ID   BSHC_OCEIH              Reviewed;         543 AA.
AC   Q8ER55;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 85.
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=OB1460;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13416.1; -; Genomic_DNA.
DR   RefSeq; WP_011065861.1; NC_004193.1.
DR   AlphaFoldDB; Q8ER55; -.
DR   SMR; Q8ER55; -.
DR   STRING; 221109.22777142; -.
DR   EnsemblBacteria; BAC13416; BAC13416; BAC13416.
DR   KEGG; oih:OB1460; -.
DR   eggNOG; COG4365; Bacteria.
DR   HOGENOM; CLU_022249_1_0_9; -.
DR   OMA; TTGHQLN; -.
DR   OrthoDB; 295429at2; -.
DR   PhylomeDB; Q8ER55; -.
DR   Proteomes; UP000000822; 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..543
FT                   /note="Putative cysteine ligase BshC"
FT                   /id="PRO_0000378245"
FT   COILED          419..440
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ   SEQUENCE   543 AA;  62829 MW;  808E4E36FE5AE67C CRC64;
     MKTTPLSIQT TNKLVTNYKN NDASVMKYFD YSSIHYEQER LAYLNNRTYK RQDFVKAVHK
     LHKKWGAPEA SMEKLNKLVD EQAVAVVGGQ QAGLLSGPLY SIHKVISVIQ LAKEQEKKLG
     IPVVPIFWIA GEDHDFDEIN HTYVPTTDMK MKKVKLQNKS IDAGRKSVTD LEFEKDKLRE
     WVEDVFLSLK ETDYTQDIHS LVQTVLSESD SYSEFFAKFI FQLFPDQGIV LLDSHASEIR
     EIETDFFLEM IEHQQGISSA VKSTIDELKA EEYSISLDAL DGDAHLFYHD EQLGRVLLQV
     DPDGMWVDKQ HNMRFTVEEL RSIAINSPHL LSNNVITRPM MQEKLIPTLA FVGGPGEIAY
     WSALKDSFHL LELKMPPIVP RISFTYIDRY TSRLLDKYNL NVSEIISTGV NDHKRRFLDE
     KNNDNIDEVV EEVKAQISDI HKPLRDISAS MGDDIKALSE SNLSYILNDV EFLRKRLNNE
     IRKTYAKEIS EFDRMEMILR PNNGLQERIW NPIYIMNCCG VDVFTEMVNN HTFVQEEHWI
     IHL