ID   BSHC_STAAS              Reviewed;         537 AA.
AC   Q6GA35;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
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}; OrderedLocusNames=SAS1111;
OS   Staphylococcus aureus (strain MSSA476).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSSA476;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG42888.1; -; Genomic_DNA.
DR   RefSeq; WP_000340475.1; NC_002953.3.
DR   AlphaFoldDB; Q6GA35; -.
DR   SMR; Q6GA35; -.
DR   KEGG; sas:SAS1111; -.
DR   HOGENOM; CLU_022249_0_0_9; -.
DR   OMA; TTGHQLN; -.
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_0000378257"
FT   COILED          422..450
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   537 AA;  62807 MW;  7D79964314F46AA4 CRC64;
     MDCKVVSLNE KDQFIPKIKS SDPVITGLFQ YDAAQQTSFE KRMSKENNGR EAALANVIRE
     YMSDLKLSSE QELNIQHLAN GSKVVIGGQQ AGLFGGPLYT FHKIFSIITL SKELTDTHKQ
     QVVPVFWIAG EDHDFDEVNH TFVYNENHGS LHKVKYHTME MPETTVSRYY PDKAELKQTL
     KTMFIHMKET VHTQGLLEIC DRIIDQYDSW TDMFKALLHE TFKAYGVLFI DAQFEPLRKM
     EAPMFKKILK KHQLLDDAFR ATQQRTQNQG LNAMIQTDTN VHLFLHDENM RQLVSYDGKH
     FKLNKTDKTY IKEEIINIAE NQPELFSNNV VTRPLMEEWL FNTVAFVGGP SEIKYWAELK
     DVFELFDVEM PIVMPRLRIT YLNDRIEKLL SKYNIPLEKV LVDGVEGERS KFIREQASHQ
     FIEKVEGMIE QQRRLNKDLL DEVAGNQNNI NLVNKNNEIH IQQYDYLLKR YLLNIEREND
     ISMKQFREIQ ETLHPMGGLQ ERIWNPLQIL NDFGTDVFKP STYPPLSYTF DHIIIKP