ID   BSHC_BACMK              Reviewed;         538 AA.
AC   A9VU81;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 58.
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};
GN   OrderedLocusNames=BcerKBAB4_3746;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
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; CP000903; ABY44915.1; -; Genomic_DNA.
DR   RefSeq; WP_012261611.1; NC_010184.1.
DR   AlphaFoldDB; A9VU81; -.
DR   SMR; A9VU81; -.
DR   STRING; 315730.BcerKBAB4_3746; -.
DR   EnsemblBacteria; ABY44915; ABY44915; BcerKBAB4_3746.
DR   KEGG; bwe:BcerKBAB4_3746; -.
DR   eggNOG; COG4365; Bacteria.
DR   HOGENOM; CLU_022249_1_0_9; -.
DR   OMA; TTGHQLN; -.
DR   Proteomes; UP000002154; 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_0000378223"
FT   COILED          460..483
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   538 AA;  62933 MW;  C0EE8AAA00F8859E CRC64;
     MEIKEISVPL QGVVADYMNG KKEIQSCFDY LLTEDAFKQR LHDLREREFF RQDLVTHLLE
     YNTQLQAGEF TIQNIKALED ENTYVVIAGQ QAGLLTGPLY TVHKIISILQ LAKEKEESLG
     VRVVPVFWIA GEDHDMDEIN HTFVTKNKKI KKTIFHDRYP KKASASESEF SIEDCRKWVE
     EIFKTYPETN FTKDVLQFVD DALGKSHTYV DFFAHLITKM FANSGLILVD SHHPALRKLE
     VPFLQQIISK YKEIQVGLRN QQEVLKELGF KPIIETKTNA VHIFMEIDNE RVLLEENQGK
     FIGKDGVHSF SYEELMEEME RSPERFSNNV VTRPLMQEYV FPTLAFIGGP GELAYWSELQ
     QVFHTAGFQM PPVVPRLTIT YMERDTATDL YDLDLQEIDP FLNNIDNLRD NWLSNQIEEP
     IDERFIEAKK EIMDIHTSLQ QFVKKIDPGL NEFAGKNELK INEQIELLEK MLKRNVEKKH
     EVQLNKFRRL QFALRPLGAP QERVWNVCYY LNQFGLDFVD RVMEQSFSWD GKHHVIKL