CYSL_BACSU
ID CYSL_BACSU Reviewed; 299 AA.
AC P39647;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=HTH-type transcriptional regulator CysL;
DE AltName: Full=CysJI operon transcriptional activator;
GN Name=cysL; Synonyms=ywfK; OrderedLocusNames=BSU37650; ORFNames=ipa-89d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP FUNCTION AS A REPRESSOR OF SULFUR ASSIMILATION, DISRUPTION PHENOTYPE, AND
RP INDUCTION.
RC STRAIN=168;
RX PubMed=12169591; DOI=10.1128/jb.184.17.4681-4689.2002;
RA Guillouard I., Auger S., Hullo M.-F., Chetouani F., Danchin A.,
RA Martin-Verstraete I.;
RT "Identification of Bacillus subtilis CysL, a regulator of the cysJI operon,
RT which encodes sulfite reductase.";
RL J. Bacteriol. 184:4681-4689(2002).
CC -!- FUNCTION: Transcriptional activator of the cysJI operon which is
CC involved in sulfur assimilation. Also negatively regulates its own
CC transcription. {ECO:0000269|PubMed:12169591}.
CC -!- INDUCTION: Negatively autoregulated. {ECO:0000269|PubMed:12169591}.
CC -!- DISRUPTION PHENOTYPE: Cannot grow on sulfate, sulfite or
CC butanesulfonate as sole sulfur source. {ECO:0000269|PubMed:12169591}.
CC -!- SIMILARITY: Belongs to the LysR transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; X73124; CAA51645.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15792.1; -; Genomic_DNA.
DR PIR; S39744; S39744.
DR RefSeq; NP_391645.1; NC_000964.3.
DR RefSeq; WP_003243173.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P39647; -.
DR SMR; P39647; -.
DR STRING; 224308.BSU37650; -.
DR PaxDb; P39647; -.
DR PRIDE; P39647; -.
DR DNASU; 936502; -.
DR EnsemblBacteria; CAB15792; CAB15792; BSU_37650.
DR GeneID; 936502; -.
DR KEGG; bsu:BSU37650; -.
DR PATRIC; fig|224308.179.peg.4077; -.
DR eggNOG; COG0583; Bacteria.
DR InParanoid; P39647; -.
DR OMA; IEGPCHH; -.
DR PhylomeDB; P39647; -.
DR BioCyc; BSUB:BSU37650-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005119; LysR_subst-bd.
DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00126; HTH_1; 1.
DR Pfam; PF03466; LysR_substrate; 1.
DR PRINTS; PR00039; HTHLYSR.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS50931; HTH_LYSR; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..299
FT /note="HTH-type transcriptional regulator CysL"
FT /id="PRO_0000105824"
FT DOMAIN 1..58
FT /note="HTH lysR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
FT DNA_BIND 18..37
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00253"
SQ SEQUENCE 299 AA; 34190 MW; 7E888CABB588F6FC CRC64;
MYYDVLKTFI AVVEEKNFTK AAEKLMISQP SVSLHIKNLE KEFQTALLNR SPKHFTTTPT
GDILYQRAKQ MVFLYEQAKA EIYAHHHYVK GELKIAASFT IGEYILPPLL AQLQKLYPEL
NLDVMIGNTE EVSERVRMLQ ADIGLIEGHT NENELEIEPF MEDEMCIAAP NQHPLAGRKE
ISISDLQNEA WVTREKGSGT REYLDHVLSS NGLRPKSMFT ISSNQGVKEA VINGMGLSVL
SRSVLRKDLI HREISILHIN NFSLKRKLSY IHSPLMENTK NKEIFITMLK SNYQSQLLK