BSHC_BACC7
ID BSHC_BACC7 Reviewed; 538 AA.
AC B7HM40;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 51.
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=BCAH187_A3972;
OS Bacillus cereus (strain AH187).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
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}.
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DR EMBL; CP001177; ACJ80831.1; -; Genomic_DNA.
DR RefSeq; WP_000403053.1; NC_011658.1.
DR AlphaFoldDB; B7HM40; -.
DR SMR; B7HM40; -.
DR EnsemblBacteria; ACJ80831; ACJ80831; BCAH187_A3972.
DR KEGG; bcr:BCAH187_A3972; -.
DR HOGENOM; CLU_022249_1_0_9; -.
DR OMA; TTGHQLN; -.
DR OrthoDB; 295429at2; -.
DR Proteomes; UP000002214; 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_0000378208"
FT COILED 460..484
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ SEQUENCE 538 AA; 63133 MW; A44AEF472952EE55 CRC64;
MEIKEISVPQ QGVVADYMNG KKEIQSCFDY MLTEDAFKQR VQDLREREFF RQDLVAHLLE
YNTKLQAGEA TIQNVKALED EDTYVVIAGQ QAGLLTGPLY TIHKIISVLQ LAKEKEESLG
VKVVPVFWIA GEDHDMDEIN HTFVTKNKKI KKTIFHDRNP KKASASESEL SLEDCRKWIE
EIFKTYPETN FTKDVLRFID DSLRKSNTYV DFFGHLIMKM FMNSGLILVD SHHPELRKLE
VPFFKQIVSK YKEVQEGLHN QQEVIKELGY KPIIETKSNA VHIFMEIDNE RVLLEDNQRK
FVGKDGTYSF SYEELIEEME RSPERFSNNV VTRPLMQEYV FPTLAFIGGP GELAYWSELQ
QVFHAIGFRM PPVVPRITIT YIERDIATDL HDLQLQESDP FLNNVDKLRE NWLSNQIEEP
IDERFEEAKK EIIDIHKSLQ QFVKKIDPGL SSFAGKNEFK INEQIELLER MLKRNVEKKH
EVELNKFRRI QFAIRPLGAP QERVWNVCYY LNQFGLDFVD RVMEKPFSWD GKHHVIKL