SAS2_PRIMG
ID SAS2_PRIMG Reviewed; 73 AA.
AC P10571;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Small, acid-soluble spore protein C2;
DE Short=SASP;
GN Name=SASP-C2;
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=3928443; DOI=10.1016/0378-1119(85)90167-2;
RA Fliss E.R., Setlow P.;
RT "Genes for Bacillus megaterium small, acid-soluble spore proteins:
RT nucleotide sequence of two genes and their expression during sporulation.";
RL Gene 35:151-157(1985).
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; M10920; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; B24033; B24033.
DR AlphaFoldDB; P10571; -.
DR SMR; P10571; -.
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..73
FT /note="Small, acid-soluble spore protein C2"
FT /id="PRO_0000196295"
FT SITE 27..28
FT /note="Cleavage; by spore protease"
SQ SEQUENCE 73 AA; 7731 MW; C44EFAFFECAFB24F CRC64;
MANNKSSNNN ELLVYGAEQA IDQMKYEIAS EFGVNLGADT TARANGSVGG EITKRLVQLA
EQQLGGGRSK TTL