BSHC_BACCQ
ID BSHC_BACCQ Reviewed; 538 AA.
AC B9IVZ6;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=BCQ_3705;
OS Bacillus cereus (strain Q1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=361100;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Q1;
RX PubMed=19060151; DOI=10.1128/jb.01629-08;
RA Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X.,
RA Xue Y., Zhu Y., Jin Q.;
RT "Complete genome sequence of the extremophilic Bacillus cereus strain Q1
RT with industrial applications.";
RL J. Bacteriol. 191:1120-1121(2009).
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; CP000227; ACM14133.1; -; Genomic_DNA.
DR RefSeq; WP_000403033.1; NC_011969.1.
DR AlphaFoldDB; B9IVZ6; -.
DR SMR; B9IVZ6; -.
DR EnsemblBacteria; ACM14133; ACM14133; BCQ_3705.
DR KEGG; bcq:BCQ_3705; -.
DR HOGENOM; CLU_022249_1_0_9; -.
DR OMA; TTGHQLN; -.
DR Proteomes; UP000000441; 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_0000378214"
FT COILED 460..485
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ SEQUENCE 538 AA; 62931 MW; CF1AFAEE2A7C6898 CRC64;
MEIKEISVPQ QGVVADYMNG EKEIQSCFDY MLTEDAFKQR VQDLREREFF RQDLVAHLLE
YNTKLQAGEA TIQNVKALED EDTYVVIAGQ QAGLLTGPLY TIHKIISVLQ LAKEKEESLG
VKVVPVFWIA GEDHDMDEIN HTFVTKNKKI KKTIFHDRNP KKASASESEL SLEDCRKWIE
EIFKTYPETN FTKDVLRFID DSLGKSNTYV DFFGHLIMKM FINSGLILVD SHHPELRKLE
VPFFKQIVSK YKEVQEGLHN QQEVIKELGY KPIIETKSNA VHIFMEIDNE RVLLEDNQGK
FVGKDGTYSF SYEELIEEME RSPERFSNNV VTRPLMQEYV FPTLAFIGGP GELAYWSELQ
QVFHTIGFRM PPVVPRITIT YIERDIATDL HDLQLQESDP FLNNVDKLRE NWLSNQIEEP
IDERFVEAKK EIIDIHKSLQ QFVKKIDPGL SSFAGKNEFK INEQIELLER MLKRNIEKKH
EVELNKFRRI QFAIRPLGAP QERVWNVCYY LNQFGLDFVD RVMEKPFSWN GKHHVIKL