ID   BSHC_CARHZ              Reviewed;         535 AA.
AC   Q3AAW3;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=CHY_1902;
OS   Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS   Z-2901).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Carboxydothermus.
OX   NCBI_TaxID=246194;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX   PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA   Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA   Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA   Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT   "Life in hot carbon monoxide: the complete genome sequence of
RT   Carboxydothermus hydrogenoformans Z-2901.";
RL   PLoS Genet. 1:563-574(2005).
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; CP000141; ABB14445.1; -; Genomic_DNA.
DR   RefSeq; WP_011344794.1; NC_007503.1.
DR   AlphaFoldDB; Q3AAW3; -.
DR   SMR; Q3AAW3; -.
DR   STRING; 246194.CHY_1902; -.
DR   EnsemblBacteria; ABB14445; ABB14445; CHY_1902.
DR   KEGG; chy:CHY_1902; -.
DR   eggNOG; COG4365; Bacteria.
DR   HOGENOM; CLU_022249_1_0_9; -.
DR   OMA; TTGHQLN; -.
DR   OrthoDB; 295429at2; -.
DR   Proteomes; UP000002706; 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; Reference proteome.
FT   CHAIN           1..535
FT                   /note="Putative cysteine ligase BshC"
FT                   /id="PRO_0000378224"
FT   COILED          420..477
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   535 AA;  62432 MW;  9FD12B104F6188F3 CRC64;
     MRYEEINLGY EKNLVRYYLT GYDRVAKFYH YNPWNTRSFY DRADYLKDKS NPEALYNLLS
     FYLKDFALDQ KVVENLDKIK KGAFIVLTGQ QPGFLTGPLY TIYKAVHAII EAKRLSELLN
     HEVVPLFWIG SEDHDVEEVN FLYFPGKEGP QEIKIEFTDL RKIPAGLRPA EPETVEAIEK
     FEGLLPNFDY KEEVFTEIKK AYHSANLGQA FARLMLKLFG KFGLLVYDGL NPEFKRVTKG
     YLKNAFLKRD AIEKALFKVY TEQQSLGIEP QLDPCPNHCN MFIFKNDERI ALEVAGEKVV
     SRDGEVSFTR EEFLEFMERY PEKLSPNLVV RTSIQSLVFP VLAYVAGPGE IGYYGMLKEV
     YEIMGTQMPV ILPRFTATLI EPRVEKALKE FALLPQEIYQ DYDGVFHRVL ERLDNLGIDD
     TFKALKESIN SAYKNLQEKL APLGADFQKL TGENLGRVMA QVKYLEERAQ KYHREKNSKY
     IEKLWYLKTN FLPENEWQER VYNVFYYLAK YGFALIEKLL GIPFNPGKHY LLYLE