ID   SASA_PRIMG              Reviewed;          62 AA.
AC   P02959;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Small, acid-soluble spore protein A;
DE            Short=SASP;
GN   Name=sasP-A;
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-62.
RX   PubMed=115874; DOI=10.1016/s0021-9258(19)86407-4;
RA   Setlow P., Ozols J.;
RT   "Covalent structure of protein A. A low molecular weight protein degraded
RT   during germination of Bacillus megaterium spores.";
RL   J. Biol. Chem. 254:11938-11942(1979).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M14109; AAA22285.1; -; Genomic_DNA.
DR   PIR; A24543; USBSAM.
DR   RefSeq; WP_013059477.1; NZ_WIPB01000142.1.
DR   AlphaFoldDB; P02959; -.
DR   SMR; P02959; -.
DR   GeneID; 48015274; -.
DR   GeneID; 64145494; -.
DR   OMA; TNEPVMP; -.
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:115874"
FT   CHAIN           2..62
FT                   /note="Small, acid-soluble spore protein A"
FT                   /id="PRO_0000196292"
FT   SITE            22..23
FT                   /note="Cleavage; by spore protease"
SQ   SEQUENCE   62 AA;  6391 MW;  8F1A8766DC86DBBD CRC64;
     MANTNKLVAP GSAAAIDQMK YEIASEFGVN LGPEATARAN GSVGGEITKR LVQMAEQQLG
     GK