BSHC_STAAR
ID BSHC_STAAR Reviewed; 537 AA.
AC Q6GHQ8;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=SAR1153;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX571856; CAG40155.1; -; Genomic_DNA.
DR RefSeq; WP_000340456.1; NC_002952.2.
DR AlphaFoldDB; Q6GHQ8; -.
DR SMR; Q6GHQ8; -.
DR KEGG; sar:SAR1153; -.
DR HOGENOM; CLU_022249_0_0_9; -.
DR OMA; TTGHQLN; -.
DR OrthoDB; 295429at2; -.
DR Proteomes; UP000000596; 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_0000378256"
FT COILED 422..450
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ SEQUENCE 537 AA; 62956 MW; 6CB5C25F8ADCC5E6 CRC64;
MDCKVVSLNE KDQFIPKIKS SDPVITGLFQ YDAAQQISFE KRMSKENNGR EAALANVIRE
YMNDLKLSSE QELNIQHLAN GSKVVIGGQQ AGLFGGPLYT FHKIFSIITL SKELTDTHKQ
QVVPVFWIAG EDHDFDEVNH TFVYNENHGS LHKVKYHTME MPETTVSRYY PDKAELKQTL
KTMFIHMKET VHTQGLLEIC DRIIDQYDSW TDMFKALLHE TFKAYGVLFI DAQFEPLRKM
EAPMFKKILK KHQLLDDAFR ATQKRTQNQG LKAMIQTDTN VHLFLHDENM RQLVSYDGKH
FRLNKTDKKY IKEEIINIAE NQPELFSNNV VTRPLMEEWL FNTVAFIGGP SEIKYWAELK
DVFELFDVEM PIVMPRLRIT YLNDRIEKLL SKYNIPLEKV LVDGVEGERS KFIREQASDQ
FIEKVEGMIE QQRRLYQDLL DEVAGNQNNI NLVNKNNEIH IQQYDYLLKR YLLNIEREND
ISMKQFREIQ ETLHPMGGLQ ERIWNPLQIL NDFGTDVFKP STYPPLSYTF DHIIIKP