ID   SINI_BACLI              Reviewed;          58 AA.
AC   P22755;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Protein SinI;
GN   Name=sinI;
OS   Bacillus licheniformis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FD0120;
RX   PubMed=2121898; DOI=10.1099/00221287-136-7-1223;
RA   Sekiguchi J., Ohsu H., Kuroda A., Moriyama H., Akamatsu T.;
RT   "Nucleotide sequences of the Bacillus subtilis flaD locus and a B.
RT   licheniformis homologue affecting the autolysin level and flagellation.";
RL   J. Gen. Microbiol. 136:1223-1230(1990).
CC   -!- FUNCTION: Acts as an antagonist to SinR. SinI prevents SinR from
CC       binding to its target sequence on the gene for AprE (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Heterodimer with SinR. {ECO:0000250}.
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DR   EMBL; M60287; AAA22438.1; -; Genomic_DNA.
DR   PIR; A45824; A45824.
DR   AlphaFoldDB; P22755; -.
DR   SMR; P22755; -.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   InterPro; IPR010981; SinR/SinI_dimer_dom.
DR   InterPro; IPR036281; SinR/SinI_dimer_dom_sf.
DR   Pfam; PF08671; SinI; 1.
DR   SUPFAM; SSF47406; SSF47406; 1.
DR   PROSITE; PS51500; SIN; 1.
PE   3: Inferred from homology;
FT   CHAIN           1..58
FT                   /note="Protein SinI"
FT                   /id="PRO_0000097762"
FT   DOMAIN          2..40
FT                   /note="Sin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00833"
SQ   SEQUENCE   58 AA;  6694 MW;  3F91E477F0BFC858 CRC64;
     MNKDKNEKEE LDEEWTELIK HALEQGISPD DIRIFLNLGK KSSKPSASIE RSHSINPF