. J. Syst. Evol. Microbiol. 63:2216-2222(2013).
RN [3] {ECO:0000313|EMBL:AFI84422.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JAM1 {ECO:0000313|EMBL:AFI84422.1};
RA Villeneuve C., Villemur R.;
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AUZ84489.1, ECO:0000313|Proteomes:UP000238402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP59 {ECO:0000313|EMBL:AUZ84489.1,
RC ECO:0000313|Proteomes:UP000238402};
RA Villemur R.;
RT "The sequence of the genome of Methylophaga nitratireducenticrescens GP59
RT and its two plasmids.";
RL Submitted (JUN-2017) 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}.
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DR EMBL; CP003390; AFI84422.1; -; Genomic_DNA.
DR EMBL; CP021973; AUZ84489.1; -; Genomic_DNA.
DR RefSeq; WP_014706795.1; NZ_CP021973.1.
DR AlphaFoldDB; I1XJ53; -.
DR STRING; 754476.Q7A_1598; -.
DR KEGG; mej:Q7A_1598; -.
DR PATRIC; fig|754476.3.peg.1578; -.
DR eggNOG; COG0189; Bacteria.
DR HOGENOM; CLU_054353_0_1_6; -.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000009144; Chromosome.
DR Proteomes; UP000238402; Chromosome.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
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:0016740; F:transferase activity; 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}; Ribonucleoprotein {ECO:0000313|EMBL:AUZ84489.1};
KW Ribosomal protein {ECO:0000313|EMBL:AUZ84489.1};
KW Transferase {ECO:0000313|EMBL:AFI84422.1}.
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 301 AA; 32399 MW; 31ACD457237F942F CRC64;
MKIAILSRNS KLYSTRRLVE AAEARGHEVD VLDVLRCYMN ITSMKPEVHY KGENLTGYDA
VIPRIGASVT FYGTAVLRQF EMMNVYPLNE SVAISRSRDK LRALQLLSRR GIGLPVTGFA
HRPDDVDDLI KMVGGAPLVI KLLEGTQGIG VVLAETAGAA ESVIEAFMGM KANILVQEFI
KEAGGADIRC FVVGEKVVAA MKRQGKEGEF RSNLHRGGSA NLIRITPAER ATAVRAAKTM
GLNVCGVDLL RSNHGPVVME VNSSPGLEGI ESATGKDIAS LIIDFIEKNS VSGTTKTKGR
G
//
