ID   BSHC_DESRM              Reviewed;         540 AA.
AC   A4J3Q5;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=Dred_1174;
OS   Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS   (Desulfotomaculum reducens).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=349161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1160 / DSM 100696 / MI-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT   "Complete sequence of Desulfotomaculum reducens MI-1.";
RL   Submitted (MAR-2007) 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; CP000612; ABO49708.1; -; Genomic_DNA.
DR   RefSeq; WP_011877534.1; NC_009253.1.
DR   AlphaFoldDB; A4J3Q5; -.
DR   SMR; A4J3Q5; -.
DR   STRING; 349161.Dred_1174; -.
DR   EnsemblBacteria; ABO49708; ABO49708; Dred_1174.
DR   KEGG; drm:Dred_1174; -.
DR   eggNOG; COG4365; Bacteria.
DR   HOGENOM; CLU_022249_1_0_9; -.
DR   OMA; TTGHQLN; -.
DR   OrthoDB; 295429at2; -.
DR   Proteomes; UP000001556; 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..540
FT                   /note="Putative cysteine ligase BshC"
FT                   /id="PRO_0000378234"
FT   COILED          455..491
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   540 AA;  62052 MW;  79709DD4D9FF1F6F CRC64;
     MRIEYVDSFY SQPFPGTYMR DFGQVKHFFE YNPHQLQEYK TRCEHELALP KEHLVALAEN
     LKDFNQGLGC GEKTLHNIEL LDQGKALTVV TGQQPGILTG PLYTIYKAMG TIGLAEKLSK
     ELNRKVIPVF WIGADDHDHE EINHIFIPTA KGPKRITLAG KPAGRISVGN IPIPDIALLL
     EELEDLLPPI GWKNQGIELI KRTAHEAANL AEWFGKLMTF LFKDYGLVFI NPVLPQVRAI
     TASLFYKVVT TAPAVNQLLQ ASCQQMLGCG YTPQVQGEKD KLHLFWYNEH GYREALYYKK
     GLISNKDGTR TWTKGQLGEL CLTNPAKFSP DVVMRPVVQE KLLPVLAYVA GPGEISYYAL
     LKRIFHYFAM KMPVIYPRPN ITVIEPLIKR LITKYQVPLS CLTYGLEEFI ENYLQQEDQL
     GIETVFNELR GTLKEKQGEV VKKLSILDPD IEGMGKENLK RLIRVVNSFE EKVKQRHRKN
     NQVAIQQLQK IQHMTQPMGQ WQERVYNIFP YVMKYGPGII KEMYHLIEIS DWRQKIIFFD