ID   BSHC_BACCZ              Reviewed;         538 AA.
AC   Q636A7;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=BCE33L3678;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZK / E33L;
RX   PubMed=16621833; DOI=10.1128/jb.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D.,
RA   Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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; CP000001; AAU16588.1; -; Genomic_DNA.
DR   RefSeq; WP_000403063.1; NZ_CP009968.1.
DR   AlphaFoldDB; Q636A7; -.
DR   SMR; Q636A7; -.
DR   EnsemblBacteria; AAU16588; AAU16588; BCE33L3678.
DR   KEGG; bcz:BCE33L3678; -.
DR   PATRIC; fig|288681.22.peg.1733; -.
DR   OMA; TTGHQLN; -.
DR   Proteomes; UP000002612; 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_0000378215"
FT   COILED          460..484
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   538 AA;  62853 MW;  E210AD5D1342C333 CRC64;
     MEIKEISVPQ QGVVADYMNG KKEIQSCFDY MLTEDAFKQR VQDLREREFF RQDLVTHLLE
     YNTKLQAGEA TIQNVKALGD ENTYVVIAGQ QAGLLTGPLY TIHKIISVLQ LAKEKEESLG
     VKVVPVFWIA GEDHDMDEIN HTFVTKNKKI KKTIFHDRNP KKASASESEL SLEDCRKWIE
     EIFKTYPETN FTKDVLQFVD DSLRKSNTYV DFFGHLIMKM FVNSGLILVD SHHPELRKLE
     VPFFKQIVSK YKEVQEGLLN QQEVIKELGY KPIIETKSNA VHIFMEIDNE RVLLEDNQGE
     FVGKDGTYSF SYEELIEEME RSPERFSNNV VTRPLMQEYV FPTLAFIGGP GELAYWSELQ
     QVFHTIGFRM PPVVPRITIT YLERDIATDL HDLQLQESDP FLNNVDKLRE NWLSNQIEEP
     IDERFVEAKK EIMNIHTSLQ QFVKEIDPGL SAFAGKNEFK INEQIELLER MLKRNVEKKH
     EVELNKFRRI QFALRPLGAP QERVWNVCYY LNQFGLDFVD HVMEKTFSWN GKHHVIKL