ID   BSHC_EXIS2              Reviewed;         519 AA.
AC   B1YIU4;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 75.
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=Exig_1968;
OS   Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS   255-15).
OC   Bacteria; Firmicutes; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=262543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA   Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA   Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL   Submitted (APR-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; CP001022; ACB61420.1; -; Genomic_DNA.
DR   RefSeq; WP_012370838.1; NC_010556.1.
DR   AlphaFoldDB; B1YIU4; -.
DR   SMR; B1YIU4; -.
DR   STRING; 262543.Exig_1968; -.
DR   EnsemblBacteria; ACB61420; ACB61420; Exig_1968.
DR   KEGG; esi:Exig_1968; -.
DR   eggNOG; COG4365; Bacteria.
DR   HOGENOM; CLU_022249_1_0_9; -.
DR   OMA; TTGHQLN; -.
DR   OrthoDB; 295429at2; -.
DR   Proteomes; UP000001681; 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..519
FT                   /note="Putative cysteine ligase BshC"
FT                   /id="PRO_0000378235"
FT   COILED          51..71
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
FT   COILED          440..464
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   519 AA;  59678 MW;  F4AF5CAA1E0A8498 CRC64;
     MKVQSFDALY DEDSLMQKAS RQEFSKYVDH IGTEGMQARS GLLQERQYPH LNALVDELMR
     QNPRLNDSLK ERLELLRTGE AQVVITGQQT GIFGGPMYAV YKLLTCLKVA RQTEELLNRP
     VLPIFWLATE DHDFDEINHL IVPTHDFRTR KLAIQAPDSI SRSVSRLAFD QTAVKDIVRQ
     ALCTERETPY TKELLALSDR LIESSTTYGE FFASFMGELV DHDIIFFDAD TEAVRQLEIP
     FFERLIQDNA EIRQALSKGI QETTELPDTF LNEEAAHLFV EDIGRDLLYP GQDFVTKQGK
     TYTELELLAL LYASPERFSN SVVTRPLMQD YLFPTLAYIG GPGEIAYWTR LRPLFHHFDW
     TMPVLIPRMG AVMLQARDEK GLRRHGLSLE QVLHTGVPLT PFDAAAIKRH LHDATLLGTV
     LVEEVTRIEQ QELRTTAVAT KLNKQLQLAV ETIVDQKRRL HEQANRSDRA LQYQLAPDHA
     PQERIHSILP WLNRYGLNLV QTLRMHYEQT EAEQLKIML