ID   BSHC_BACVZ              Reviewed;         539 AA.
AC   A7Z4D5;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-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=RBAM_014980;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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; CP000560; ABS73861.1; -; Genomic_DNA.
DR   RefSeq; WP_012117499.1; NC_009725.2.
DR   AlphaFoldDB; A7Z4D5; -.
DR   SMR; A7Z4D5; -.
DR   STRING; 326423.RBAM_014980; -.
DR   EnsemblBacteria; ABS73861; ABS73861; RBAM_014980.
DR   KEGG; bay:RBAM_014980; -.
DR   HOGENOM; CLU_022249_1_0_9; -.
DR   OMA; TTGHQLN; -.
DR   Proteomes; UP000001120; 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..539
FT                   /note="Putative cysteine ligase BshC"
FT                   /id="PRO_0000378206"
FT   COILED          455..475
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   539 AA;  62585 MW;  84B25A8893B415D7 CRC64;
     MQLTELSIKS QNKFVQHYID GENMSSFFDY DIHSEDVWQK RLHDLSSQPF AREELADYLS
     SYHEKFHSAA MQASIEKLRD PKSAAVVGGQ QAGLLTGPLY TIHKIISIIV LARQQEEALQ
     IPVVPIFWVA GEDHDLEEIN FVHTSTENKG PVKQKLPQSY WKKTSAAKTE LDQEKCAAWI
     DEVFAAFEET DHTNTLLQNV KRCLRSSETF TDFFELLIAD LFQEEGLILM NSGDPGIKKL
     ETGMFQQILK HNHELAKAVS DQQRLMREAG YHPIIESDKD QANLFYEHEG ERFLIEKENG
     VFVIKELDLK WTNDELHTHM EEKPECFSNN VVTRPLMQEF LIPTLAFIAG PGEINYWGEL
     KRAFSLMGFR MTPVVPRLNI TILERHIEKK LSERNIPLQE AIEHGTGHLK DTYFEEQIPE
     EFSSVMEQAK SQIEAVHKRA RDEALKVDSS LEPLLQKNAA FIQDQLLFLE RTVTKRIEEK
     EGFVLRDYER IQNSIRPLGA PQERIWNVMY YLNRYGPKFF TTFKHLPFSF QNQHQIVKL