BSHC_HELMI
ID BSHC_HELMI Reviewed; 547 AA.
AC B0TAU6;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 61.
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=Helmi_24320;
GN ORFNames=HM1_2509;
OS Heliobacterium modesticaldum (strain ATCC 51547 / Ice1).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Heliobacteriaceae;
OC Heliomicrobium.
OX NCBI_TaxID=498761;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51547 / Ice1;
RX PubMed=18441057; DOI=10.1128/jb.00299-08;
RA Sattley W.M., Madigan M.T., Swingley W.D., Cheung P.C., Clocksin K.M.,
RA Conrad A.L., Dejesa L.C., Honchak B.M., Jung D.O., Karbach L.E.,
RA Kurdoglu A., Lahiri S., Mastrian S.D., Page L.E., Taylor H.L., Wang Z.T.,
RA Raymond J., Chen M., Blankenship R.E., Touchman J.W.;
RT "The genome of Heliobacterium modesticaldum, a phototrophic representative
RT of the Firmicutes containing the simplest photosynthetic apparatus.";
RL J. Bacteriol. 190:4687-4696(2008).
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; CP000930; ABZ85057.1; -; Genomic_DNA.
DR RefSeq; WP_012283553.1; NC_010337.2.
DR AlphaFoldDB; B0TAU6; -.
DR SMR; B0TAU6; -.
DR STRING; 498761.HM1_2509; -.
DR EnsemblBacteria; ABZ85057; ABZ85057; HM1_2509.
DR KEGG; hmo:HM1_2509; -.
DR eggNOG; COG4365; Bacteria.
DR HOGENOM; CLU_022249_1_0_9; -.
DR OMA; TTGHQLN; -.
DR Proteomes; UP000008550; 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..547
FT /note="Putative cysteine ligase BshC"
FT /id="PRO_0000378241"
FT COILED 462..484
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ SEQUENCE 547 AA; 61944 MW; E7FEE0B61381FCD9 CRC64;
MSFERTGSIF SGLAGAYVQR EAHVVSLFPY AFPDENALAL RARRMTATDS YPRSELSSLL
EGYQRRLADL AGLEGSSNRA ADQARRLAEA NSLAVVTGQQ AGLFTGPLYT IYKAVTCINL
AKRLEAKTGQ PVIPVFWVAS EDHDFEEISH IKLLQGEKTV VITMTSRPDE DRFAIGHRTL
PEDLAVTLES FLSHLPQSEH RLPWEETWHR LLTGPTGPHE HFAALLHKLL GPYGLVILDP
LLSGLKQLPR CASFFASVLE NEVSLREGLS RGVEQIRRLG YTPQVEKGPE ETSLFYFHQG
RRLAILRDGR GYRLRGAEIT FSRDELLDLA QRQPDLFSTN VVTRPLLQDQ LLPTTAYVAG
PGEIAYFAAY RDVYRAMGME MPPIVPRLSV TIIEGFVDKL LERYALSFAD VPAGLEGRLR
EELAAQDELG IGALFEELES QVRAAYLPAV ERIARWDRQM GNLAEENLDR VIAQARFLRQ
KVEHRHRQRC QDKRNHFRKV ELHLWPGAPQ ERVYNIFPYL LKYGSSLIET LLEAPVEWLD
SHCLFRC