ID   A0A2K4G2P4_9PSED        Unreviewed;       528 AA.
AC   A0A2K4G2P4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=RimK family alpha-L-glutamate ligase {ECO:0000313|EMBL:POA17880.1};
GN   ORFNames=C1886_19825 {ECO:0000313|EMBL:POA17880.1};
OS   Pseudomonas sp. FW300-N1A1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2075555 {ECO:0000313|EMBL:POA17880.1, ECO:0000313|Proteomes:UP000236411};
RN   [1] {ECO:0000313|EMBL:POA17880.1, ECO:0000313|Proteomes:UP000236411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FW300-N1A1 {ECO:0000313|EMBL:POA17880.1,
RC   ECO:0000313|Proteomes:UP000236411};
RA   Spencer S.J., Aaring A.B., Hendricks A., Penterman J., Chakraborty R.,
RA   Alm E.J.;
RT   "Whole genome sequencing of deep branching strains shows evolution and
RT   exchange across a contaminated watershed.";
RL   Submitted (JAN-2018) 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:POA17880.1}.
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DR   EMBL; PPSF01000055; POA17880.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K4G2P4; -.
DR   Proteomes; UP000236411; 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   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   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR025839; RLAN_dom.
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; PF14401; RLAN; 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:POA17880.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          325..516
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   528 AA;  59876 MW;  566F97514C95029C CRC64;
     MSAVQGGLRE VSEQNRLTAI SNLTYLAGAP GRSSQVIIIV ERKEDWASYF PSEDVMSAQE
     YLEQPLEIEA GKRVQVINLC RSYKYLGHGY YCSLLAEARG HKVIPSVRTI SELTKKSLYG
     LALDDLGKTL DKALNNHIYS NTEGFTLTLY FGKTNLEPLQ ELARQIFEIF PCPILLVEFR
     KSNSWRIDGI KSGVLQKLRE DQEDPFANSL DSFSRKVWRV PRSPRVARYD LAILHDPQEA
     LPPSNAKALD SFIRVGKGLG IDVDLIEKKD YSRIAEYDAL LIRETTSVDN HTYRFAKKAE
     SEGLVVMDDP ASILRCTNKV YLTDLLKSHQ LGMPATEILY KERPEDFERV GERLGFPLVL
     KIPDGCFSRG VIKVESQQAL LEATSELFEH SVLLLAQEFF YTEYDWRIGV LNRKPIFACQ
     YFMSKGHWQI YNHKAKGQDI NGECRTLAVH EAPRAVVELA VKTANLIGDG LYGVDLKQSG
     DKVVVIEVND NPNLDAGIED AYLQDDLYAL VLEEFIRRLE LKRRGQAW
//