ID   SAS1_LACSH              Reviewed;          71 AA.
AC   P06553;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Small, acid-soluble spore protein 1;
DE            Short=SASP;
GN   Name=sasP-1;
OS   Laceyella sacchari (Thermoactinomyces thalpophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Thermoactinomycetaceae;
OC   Laceyella.
OX   NCBI_TaxID=37482;
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; M13062; AAA23003.1; -; Genomic_DNA.
DR   RefSeq; WP_022736790.1; NZ_CP025943.1.
DR   AlphaFoldDB; P06553; -.
DR   SMR; P06553; -.
DR   STRING; 1341151.ASZU01000004_gene508; -.
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..71
FT                   /note="Small, acid-soluble spore protein 1"
FT                   /id="PRO_0000196314"
FT   SITE            28..29
FT                   /note="Cleavage; by spore protease"
SQ   SEQUENCE   71 AA;  7369 MW;  AB25ED57044C4090 CRC64;
     MAQQGRNRSS NQLLVAGAAQ AIDQMKFEIA QEFGVTLGAD TTSRANGSVG GEITKRLVSL
     AQQQLGGGTS F