ID   SAS0_CLOPE              Reviewed;          60 AA.
AC   P41371;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Small, acid-soluble spore protein 1;
DE            Short=SSP-1;
GN   Name=ssp1; OrderedLocusNames=CPE2161;
OS   Clostridium perfringens (strain 13 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2037223; DOI=10.1016/0378-1097(91)90539-m;
RA   Cabrera-Martinez R.M., Setlow P.;
RT   "Cloning and nucleotide sequence of three genes coding for small, acid-
RT   soluble proteins of Clostridium perfringens spores.";
RL   FEMS Microbiol. Lett. 61:127-131(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=13 / Type A;
RX   PubMed=11792842; DOI=10.1073/pnas.022493799;
RA   Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA   Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT   "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT   eater.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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   -!- PTM: SASP are degraded in the first minutes of spore germination and
CC       provide amino acids for both new protein synthesis and metabolism.
CC   -!- SIMILARITY: Belongs to the alpha/beta-type SASP family. {ECO:0000305}.
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DR   EMBL; X59480; CAA42081.1; -; Genomic_DNA.
DR   EMBL; BA000016; BAB81867.1; -; Genomic_DNA.
DR   PIR; A54537; A54537.
DR   RefSeq; WP_003452440.1; NC_003366.1.
DR   AlphaFoldDB; P41371; -.
DR   SMR; P41371; -.
DR   STRING; 195102.gene:10491431; -.
DR   EnsemblBacteria; BAB81867; BAB81867; BAB81867.
DR   GeneID; 29570476; -.
DR   KEGG; cpe:CPE2161; -.
DR   HOGENOM; CLU_169738_2_2_9; -.
DR   OMA; AQFKNEV; -.
DR   Proteomes; UP000000818; Chromosome.
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; Reference proteome; Sporulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..60
FT                   /note="Small, acid-soluble spore protein 1"
FT                   /id="PRO_0000196306"
FT   SITE            19..20
FT                   /note="Cleavage; by spore protease"
SQ   SEQUENCE   60 AA;  6583 MW;  BAE158BE02627481 CRC64;
     MSKSLVPEAK NGLSKFKNEV ARELGVPFSD YNGDLSSRQC GSVGGEMVKR MVEAYESQIK