ID   SAS1_BACCR              Reviewed;          70 AA.
AC   P0A4F2; P06551;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Small, acid-soluble spore protein 1;
DE            Short=SASP;
GN   Name=sasP-1; OrderedLocusNames=BC_3091;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alpha/beta-type SASP family. {ECO:0000305}.
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DR   EMBL; AE016877; AAP10035.1; -; Genomic_DNA.
DR   RefSeq; NP_832834.1; NC_004722.1.
DR   RefSeq; WP_000517671.1; NZ_CP034551.1.
DR   AlphaFoldDB; P0A4F2; -.
DR   SMR; P0A4F2; -.
DR   STRING; 226900.BC_3091; -.
DR   PRIDE; P0A4F2; -.
DR   EnsemblBacteria; AAP10035; AAP10035; BC_3091.
DR   GeneID; 67507766; -.
DR   KEGG; bce:BC3091; -.
DR   PATRIC; fig|226900.8.peg.3168; -.
DR   HOGENOM; CLU_169738_2_0_9; -.
DR   OMA; MECASEV; -.
DR   Proteomes; UP000001417; Chromosome.
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; Reference proteome; Sporulation.
FT   CHAIN           1..70
FT                   /note="Small, acid-soluble spore protein 1"
FT                   /id="PRO_0000196289"
FT   SITE            27..28
FT                   /note="Cleavage; by spore protease"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   70 AA;  7466 MW;  D471D89A8CA626A0 CRC64;
     MGKNNSGSRN EVLVRGAEQA LDQMKYEIAQ EFGVQLGADT TARSNGSVGG EITKRLVAMA
     EQQLGGRANR