ID   SASC_PRIMG              Reviewed;          72 AA.
AC   P02960;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Small, acid-soluble spore protein C;
DE            Short=SASP;
GN   Name=sasP-C;
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=6327639; DOI=10.1128/jb.158.3.809-813.1984;
RA   Fliss E.R., Setlow P.;
RT   "Complete nucleotide sequence and start sites for transcription and
RT   translation of the Bacillus megaterium protein C gene.";
RL   J. Bacteriol. 158:809-813(1984).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-39.
RX   PubMed=6767722; DOI=10.1016/s0021-9258(19)85749-6;
RA   Setlow P., Gerard C., Ozols J.;
RT   "The amino acid sequence specificity of a protease from spores of Bacillus
RT   megaterium.";
RL   J. Biol. Chem. 255:3624-3628(1980).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-15 AND 32-72.
RX   PubMed=6773941; DOI=10.1016/s0021-9258(18)43511-9;
RA   Setlow P., Ozols J.;
RT   "Covalent structure of protein C. A second major low molecular weight
RT   protein degraded during germination of Bacillus megaterium spores.";
RL   J. Biol. Chem. 255:8413-8416(1980).
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; K01833; AAA22282.1; -; Genomic_DNA.
DR   PIR; I39794; USBSCM.
DR   RefSeq; WP_013055290.1; NZ_WIPB01000114.1.
DR   AlphaFoldDB; P02960; -.
DR   SMR; P02960; -.
DR   PRIDE; P02960; -.
DR   GeneID; 48011215; -.
DR   GeneID; 64149480; -.
DR   OMA; SEDYWGT; -.
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:6767722,
FT                   ECO:0000269|PubMed:6773941"
FT   CHAIN           2..72
FT                   /note="Small, acid-soluble spore protein C"
FT                   /id="PRO_0000196293"
FT   SITE            31..32
FT                   /note="Cleavage; by spore protease"
SQ   SEQUENCE   72 AA;  7554 MW;  7463B99AC47F9567 CRC64;
     MANYQNASNR NSSNKLVAPG AQAAIDQMKF EIASEFGVNL GPDATARANG SVGGEITKRL
     VQLAEQNLGG KY