ID   SAS2_PARBF              Reviewed;          64 AA.
AC   P22066;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   25-MAY-2022, entry version 61.
DE   RecName: Full=Small, acid-soluble spore protein beta;
DE            Short=ASSP;
DE            Short=SASP;
OS   Paraclostridium bifermentans (Clostridium bifermentans).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Paraclostridium.
OX   NCBI_TaxID=1490;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=2599354; DOI=10.1016/0378-1097(89)90185-7;
RA   Cabrera-Martinez R.M., Mason J.M., Setlow B., Waites W.M., Setlow P.;
RT   "Purification and amino acid sequence of two small, acid-soluble proteins
RT   from Clostridium bifermentans spores.";
RL   FEMS Microbiol. Lett. 52:139-143(1989).
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   PIR; B61028; B61028.
DR   AlphaFoldDB; P22066; -.
DR   SMR; P22066; -.
DR   STRING; 1490.B2H97_10690; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Sporulation.
FT   CHAIN           1..64
FT                   /note="Small, acid-soluble spore protein beta"
FT                   /id="PRO_0000196310"
FT   SITE            19..20
FT                   /note="Cleavage; by spore protease"
SQ   SEQUENCE   64 AA;  6992 MW;  4C27AC3183C7DC9B CRC64;
     STKKAVPEAK AALNQMKLEI ANELGLSNYE SVDKGNLTAR QNGYVGGYMT KKLVEMAERQ
     MSGK