BSHC_BACC3
ID BSHC_BACC3 Reviewed; 538 AA.
AC C1EPT3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 57.
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=BCA_4023;
OS Bacillus cereus (strain 03BB102).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=572264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03BB102;
RA Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C.,
RA Tapia R., Han C., Sutton G., Sims D.;
RT "Genome sequence of Bacillus cereus 03BB102.";
RL Submitted (FEB-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}.
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DR EMBL; CP001407; ACO30334.1; -; Genomic_DNA.
DR RefSeq; WP_000403058.1; NZ_CP009318.1.
DR AlphaFoldDB; C1EPT3; -.
DR SMR; C1EPT3; -.
DR EnsemblBacteria; ACO30334; ACO30334; BCA_4023.
DR KEGG; bcx:BCA_4023; -.
DR PATRIC; fig|572264.18.peg.3976; -.
DR OMA; TTGHQLN; -.
DR Proteomes; UP000002210; 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_1000188716"
FT COILED 460..484
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ SEQUENCE 538 AA; 62931 MW; DD9B51833AC8E7EC 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 YKEVQEGLHN QQEVIKELGY KPIIETKSNA VHIFMEIDNE RVLLEDNQGK
FVGKDGTYSF SYEELIEEME RSPERFSNNV VTRPLMQEYV FPTLAFIGGP GELAYWSELQ
QVFHTIGFRM PPVVPRITIT YIERDIATDL HDLQLQERDP FLNNVDKLRE NWLSNQIEEP
IDDRFVEAKK EIMNIHTSLQ QFVKEIDPGL SAFAGKNEFK INEQIELLER MLKRNVEKKH
EVELNKFRRI QFALRPLGAP QERVWNVCYY LNQFGLDFVD HVMEKTFSWN GKHHVIKL