SAS1_CLOPE
ID SAS1_CLOPE Reviewed; 59 AA.
AC P21886; P10573;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 112.
DE RecName: Full=Small, acid-soluble spore protein C1;
DE Short=ASSP;
DE Short=SASP;
DE AltName: Full=SSP-2;
GN Name=sspC1; Synonyms=ssp2; OrderedLocusNames=CPE2064;
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].
RC STRAIN=ATCC 12917 / NCTC 8239 / Type A;
RX PubMed=2401406; DOI=10.1016/0378-1119(90)90169-r;
RA Holck A., Blom H., Granum P.E.;
RT "Cloning and sequencing of the genes encoding acid-soluble spore proteins
RT from Clostridium perfringens.";
RL Gene 91:107-111(1990).
RN [2]
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 [3]
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).
RN [4]
RP PRELIMINARY PROTEIN SEQUENCE OF 2-59.
RA Granum P.E., Richardson M., Blom H.;
RT "Isolation and amino acid sequence of an acid soluble protein from
RT Clostridium perfringens spores.";
RL FEMS Microbiol. Lett. 42:225-230(1987).
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; M57433; AAA62757.1; -; Genomic_DNA.
DR EMBL; X59481; CAA42082.1; -; Genomic_DNA.
DR EMBL; BA000016; BAB81770.1; -; Genomic_DNA.
DR PIR; JN0082; JN0082.
DR RefSeq; WP_003451068.1; NC_003366.1.
DR AlphaFoldDB; P21886; -.
DR SMR; P21886; -.
DR STRING; 195102.gene:10491334; -.
DR EnsemblBacteria; BAB81770; BAB81770; BAB81770.
DR GeneID; 29570572; -.
DR KEGG; cpe:CPE2064; -.
DR HOGENOM; CLU_169738_2_2_9; -.
DR OMA; DSMANRN; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; DNA-binding; Reference proteome; Sporulation.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..59
FT /note="Small, acid-soluble spore protein C1"
FT /id="PRO_0000196307"
FT SITE 19..20
FT /note="Cleavage; by spore protease"
SQ SEQUENCE 59 AA; 6437 MW; AF5C1382D37FCAE5 CRC64;
MSQHLVPEAK NGLSKFKNEV AAEMGVPFSD YNGDLSSKQC GSVGGEMVKR MVEQYEKGI