ID   BSHC_GEOSW              Reviewed;         542 AA.
AC   C5D8L4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 53.
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=GWCH70_1011;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) 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; CP001638; ACS23871.1; -; Genomic_DNA.
DR   RefSeq; WP_015863347.1; NC_012793.1.
DR   AlphaFoldDB; C5D8L4; -.
DR   SMR; C5D8L4; -.
DR   STRING; 471223.GWCH70_1011; -.
DR   EnsemblBacteria; ACS23871; ACS23871; GWCH70_1011.
DR   KEGG; gwc:GWCH70_1011; -.
DR   eggNOG; COG4365; Bacteria.
DR   HOGENOM; CLU_022249_1_0_9; -.
DR   OMA; TTGHQLN; -.
DR   OrthoDB; 295429at2; -.
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..542
FT                   /note="Putative cysteine ligase BshC"
FT                   /id="PRO_1000216164"
FT   COILED          458..479
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   542 AA;  62909 MW;  AEBC4BEC26DFABB9 CRC64;
     MEVREISLAA TTPLATDYIN GTFPIEKGFS YSLQAEDVFW RRLDDIKGRA YPRRELVEYL
     RSYHQRFHAS SETFYNIEKL LHPESVVVVG GQQAGLLTGP LYTIYKIISV IKLAKEQERK
     LGVPVVPLFW IAGEDHDIAE VNHVYIAEDG KIKKYVYPDI PQEKRMVSDV PLDHQVCSTW
     ITNIVKTYGE TETTNKLLDF LFQCLDQSKT FVDFFASIVL RLFASEGLVV LNAADVPLRA
     IESSFFTALI ECHREVTDAV LRKQHQLRQL GYKNTLDIQP HCANLFYYDG RQRWLLEHDP
     QKEVFHSKKG EFVFSKDELI QLAKTKPGHL SNNVVTRPLM QEFLLPTLAF VAGPGEIAYW
     AELKEAFSIF GFKMPPVIPR VNITIVERSI QTDLAEIGID IMDVFKGRLE EAKQQWLAQQ
     TRYPLEEMFA KAKAEIEEIH RPLREFGMEI DRGLAGLLTK NATLLQAQID FLHQTLQRAL
     IRKYEVELRK FSRVEMSLMP NQAPQERIWN IFYYINKYGF DFLEKLLQLD YKWNGMHKIV
     YI