ID   BSHC_STAA8              Reviewed;         540 AA.
AC   Q2FZ98; Q2FZ99; Q2FZA0;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   25-MAY-2022, entry version 79.
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};
GN   OrderedLocusNames=SAOUHSC_01139/SAOUHSC_01140/SAOUHSC_01141;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABD30249.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=ABD30250.1; Type=Miscellaneous discrepancy; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC       Sequence=ABD30251.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP000253; ABD30249.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CP000253; ABD30250.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP000253; ABD30251.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; YP_499681.1; NC_007795.1.
DR   RefSeq; YP_499683.1; NC_007795.1.
DR   AlphaFoldDB; Q2FZ98; -.
DR   SMR; Q2FZ98; -.
DR   STRING; 1280.SAXN108_1175; -.
DR   EnsemblBacteria; ABD30249; ABD30249; SAOUHSC_01139.
DR   EnsemblBacteria; ABD30250; ABD30250; SAOUHSC_01140.
DR   EnsemblBacteria; ABD30251; ABD30251; SAOUHSC_01141.
DR   GeneID; 3920699; -.
DR   GeneID; 3920701; -.
DR   KEGG; sao:SAOUHSC_01139; -.
DR   KEGG; sao:SAOUHSC_01141; -.
DR   PATRIC; fig|93061.5.peg.1045; -.
DR   eggNOG; COG4365; Bacteria.
DR   HOGENOM; CLU_2669235_0_0_9; -.
DR   Proteomes; UP000008816; 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_0000378262"
FT   COILED          425..453
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   540 AA;  63135 MW;  3565120ABC3586C3 CRC64;
     MDCKVVSLNE KDQFIPKIKS SDPVITGLFQ YDAAQQTSFE KRMSKENNGR EAALANVIRE
     YMSDLKLSKL SSEQELNIQH LANGSKVVIG GQQAGLFGGP LYTFHKIFSI ITLSKELTDT
     HKQQVVPVFW IAGEDHDFDE VNHTFVYNEN HGSLHKVKYH TMEMPETTVS RYYPDKAELK
     QTLKTMFIHM KETVHTQGLL EICDRIIDQY DSWTDMFKAL LHETFKAYGV LFIDAQFEPL
     RKMEAPMFKK ILKKHQLLDD AFRATQQRTQ NQGLNAMIQT DTNVHLFLHD ENMRQLVSYD
     GKHFKLNKTD KTYIKEEIIN IAENQPELFS NNVVTRPLME EWLFNTVAFV GGPSEIKYWA
     ELKDVFELFD VEMPIVMPRL RITYLNDRIE KLLSKYNIPL EKVLVDGVEG ERSKFIREQA
     SHQFIEKVEG MIEQQRRLNK DLLDEVAGNQ NNINLVNKNN EIHIQQYDYL LKRYLLNIER
     ENDISMKQFR EIQETLHPMG GLQERIWNPL QILNDFGTDV FKPSTYPPLS YTFDHIIIKP