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 03-AUG-2022, entry version 171.
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}.
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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 AlphaFoldDB; P06533; -.
DR BMRB; P06533; -.
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; BSU_24610.
DR GeneID; 50137039; -.
DR GeneID; 64304251; -.
DR GeneID; 938544; -.
DR KEGG; bsu:BSU24610; -.
DR PATRIC; fig|224308.43.peg.2568; -.
DR eggNOG; COG1396; Bacteria.
DR InParanoid; P06533; -.
DR OMA; YQKWRKA; -.
DR PhylomeDB; P06533; -.
DR BioCyc; BSUB:BSU24610-MON; -.
DR EvolutionaryTrace; P06533; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
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:0045892; P:negative regulation of transcription, DNA-templated; IMP:CACAO.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
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;
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:0007829|PDB:1B0N"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:1B0N"
FT HELIX 28..35
FT /evidence="ECO:0007829|PDB:1B0N"
FT HELIX 44..54
FT /evidence="ECO:0007829|PDB:1B0N"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:1B0N"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:5TN2"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:1B0N"
FT HELIX 92..107
FT /evidence="ECO:0007829|PDB:1B0N"
SQ SEQUENCE 111 AA; 12989 MW; B6FC6463FF4B52C6 CRC64;
MIGQRIKQYR KEKGYSLSEL AEKAGVAKSY LSSIERNLQT NPSIQFLEKV SAVLDVSVHT
LLDEKHETEY DGQLDSEWEK LVRDAMTSGV SKKQFREFLD YQKWRKSQKE E
