ID   SAS2_BACIU              Reviewed;          71 AA.
AC   P84584;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 37.
DE   RecName: Full=Small, acid-soluble spore protein 2;
DE            Short=SASP-2;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-71, AND MASS SPECTROMETRY.
RC   STRAIN=Globigii {ECO:0000269|PubMed:15468161};
RX   PubMed=15468161; DOI=10.1002/jms.668;
RA   Whiteaker J.R., Warscheid B., Pribil P., Hathout Y., Fenselau C.;
RT   "Complete sequences of small acid-soluble proteins from Bacillus
RT   globigii.";
RL   J. Mass Spectrom. 39:1113-1121(2004).
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 (By
CC       similarity). {ECO:0000250|UniProtKB:P06552}.
CC   -!- MASS SPECTROMETRY: Mass=7331.90; Mass_error=0.46; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15468161};
CC   -!- MASS SPECTROMETRY: Mass=7332.20; Mass_error=0.07; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15468161};
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. {ECO:0000250|UniProtKB:P06552}.
CC   -!- SIMILARITY: Belongs to the alpha/beta-type SASP family. {ECO:0000255}.
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DR   AlphaFoldDB; P84584; -.
DR   SMR; P84584; -.
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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:15468161"
FT   CHAIN           2..71
FT                   /note="Small, acid-soluble spore protein 2"
FT                   /id="PRO_0000196304"
FT   SITE            29..30
FT                   /note="Cleavage; by spore protease"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   71 AA;  7463 MW;  4CE3E53D9D1CCE83 CRC64;
     MAQNSQNGNS SNQLLVPGAA QAIDQMKFEI ASEFGVNLGA ETTSRANGSV GGEITKRLVS
     FAQQNMSGQQ F