ID   SAS1_BACCE              Reviewed;          70 AA.
AC   P0A4F3; P06551;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Small, acid-soluble spore protein 1;
DE            Short=SASP;
GN   Name=sasP-1;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3087949; DOI=10.1128/jb.167.1.168-173.1986;
RA   Loshon C.A., Fliss E.R., Setlow B., Foerster H.F., Setlow P.;
RT   "Cloning and nucleotide sequencing of genes for small, acid-soluble spore
RT   proteins of Bacillus cereus, Bacillus stearothermophilus, and
RT   'Thermoactinomyces thalpophilus'.";
RL   J. Bacteriol. 167:168-173(1986).
CC   -!- FUNCTION: SASP are bound to spore DNA. They are double-stranded DNA-
CC       binding proteins that cause DNA to change to an a-like conformation.
CC       They protect the DNA backbone from chemical and enzymatic cleavage and
CC       are thus involved in dormant spore's high resistance to UV light.
CC   -!- MISCELLANEOUS: SASP are degraded in the first minutes of spore
CC       germination and provide amino acids for both new protein synthesis and
CC       metabolism.
CC   -!- SIMILARITY: Belongs to the alpha/beta-type SASP family. {ECO:0000305}.
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DR   EMBL; M13059; AAA22738.1; -; Genomic_DNA.
DR   PIR; A25234; A25234.
DR   RefSeq; WP_000517671.1; NZ_WBPB01000052.1.
DR   AlphaFoldDB; P0A4F3; -.
DR   SMR; P0A4F3; -.
DR   STRING; 1396.DJ87_1805; -.
DR   GeneID; 67507766; -.
DR   eggNOG; ENOG5032YCI; Bacteria.
DR   OMA; MECASEV; -.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.10.80; -; 1.
DR   InterPro; IPR001448; SASP_alpha/beta-type.
DR   InterPro; IPR018126; SASP_alpha/beta-type_CS.
DR   InterPro; IPR038300; SASP_sf_alpha/beta.
DR   Pfam; PF00269; SASP; 1.
DR   PROSITE; PS00304; SASP_1; 1.
DR   PROSITE; PS00684; SASP_2; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Sporulation.
FT   CHAIN           1..70
FT                   /note="Small, acid-soluble spore protein 1"
FT                   /id="PRO_0000196288"
FT   SITE            27..28
FT                   /note="Cleavage; by spore protease"
SQ   SEQUENCE   70 AA;  7466 MW;  D471D89A8CA626A0 CRC64;
     MGKNNSGSRN EVLVRGAEQA LDQMKYEIAQ EFGVQLGADT TARSNGSVGG EITKRLVAMA
     EQQLGGRANR