ID   BSHC_BACC1              Reviewed;         538 AA.
AC   Q732E9;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-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=BCE_3965;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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; AE017194; AAS42868.1; -; Genomic_DNA.
DR   RefSeq; WP_000403055.1; NC_003909.8.
DR   AlphaFoldDB; Q732E9; -.
DR   SMR; Q732E9; -.
DR   EnsemblBacteria; AAS42868; AAS42868; BCE_3965.
DR   GeneID; 59155580; -.
DR   KEGG; bca:BCE_3965; -.
DR   HOGENOM; CLU_022249_1_0_9; -.
DR   OMA; TTGHQLN; -.
DR   Proteomes; UP000002527; 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_0000378210"
FT   COILED          460..484
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   538 AA;  62807 MW;  84D7EF58EE6039E7 CRC64;
     MEIKEISVPQ QGVVADYMNG KKEIQSCFDY MLTEDAFKQR VQDLREREFF RQDLVAHLLE
     YNTKLQAGEA TIQNVKALGD EDTYVVIAGQ QAGLLTGPLY TIHKIISVLQ LAKEKEESLG
     VKVVPVFWIA GEDHDMDEIN HTFVTKNKKI KKTIFHDRNP KKASASESEL SLEDCRKWIE
     EIFKTYPETN FTKDVLQFID DSLGESNTYV DFFGHLIMKM FINSGLILVD SHHPELRKLE
     VPFFKQIISK YKEVQEGLHN QQEVIKELGY KPIIETKSNA VHIFMEIDNE RVLLEDNQGK
     FVGKDGTYSF SYEELIEEME RSPERFSNNV VTRPLMQEYV FPTLAFIGGP GELAYWSELQ
     QVFHTIGFRM PPVVPRITIT YIERDIATDL HDLQLQESDP FLNNVDKLRE NWLSNQIEEP
     IDERFVEAKK EIIDIHKSLQ QFVKKIDPGL SSFAGKNEFK INEQIELLER MLKRNVEKKH
     EVELNKFRRI QFAIRPLGAP QERVWNVCYY LNQFGLDFVD RVMENSFSWN GKHHVIKL