ID   BSHC_BACC4              Reviewed;         538 AA.
AC   B7H6Q5;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 55.
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=BCB4264_A4020;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus B4264.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001176; ACK63708.1; -; Genomic_DNA.
DR   RefSeq; WP_000403039.1; NZ_VEHB01000002.1.
DR   AlphaFoldDB; B7H6Q5; -.
DR   SMR; B7H6Q5; -.
DR   EnsemblBacteria; ACK63708; ACK63708; BCB4264_A4020.
DR   KEGG; bcb:BCB4264_A4020; -.
DR   HOGENOM; CLU_022249_1_0_9; -.
DR   OMA; TTGHQLN; -.
DR   Proteomes; UP000007096; 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_0000378212"
FT   COILED          248..268
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   538 AA;  62704 MW;  7A97B06DFFC2CC16 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 VHIFMEIDNE RVLLEDQQGK
     FVGKDGAHSF SYEELIEEME RNPARFSNNV VTRPLMQEYV FPTLAFIGGP GELAYWSELQ
     QVFHTVGFQM PPVVPRLTIT YVERDIATDL FDLQLRESDP FLNDVDKLRE NWLSNQIEEP
     IDDHFEKAKK EIADIHTSLQ RFVKKIEPGL GAFAGKNELK INEQIELLER MLKRNVEKKY
     EVQLNKFRRI QFALRPLGAP QERVWNVCYY LNQFGLDFVD RVMENSFSWD GKHHVIKL