ID A0A0Q8VJE7_9ACTN Unreviewed; 395 AA.
AC A0A0Q8VJE7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Alpha-L-glutamate ligase {ECO:0000313|EMBL:KRC53255.1};
GN ORFNames=ASE19_12915 {ECO:0000313|EMBL:KRC53255.1};
OS Nocardioides sp. Root79.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC53255.1, ECO:0000313|Proteomes:UP000051414};
RN [1] {ECO:0000313|EMBL:KRC53255.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC53255.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC53255.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC53255.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRC53255.1}.
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DR EMBL; LMIP01000011; KRC53255.1; -; Genomic_DNA.
DR RefSeq; WP_056895717.1; NZ_LMIP01000011.1.
DR AlphaFoldDB; A0A0Q8VJE7; -.
DR OrthoDB; 3865600at2; -.
DR Proteomes; UP000051414; Unassembled WGS sequence.
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:0008324; F:monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; 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; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.30.70.1450; Regulator of K+ conductance, C-terminal domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013651; ATP-grasp_RimK-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006037; RCK_C.
DR InterPro; IPR036721; RCK_C_sf.
DR InterPro; IPR041107; Rimk_N.
DR InterPro; IPR004666; Rp_bS6_RimK/Lys_biosynth_LsyX.
DR NCBIfam; TIGR00768; rimK_fam; 1.
DR PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR Pfam; PF08443; RimK; 1.
DR Pfam; PF18030; Rimk_N; 1.
DR Pfam; PF02080; TrkA_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF116726; TrkA C-terminal domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS51202; RCK_C; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Ligase {ECO:0000313|EMBL:KRC53255.1};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000051414}.
FT DOMAIN 104..287
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 296..380
FT /note="RCK C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51202"
SQ SEQUENCE 395 AA; 43427 MW; 02F5857E1B6F7D20 CRC64;
MKLAILSRAP RSYSTQRLRT AALDRGHQVK VLNTLRFAID LSGDLPDLQF RGKQLSDYDA
ILPRIGNSIT YFGTAVVRQF EQMDVYTPNT ANGISNSRDK LRASQILSRH NISMPATTFV
RDRADVIPAI ERVGGAPVVI KLLEGTQGIG VILAPSIKVA EAIIETLQST KQQVLIQRFV
KESRGRDLRA LVVGDRVVAA MRRVAQGDEF RSNVHRGGSV EPVELDAEAE RIAVRAAQIM
GLKVAGVDML EADDGPQVME VNSSPGLEGI ENATKLDVAG AIIDYIDNQV AFPQIDVRER
LSVSTGYGVA ELLVHADADL VGKSLGDSGL RDRDITVLTL HRGTMVIPNP FPHHVLEAED
RLLCFGKLEE MRSMIPARRK RTRVKKLPKQ PIHTD
//
