SAS1_GEOSE
ID SAS1_GEOSE Reviewed; 70 AA.
AC P06552;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Small, acid-soluble spore protein 1;
DE Short=SASP;
GN Name=sasP-1;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
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; M13061; AAA22740.1; -; Genomic_DNA.
DR PIR; C25234; C25234.
DR AlphaFoldDB; P06552; -.
DR SMR; P06552; -.
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_0000196305"
FT SITE 28..29
FT /note="Cleavage; by spore protease"
SQ SEQUENCE 70 AA; 7227 MW; 2038C1C0DC6642B0 CRC64;
MPNQSGSNSS NQLLVPGAAQ VIDQMKFEIA SEFGVNLGAE TTSRANGSVG GEITKRLVSF
AQQQMGGGVQ