ID   BSHC_STAHJ              Reviewed;         537 AA.
AC   Q4L5M8;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 96.
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=SH1738;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(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; AP006716; BAE05047.1; -; Genomic_DNA.
DR   RefSeq; WP_011276023.1; NC_007168.1.
DR   AlphaFoldDB; Q4L5M8; -.
DR   SMR; Q4L5M8; -.
DR   STRING; 279808.SH1738; -.
DR   EnsemblBacteria; BAE05047; BAE05047; SH1738.
DR   GeneID; 58062072; -.
DR   KEGG; sha:SH1738; -.
DR   eggNOG; COG4365; Bacteria.
DR   HOGENOM; CLU_022249_1_0_9; -.
DR   OMA; TTGHQLN; -.
DR   OrthoDB; 295429at2; -.
DR   Proteomes; UP000000543; 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..537
FT                   /note="Putative cysteine ligase BshC"
FT                   /id="PRO_0000378269"
FT   COILED          383..451
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   537 AA;  62913 MW;  655A724C46268A35 CRC64;
     MDCRVTHFKE KDSFISKLKE SDKSLLEFYQ YNPVETASFT TKMKRPNNGR EKQLAQIIKD
     YMADLKLTTS QLEHIEALEQ GAKVVIGGQQ AGLFGGPLYT FHKILSIVTL SSQLTKEYGE
     TVVPVFWIAG EDHDFDEVNH TYVYNAKEAQ LKKVKYHTMT PPETNVSRYT PDKEAMLNAL
     NLFFEELKET NHSKPLYKLC VDIINEFDTW TDIFKALLHA VFKEHGVLLI DAQNDKLRQL
     EKPLLKQIVT NHSKINQVFR QTQEQTIASG LTQMIQTDTN VHLFLHEDGM RQLISKEDNL
     FKLSKSDITY SEEELIELIE TEPERFSNNV VTRPVMEEWL FNTVAFIGGP SEIKYWAELN
     NVFKLLNVEM PIVLPRMKMT YMMERTQKLL KQYSLNVEKV IQNGIDDDKN EFVREKASDT
     FIQQVEELKA KHENVYQQLL NEVKENQDNF NLVTKNEEIH NKQFDYLLKR YLLNIEREND
     ISMRQFRELD LVLHPHHGLQ ERIWNPLQIM NDFGIDVFSP STFPPLEYTF DQIIIKP