ID   B0SSC5_LEPBP            Unreviewed;       335 AA.
AC   B0SSC5;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Glutathione synthase {ECO:0000313|EMBL:ABZ98015.1};
DE            EC=6.3.2.3 {ECO:0000313|EMBL:ABZ98015.1};
GN   Name=gshB {ECO:0000313|EMBL:ABZ98015.1};
GN   OrderedLocusNames=LEPBI_I1912 {ECO:0000313|EMBL:ABZ98015.1};
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ98015.1, ECO:0000313|Proteomes:UP000001847};
RN   [1] {ECO:0000313|EMBL:ABZ98015.1, ECO:0000313|Proteomes:UP000001847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris
RC   {ECO:0000313|Proteomes:UP000001847};
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
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DR   EMBL; CP000786; ABZ98015.1; -; Genomic_DNA.
DR   RefSeq; WP_012388893.1; NC_010602.1.
DR   AlphaFoldDB; B0SSC5; -.
DR   STRING; 456481.LEPBI_I1912; -.
DR   KEGG; lbi:LEPBI_I1912; -.
DR   HOGENOM; CLU_053807_0_0_12; -.
DR   OrthoDB; 9803907at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS09440-MONOMER; -.
DR   Proteomes; UP000001847; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004363; F:glutathione synthase activity; IEA:UniProtKB-EC.
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; 2.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR040657; GshAB_ATP-grasp.
DR   PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR   PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR   Pfam; PF18419; ATP-grasp_6; 1.
DR   Pfam; PF08443; RimK; 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:ABZ98015.1};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT   DOMAIN          77..333
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   335 AA;  37370 MW;  7A0C8D368DE7ADF5 CRC64;
     MTEPKPLLPG WEDLEISTQI IIRDAISRGI EVQVIDRKEN FLRLKQGSHT EFVKEASKTR
     LDSLMTYLVM ENKIASKLVL AEDGVRVPIG KHYSRLEDAL NDYTIFQNKK KVVKPVTTNF
     GIGIGISEPN DSLEKFTYFV KQSFSFSSSI IIEEFIEGPE YRFLVLGDEV VAVCNRVPAN
     VVGDGIKTIS ELIEEKNRDP RRGEGHITAL EKIQMSDVER LVLLDQGFEF LSIPKKGEQV
     FLRKNSNIST GGDSVDVTDL VHPEFKTIAL KAARAAGAVI CGIDIISSAI TETPNPETYA
     ILEINFNPVL YIHEFPYSGT PRAVGDTILN LLGFH
//