ID   BSHC_BACCR              Reviewed;         538 AA.
AC   Q812W2;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=BC_3919;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP10840.1; -; Genomic_DNA.
DR   RefSeq; NP_833639.1; NC_004722.1.
DR   RefSeq; WP_000403038.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q812W2; -.
DR   SMR; Q812W2; -.
DR   STRING; 226900.BC_3919; -.
DR   EnsemblBacteria; AAP10840; AAP10840; BC_3919.
DR   GeneID; 67508553; -.
DR   KEGG; bce:BC3919; -.
DR   PATRIC; fig|226900.8.peg.4041; -.
DR   HOGENOM; CLU_022249_1_0_9; -.
DR   OMA; TTGHQLN; -.
DR   Proteomes; UP000001417; 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; Reference proteome.
FT   CHAIN           1..538
FT                   /note="Putative cysteine ligase BshC"
FT                   /id="PRO_0000378211"
FT   COILED          248..268
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   538 AA;  62687 MW;  D597EDBF0126FEE9 CRC64;
     MEIKEISVPQ QGVVADYMNG KKEIQSCFDY MLTEDAFKQR LHDLREREFF RQDLVAHLLE
     YNTKLQAGES TLQNVKALGD ENTYVVIAGQ QAGLLTGPLY TIHKVISILQ LAKEKEESLG
     VKVVPVFWIA GEDHDMDEIN HTFVAKNKKM KKTIFYDRNP KKASASESEL SVEDCRNWIE
     EIFKTYPETN FTKDVLKFVD DALKKSNTYV DFFAHLITKI FANSGLILVD SHHPELRKLE
     IPFFKRIISK YKEVQEGLRN QQEVIKELGY KPIIETKSHA VHIFMEIDDE RVLLEDQQGK
     FVGKDGAHSF SYEELIEEME RNPARFSNNV VTRPLMQEYV FPTLAFIGGP GELAYWSELQ
     QVFHTVGFQM PPVVPRLTIT YVERDIATDL FDLQLRESDP FLNDVDKLRE NWLSNQIEEP
     IDDHFEKAKK EIADIHTSLQ QFVKKIEPGL GAFAGKNELK INEQIELLER MLKRNVEKKY
     EVQLNKFRRI QFALRPLGAP QERVWNVCYY LNQFGLDFVD RVMENPFSWD GKHHVIKL