ID   SAS4_PRIMG              Reviewed;          69 AA.
AC   P04834;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Small, acid-soluble spore protein C4;
DE            Short=SASP;
GN   Name=SASP-C4;
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=3080406; DOI=10.1128/jb.165.2.467-473.1986;
RA   Fliss E.R., Loshon C.A., Setlow P.;
RT   "Genes for Bacillus megaterium small, acid-soluble spore proteins: cloning
RT   and nucleotide sequence of three additional genes from this multigene
RT   family.";
RL   J. Bacteriol. 165:467-473(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; M14110; AAA22283.1; -; Genomic_DNA.
DR   PIR; B24543; B24543.
DR   RefSeq; WP_013058452.1; NZ_WIPB01000220.1.
DR   AlphaFoldDB; P04834; -.
DR   SMR; P04834; -.
DR   GeneID; 48012189; -.
DR   GeneID; 64148463; -.
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..69
FT                   /note="Small, acid-soluble spore protein C4"
FT                   /id="PRO_0000196297"
FT   SITE            27..28
FT                   /note="Cleavage; by spore protease"
SQ   SEQUENCE   69 AA;  7347 MW;  20DFB24FD97AD778 CRC64;
     MANNKSSNNN ELLVYGAEQA IDQMKYEIAS EFGVNLGADT TARANGSVGG EITKRLVQLA
     EQQLGGGRF