ID   BSHC_BACCN              Reviewed;         538 AA.
AC   A7GRP5;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Putative cysteine ligase BshC {ECO:0000255|HAMAP-Rule:MF_01867};
DE            EC=6.-.-.- {ECO:0000255|HAMAP-Rule:MF_01867};
GN   Name=bshC {ECO:0000255|HAMAP-Rule:MF_01867}; OrderedLocusNames=Bcer98_2569;
OS   Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22905 / CIP 110041 / 391-98 / NVH 391-98;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
CC   -!- FUNCTION: Involved in bacillithiol (BSH) biosynthesis. May catalyze the
CC       last step of the pathway, the addition of cysteine to glucosamine
CC       malate (GlcN-Mal) to generate BSH. {ECO:0000255|HAMAP-Rule:MF_01867}.
CC   -!- SIMILARITY: Belongs to the BshC family. {ECO:0000255|HAMAP-
CC       Rule:MF_01867}.
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DR   EMBL; CP000764; ABS22803.1; -; Genomic_DNA.
DR   RefSeq; WP_012095010.1; NC_009674.1.
DR   AlphaFoldDB; A7GRP5; -.
DR   SMR; A7GRP5; -.
DR   STRING; 315749.Bcer98_2569; -.
DR   EnsemblBacteria; ABS22803; ABS22803; Bcer98_2569.
DR   GeneID; 56418109; -.
DR   KEGG; bcy:Bcer98_2569; -.
DR   eggNOG; COG4365; Bacteria.
DR   HOGENOM; CLU_022249_1_0_9; -.
DR   OMA; TTGHQLN; -.
DR   OrthoDB; 295429at2; -.
DR   Proteomes; UP000002300; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01867; BshC; 1.
DR   InterPro; IPR011199; Bacillithiol_biosynth_BshC.
DR   Pfam; PF10079; BshC; 1.
DR   PIRSF; PIRSF012535; UCP012535; 1.
DR   TIGRFAMs; TIGR03998; thiol_BshC; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Ligase.
FT   CHAIN           1..538
FT                   /note="Putative cysteine ligase BshC"
FT                   /id="PRO_0000378216"
FT   COILED          421..485
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   538 AA;  63193 MW;  BE8A8598F5BF028D CRC64;
     MEIKEISVPL QGVVGDYIKS DNKIQTCFDY ALTEAGFKQR LYDLRNRKFF RQELVEHLLE
     YNKQLQAGQS TIQNIEALAD ENTYVVIGGQ QAGLLTGPLY TVHKVISIVQ LAKEKEASLG
     TRVVPVFWIA GEDHDVDEIN HTFVTKNKKI KKMIFHDRHS KKTSASESEI SIEDCSKWIE
     EIFKTYPETN FTKDVLQFIQ EALEESSTYV DFFARLITKL FADTGLILVD SHHPNLRKLE
     VSFFKRIISQ YKEVQEALHN QQQIVKEYGY KPIIETKQNA IHVFMQIDEE RVLLEEENGK
     FVGKSGIYSF SYEELIEEME QSPERFSNNV VTRPLMQEYL FPTVAFIGGP GEIAYWSELQ
     QVFHVFDFQM PPVVPRLTIS YMERDIITDL YDLNLQEEDP FVKDLDKLRE KWLSNQVEEP
     VEEKFQEAKK NMMDIHSSLQ QFVNRIDPGL KEFAGKNERK IQEQIELLER MLKQNLERRH
     EVELNKFRRL QYALRPLGAP QERVWNVCYY LNQYGLDFVE RVTKQSYSWN GTHHVIKL