BSHC_GEOKA
ID BSHC_GEOKA Reviewed; 542 AA.
AC Q5L0Y5;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=GK1110;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(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; BA000043; BAD75395.1; -; Genomic_DNA.
DR RefSeq; WP_011230610.1; NC_006510.1.
DR AlphaFoldDB; Q5L0Y5; -.
DR SMR; Q5L0Y5; -.
DR STRING; 235909.GK1110; -.
DR EnsemblBacteria; BAD75395; BAD75395; GK1110.
DR KEGG; gka:GK1110; -.
DR eggNOG; COG4365; Bacteria.
DR HOGENOM; CLU_022249_1_0_9; -.
DR OMA; TTGHQLN; -.
DR Proteomes; UP000001172; 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..542
FT /note="Putative cysteine ligase BshC"
FT /id="PRO_0000378238"
FT COILED 458..487
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01867"
SQ SEQUENCE 542 AA; 61270 MW; 973104E6323830FC CRC64;
MEVREIPLPA ATKLAADYIT GAFPAESGFA YAQADDEAFC RRLAYLQGRT YDREGLADYL
RAYHRRFSAS VATMANIEKL RNERSVVIVG GQQAGLLTGP LYTIYKIITI IQLAKEQERK
LGVPVVPLFW IAGEDHDIAE IDHVYVVEEG EVKKAAYPHK TNEKRMAADV LLDRMAAKEW
IERVVKTYGE TDVTNELLFF LSSCLDEART FVDFFAAIVL RLFADHGLVV LNAGDAAVRP
LERRFFAALI ERHRDVTAAV LAQQEALRTL GYAPLIEIGR DAANLFYYDG RERSLLQYDE
ERGLFHNKAG TLVWTREELL ELAETNPARL SNNVVTRPLM QEHLLPTLAF VAGPGEIAYW
AELKEAFPLF DLEMPPVVPR LQATIVSRSL QTDLSDIGLE VADVLTGRLD EAKREWREAT
AQAPLASAFA KAKADIDAAH RPLRELGVAI DRGLEGLVAK NAAILQAQIE FLQHALERAL
LRKHETEWRK FWRIETSLRP NGALQERVWN VFYYINRYGF DFVEKLLAIR SPGNGMHKIV
YM