ID   E1X697_HALMS            Unreviewed;       316 AA.
AC   E1X697;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Glutathione synthetase {ECO:0000313|EMBL:CBW27442.1};
GN   OrderedLocusNames=BMS_2662 {ECO:0000313|EMBL:CBW27442.1};
OS   Halobacteriovorax marinus (strain ATCC BAA-682 / DSM 15412 / SJ)
OS   (Bacteriovorax marinus).
OC   Bacteria; Bdellovibrionota; Bacteriovoracia; Bacteriovoracales;
OC   Halobacteriovoraceae; Halobacteriovorax.
OX   NCBI_TaxID=862908 {ECO:0000313|EMBL:CBW27442.1, ECO:0000313|Proteomes:UP000008963};
RN   [1] {ECO:0000313|Proteomes:UP000008963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-682 / DSM 15412 / SJ
RC   {ECO:0000313|Proteomes:UP000008963};
RX   PubMed=22955231; DOI=10.1038/ismej.2012.90;
RA   Crossman L.C., Chen H., Cerdeno-Tarraga A.M., Brooks K., Quail M.A.,
RA   Pineiro S.A., Hobley L., Sockett R.E., Bentley S.D., Parkhill J.,
RA   Williams H.N., Stine O.C.;
RT   "A small predatory core genome in the divergent marine Bacteriovorax
RT   marinus SJ and the terrestrial Bdellovibrio bacteriovorus.";
RL   ISME J. 7:148-160(2013).
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DR   EMBL; FQ312005; CBW27442.1; -; Genomic_DNA.
DR   RefSeq; WP_014245217.1; NC_016620.1.
DR   AlphaFoldDB; E1X697; -.
DR   STRING; 862908.BMS_2662; -.
DR   KEGG; bmx:BMS_2662; -.
DR   PATRIC; fig|862908.3.peg.2541; -.
DR   eggNOG; COG0189; Bacteria.
DR   HOGENOM; CLU_879318_0_0_7; -.
DR   Proteomes; UP000008963; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004363; F:glutathione synthase activity; 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; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR004218; GSHS_ATP-bd.
DR   InterPro; IPR004215; GSHS_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR21621:SF4; GLUTATHIONE SYNTHETASE; 1.
DR   PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR   Pfam; PF02955; GSH-S_ATP; 1.
DR   Pfam; PF02951; GSH-S_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008963}.
FT   DOMAIN          4..124
FT                   /note="Prokaryotic glutathione synthetase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02951"
FT   DOMAIN          130..303
FT                   /note="Prokaryotic glutathione synthetase ATP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02955"
SQ   SEQUENCE   316 AA;  36237 MW;  C8A3DD1C3896A9DF CRC64;
     MKKHILLIDP LEKLVIKKDS TLMFALTLQK RGIETYLIFE EDFFVSNGDA PKLKVHSFEG
     SFEDDNCYLK DFKLTESLDY QIDKNTLMHM RLDPPFDGRY LRFLWMLRYY KSLGVEVLND
     PDGVLLFNEK LYAYEQESSL KTYVGSSKEG FLGFAQEIMA EGHRELILKP LDLYQGIGVQ
     KISLDDDYAA IFEDKVKQYQ GPVVAQPFAK VVEQGEVRSF YFKGKELGSI LKVPKKGEYL
     ANIAQGASYS RYDLNENQRR ECEKICNELA GYGVHWIAFD ILGDSISEVN ITCPGLVVEV
     SSAYKRNLCE DIIDLL
//