ID   BSHC_BACAA              Reviewed;         538 AA.
AC   C3P689;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 48.
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=BAA_4084;
OS   Bacillus anthracis (strain A0248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=592021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A0248;
RA   Dodson R.J., Munk A.C., Bruce D., Detter C., Tapia R., Sutton G., Sims D.,
RA   Brettin T.;
RT   "Genome sequence of Bacillus anthracis A0248.";
RL   Submitted (APR-2009) 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; CP001598; ACQ48905.1; -; Genomic_DNA.
DR   RefSeq; WP_000403057.1; NC_012659.1.
DR   AlphaFoldDB; C3P689; -.
DR   SMR; C3P689; -.
DR   GeneID; 45023748; -.
DR   KEGG; bai:BAA_4084; -.
DR   HOGENOM; CLU_022249_1_0_9; -.
DR   OMA; TTGHQLN; -.
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_1000188714"
FT   COILED          460..484
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   538 AA;  62974 MW;  9D5C31E2796D6590 CRC64;
     MEIKEISVPQ QGVVADYMNG KKEIQSCFDY MLTEDAFKQR VQDLREREFF RQDLVTHLLE
     YNTKLQAGEA TIQNVKALGD ENTYVVIAGQ QAGLLTGPLY TIHKIISVLQ LAKEKEESLG
     VKVVPVFWIA GEDHDMDEIN HTFVTKNKKI KKTIFHDRNP KKASASESEL SLEDCRKWIE
     EIFKTYPETN FTKDVLQFID DSLRKSNTYV DFFGHLIMKM FVNSGLILVD SHHPELRKLE
     VPFFKQIVSK YKEVQEGLHN QQRVIKELGY KPIIETKSNA VHIFMEIDNE RVLLEDNQGK
     FVGKDGTYSF SYKELIEEME RSPERFSNNV VTRPLMQEYV FPTLAFIGGP GELAYWSELQ
     QVFHTIGFRM PPVVPRITIT YIERDIATDL HDLQLQESDP FFNNVDKLRE NWLSNQIEEP
     IDERFVEAKK EIIDIHKSLQ QFVKKIDPGL SAFAGKNEFK INEQIELLER MLKRNVEKKH
     EVELNKFRRI QFALRPLGAP QERVWNVCYY LNQFGLDFVD RVMEKPFSWN GKHHVIKL