(data stored in SCRATCH zone)

SWISSPROT: SINR_BACSU

ID   SINR_BACSU              Reviewed;         111 AA.
AC   P06533;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   11-DEC-2019, entry version 160.
DE   RecName: Full=HTH-type transcriptional regulator SinR;
GN   Name=sinR; Synonyms=flaD, sin; OrderedLocusNames=BSU24610;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3096962; DOI=10.1128/jb.168.2.860-869.1986;
RA   Gaur N.K., Dubnau E., Smith I.;
RT   "Characterization of a cloned Bacillus subtilis gene that inhibits
RT   sporulation in multiple copies.";
RL   J. Bacteriol. 168:860-869(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
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   [4]
RP   FUNCTION.
RX   PubMed=1898931; DOI=10.1128/jb.173.2.678-686.1991;
RA   Gaur N.K., Oppenheim J., Smith I.;
RT   "The Bacillus subtilis sin gene, a regulator of alternate developmental
RT   processes, codes for a DNA-binding protein.";
RL   J. Bacteriol. 173:678-686(1991).
RN   [5]
RP   FUNCTION.
RX   PubMed=7642487; DOI=10.1128/jb.177.16.4619-4627.1995;
RA   Mandic-Mulec I., Doukhan L., Smith I.;
RT   "The Bacillus subtilis SinR protein is a repressor of the key sporulation
RT   gene spo0A.";
RL   J. Bacteriol. 177:4619-4627(1995).
RN   [6]
RP   INTERACTION WITH HPR.
RX   PubMed=15104138; DOI=10.1023/b:bile.0000018259.66762.ed;
RA   Sanchez A., Olmos J.;
RT   "Bacillus subtilis transcriptional regulators interaction.";
RL   Biotechnol. Lett. 26:403-407(2004).
RN   [7]
RP   FUNCTION.
RC   STRAIN=168, and 3610;
RX   PubMed=15661000; DOI=10.1111/j.1365-2958.2004.04440.x;
RA   Kearns D.B., Chu F., Branda S.S., Kolter R., Losick R.;
RT   "A master regulator for biofilm formation by Bacillus subtilis.";
RL   Mol. Microbiol. 55:739-749(2005).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH HPR.
RC   STRAIN=168;
RX   PubMed=16923912; DOI=10.1128/jb.00427-06;
RA   Kodgire P., Dixit M., Rao K.K.;
RT   "ScoC and SinR negatively regulate epr by corepression in Bacillus
RT   subtilis.";
RL   J. Bacteriol. 188:6425-6428(2006).
RN   [9]
RP   REPRESSOR OF LUTABC OPERON.
RC   STRAIN=3610;
RX   PubMed=19201793; DOI=10.1128/jb.01464-08;
RA   Chai Y., Kolter R., Losick R.;
RT   "A widely conserved gene cluster required for lactate utilization in
RT   Bacillus subtilis and its involvement in biofilm formation.";
RL   J. Bacteriol. 191:2423-2430(2009).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SINI, AND SUBUNIT.
RX   PubMed=9799632; DOI=10.1006/jmbi.1998.2163;
RA   Lewis R.J., Brannigan J.A., Offen W.A., Smith I., Wilkinson A.J.;
RT   "An evolutionary link between sporulation and prophage induction in the
RT   structure of a repressor:anti-repressor complex.";
RL   J. Mol. Biol. 283:907-912(1998).
CC   -!- FUNCTION: Negative as well as positive regulator of alternate
CC       developmental processes that are induced at the end of vegetative
CC       growth in response to nutrient depletion. Binds to the alkaline
CC       protease (aprE) gene at two sites. Also acts as a repressor of the key
CC       sporulation gene spo0A. Negatively regulates transcription of the eps
CC       operon, which is responsible for the biosynthesis of an
CC       exopolysaccharide involved in biofilm formation; therefore it could
CC       govern the transition between a state in which bacteria swim or swarm
CC       and a state in which bacteria assemble into multicellular communities.
CC       Acts with Hpr as a corepressor of epr expression. Also negatively
CC       regulates transcription of the lutABC operon, which is required for
CC       lactate utilization. Repressor activity is regulated by SinI.
CC       {ECO:0000269|PubMed:15661000, ECO:0000269|PubMed:16923912,
CC       ECO:0000269|PubMed:1898931, ECO:0000269|PubMed:7642487}.
CC   -!- SUBUNIT: Homotetramer in the absence of SinI. Heterodimer with SinI.
CC       Interaction with SinI disrupts the SinR tetramer and its repressor
CC       activity. Interacts with hpr. {ECO:0000269|PubMed:15104138,
CC       ECO:0000269|PubMed:16923912, ECO:0000269|PubMed:9799632}.
DR   EMBL; M14112; AAA22757.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12542.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14392.1; -; Genomic_DNA.
DR   PIR; B25159; B25159.
DR   RefSeq; NP_390341.1; NC_000964.3.
DR   RefSeq; WP_003226345.1; NZ_JNCM01000036.1.
DR   PDB; 1B0N; X-ray; 1.90 A; A=1-111.
DR   PDB; 2YAL; X-ray; 2.27 A; A/B=75-111.
DR   PDB; 3QQ6; X-ray; 1.90 A; A/B=1-69.
DR   PDB; 3ZKC; X-ray; 3.00 A; A/B=1-111.
DR   PDB; 5TN0; NMR; -; A=1-69.
DR   PDB; 5TN2; NMR; -; A/B/C/D=69-111.
DR   PDBsum; 1B0N; -.
DR   PDBsum; 2YAL; -.
DR   PDBsum; 3QQ6; -.
DR   PDBsum; 3ZKC; -.
DR   PDBsum; 5TN0; -.
DR   PDBsum; 5TN2; -.
DR   SMR; P06533; -.
DR   DIP; DIP-6102N; -.
DR   IntAct; P06533; 2.
DR   MINT; P06533; -.
DR   STRING; 224308.BSU24610; -.
DR   PaxDb; P06533; -.
DR   PRIDE; P06533; -.
DR   EnsemblBacteria; CAB14392; CAB14392; BSU24610.
DR   GeneID; 938544; -.
DR   KEGG; bsu:BSU24610; -.
DR   PATRIC; fig|224308.43.peg.2568; -.
DR   eggNOG; ENOG4108IMY; Bacteria.
DR   eggNOG; COG1396; LUCA.
DR   HOGENOM; HOG000225390; -.
DR   InParanoid; P06533; -.
DR   KO; K19449; -.
DR   OMA; YQKWRKA; -.
DR   PhylomeDB; P06533; -.
DR   BioCyc; BSUB:BSU24610-MONOMER; -.
DR   EvolutionaryTrace; P06533; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:CACAO.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd00093; HTH_XRE; 1.
DR   Gene3D; 1.10.260.40; -; 1.
DR   InterPro; IPR001387; Cro/C1-type_HTH.
DR   InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR   InterPro; IPR010981; SinR/SinI_dimer_dom.
DR   InterPro; IPR036281; SinR/SinI_dimer_dom_sf.
DR   Pfam; PF01381; HTH_3; 1.
DR   Pfam; PF08671; SinI; 1.
DR   SMART; SM00530; HTH_XRE; 1.
DR   SUPFAM; SSF47406; SSF47406; 1.
DR   SUPFAM; SSF47413; SSF47413; 1.
DR   PROSITE; PS50943; HTH_CROC1; 1.
DR   PROSITE; PS51500; SIN; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P06533.
DR   SWISS-2DPAGE; P06533.
KW   3D-structure; Activator; DNA-binding; Reference proteome; Repressor;
KW   Sporulation; Transcription; Transcription regulation.
FT   CHAIN           1..111
FT                   /note="HTH-type transcriptional regulator SinR"
FT                   /id="PRO_0000149738"
FT   DOMAIN          6..61
FT                   /note="HTH cro/C1-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   DOMAIN          65..103
FT                   /note="Sin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00833"
FT   DNA_BIND        17..36
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT   HELIX           3..12
FT                   /evidence="ECO:0000244|PDB:1B0N"
FT   HELIX           17..24
FT                   /evidence="ECO:0000244|PDB:1B0N"
FT   HELIX           28..35
FT                   /evidence="ECO:0000244|PDB:1B0N"
FT   HELIX           44..54
FT                   /evidence="ECO:0000244|PDB:1B0N"
FT   HELIX           58..62
FT                   /evidence="ECO:0000244|PDB:1B0N"
FT   STRAND          71..73
FT                   /evidence="ECO:0000244|PDB:5TN2"
FT   HELIX           76..87
FT                   /evidence="ECO:0000244|PDB:1B0N"
FT   HELIX           92..107
FT                   /evidence="ECO:0000244|PDB:1B0N"
SQ   SEQUENCE   111 AA;  12989 MW;  B6FC6463FF4B52C6 CRC64;
     MIGQRIKQYR KEKGYSLSEL AEKAGVAKSY LSSIERNLQT NPSIQFLEKV SAVLDVSVHT
     LLDEKHETEY DGQLDSEWEK LVRDAMTSGV SKKQFREFLD YQKWRKSQKE E
//

If you have problems or comments...

PBIL Back to PBIL home page