ID   SAS2_SPOUR              Reviewed;          67 AA.
AC   P52969;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Small, acid-soluble spore protein 2;
DE            Short=SASP;
GN   Name=Su-2;
OS   Sporosarcina ureae.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX   NCBI_TaxID=1571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13881 / BS 860;
RX   PubMed=2083842; DOI=10.1016/0378-1097(90)90320-p;
RA   Magill N.G., Loshon C.A., Setlow P.;
RT   "Small, acid-soluble, spore proteins and their genes from two species of
RT   Sporosarcina.";
RL   FEMS Microbiol. Lett. 60:293-297(1990).
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; X55159; CAA38958.1; -; Genomic_DNA.
DR   PIR; B48180; B48180.
DR   RefSeq; WP_029052872.1; NZ_CP015108.1.
DR   AlphaFoldDB; P52969; -.
DR   SMR; P52969; -.
DR   eggNOG; ENOG5032YCI; Bacteria.
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..67
FT                   /note="Small, acid-soluble spore protein 2"
FT                   /id="PRO_0000196313"
FT   SITE            25..26
FT                   /note="Cleavage; by spore protease"
SQ   SEQUENCE   67 AA;  7176 MW;  14CBE9CFE17559A2 CRC64;
     MPNNNSSNQL LVPGVQQALN QMKEEIASEF GVQLGPDASS RANGSVGGEI TKRLVRQAQS
     QMNGYTK