SAS1_PRIMG
ID SAS1_PRIMG Reviewed; 69 AA.
AC P10570;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Small, acid-soluble spore protein C1;
DE Short=SASP;
GN Name=SASP-C1;
OS Priestia megaterium (Bacillus megaterium).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.
OX NCBI_TaxID=1404;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3928443; DOI=10.1016/0378-1119(85)90167-2;
RA Fliss E.R., Setlow P.;
RT "Genes for Bacillus megaterium small, acid-soluble spore proteins:
RT nucleotide sequence of two genes and their expression during sporulation.";
RL Gene 35:151-157(1985).
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; M10919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A24033; A24033.
DR RefSeq; WP_013058446.1; NZ_VXLA01000105.1.
DR AlphaFoldDB; P10570; -.
DR SMR; P10570; -.
DR GeneID; 64146523; -.
DR OMA; MMANQNG; -.
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..69
FT /note="Small, acid-soluble spore protein C1"
FT /id="PRO_0000196294"
FT SITE 27..28
FT /note="Cleavage; by spore protease"
SQ SEQUENCE 69 AA; 7333 MW; 27A8C248AE0AD778 CRC64;
MANNNSSNNN ELLVYGAEQA IDQMKYEIAS EFGVNLGADT TARANGSVGG EITKRLVQLA
EQQLGGGRF