ID   E4PJF2_MARAH            Unreviewed;       515 AA.
AC   E4PJF2;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Glutathione synthase/ribosomal protein S6 modification enzyme {ECO:0000313|EMBL:ADP97138.1};
GN   OrderedLocusNames=HP15_1374 {ECO:0000313|EMBL:ADP97138.1};
OS   Marinobacter adhaerens (strain DSM 23420 / HP15).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Marinobacteraceae; Marinobacter.
OX   NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP97138.1, ECO:0000313|Proteomes:UP000007077};
RN   [1] {ECO:0000313|EMBL:ADP97138.1, ECO:0000313|Proteomes:UP000007077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX   PubMed=21304739;
RA   Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA   Glockner F.O., Grossart H.P., Ullrich M.S.;
RT   "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT   diatom-interacting marine microorganism.";
RL   Stand. Genomic Sci. 3:97-107(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA   Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA   Gloeckner F.O., Ullrich M.S.;
RT   "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001978; ADP97138.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4PJF2; -.
DR   STRING; 225937.HP15_1374; -.
DR   KEGG; mad:HP15_1374; -.
DR   PATRIC; fig|225937.3.peg.1381; -.
DR   eggNOG; COG0189; Bacteria.
DR   HOGENOM; CLU_016765_0_0_6; -.
DR   Proteomes; UP000007077; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          314..506
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   515 AA;  58352 MW;  F749334D3862A761 CRC64;
     MATITTGKTF QGGMPSMSRL LIVVDRAKDW APYYPSEDVL TFDQYLQFSA PPASRVRVIN
     LCQSARYLSK GYYCSLLAEA RGHHVVPSVM TLNDLGRKGL FSLELEELDE SVINWLEAAG
     SAIDPASDER AATHEVRIRT YFGQAEHPDL KPVARALFER FPCPILEIVF KRRKQWQIES
     MKPAAPADLG EQEQDVFAAA LDRFSSMVWR KPRARRRYRY DLAVLVNPDE EMPPSDKVAL
     KRFEKAGRKL GINVEQITRR DYMRLPEYDG LFIRETTAID HHTYRFARKA AAEGMVVIDD
     PVSILKCTNK VFLADLLKNN KVPTPKTLIL SKDQKNAVEQ VISELGFPVV IKIPDGAFSR
     GVTKAEDEKT LRAGLRDLFK QSALVLAQEY LYTDYDWRIG VLGGRAIYAC KYMMVKGHWQ
     IYQHSESESE SGGFETMPTY EVPRNVIQAA LNATRLIGNG LYGVDIKQSG NRVAVIEVND
     NPSIDAGVED CFLGGELYTL IMQEFLSRME ENRRR
//