ID A0A1Q2M2D3_9GAMM Unreviewed; 466 AA.
AC A0A1Q2M2D3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Alpha-L-glutamate ligase {ECO:0000313|EMBL:AQQ66830.1};
GN ORFNames=Mag101_03620 {ECO:0000313|EMBL:AQQ66830.1};
OS Microbulbifer agarilyticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Microbulbiferaceae; Microbulbifer.
OX NCBI_TaxID=260552 {ECO:0000313|EMBL:AQQ66830.1, ECO:0000313|Proteomes:UP000188219};
RN [1] {ECO:0000313|EMBL:AQQ66830.1, ECO:0000313|Proteomes:UP000188219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GP101 {ECO:0000313|EMBL:AQQ66830.1,
RC ECO:0000313|Proteomes:UP000188219};
RA Jung J., Bae S.S., Baek K.;
RT "Genome of Microbulbifer agarilyticus GP101.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP019650; AQQ66830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2M2D3; -.
DR STRING; 260552.Mag101_03620; -.
DR KEGG; maga:Mag101_03620; -.
DR eggNOG; COG0189; Bacteria.
DR eggNOG; COG4067; Bacteria.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000188219; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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; 2.40.70.10; Acid Proteases; 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 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; 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 Pfam; PF05618; Zn_protease; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:AQQ66830.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000188219}.
FT DOMAIN 267..450
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 466 AA; 50757 MW; 8398B361E737117A CRC64;
MDNKVIVGSE EWCAFPGLGI PAIKARVDSG AKTSSLHAYN IQPFNRDGEP WVSFEAHPLQ
GQRRPSVRCE ARVLDRRTVR SSSGESEKRL VIKTAISIGG SVWDVELTLT NRDSMGYRML
LGREAMMGRM LVDPSESFCL GDIPPGQLAE VYHDEQHMAG TGLRIGVLAS NPDLYSNQRI
MEAGAERGHR MTFLNIRQCY MKLDSAEPEV HYRDGRILNS LDAVIPRIRP SQTFYGCALT
RHFESMGVYA LNGAQSISQS RDKLYSLQLL QEGGLNIPIS GFANSPSDTN ELIDMVGGAP
LIVKLLEGTQ GRGVVLAETR KAAESVINAF KSLKANLLVQ EFIREAQGKD LRLFVVDGKV
IAAIQREAAP GEFRANIHQG GTASVVKVLP EERRLAIKAA KVLGLKVAGV DIIRSKKGPL
LLEVNSSPGL EGIESATRKD VAGSMILSIE KALKWKPAIV GTSDSA
//
