SAS3_PRIMG
ID SAS3_PRIMG Reviewed; 65 AA.
AC P10572;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Small, acid-soluble spore protein C3;
DE Short=SASP;
GN Name=SASP-C3;
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=6439604; DOI=10.1016/0378-1119(84)90117-3;
RA Fliss E.R., Setlow P.;
RT "Bacillus megaterium spore protein C-3: nucleotide sequence of its gene and
RT the amino acid sequence at its spore protease cleavage site.";
RL Gene 30:167-172(1984).
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; M12336; AAA22782.1; -; Genomic_DNA.
DR PIR; A22810; A22810.
DR RefSeq; WP_013055933.1; NZ_WIPB01000018.1.
DR AlphaFoldDB; P10572; -.
DR SMR; P10572; -.
DR GeneID; 48011853; -.
DR GeneID; 64144798; -.
DR OMA; WTVANEM; -.
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..65
FT /note="Small, acid-soluble spore protein C3"
FT /id="PRO_0000196296"
FT SITE 22..23
FT /note="Cleavage; by spore protease"
SQ SEQUENCE 65 AA; 7027 MW; 98387ED2C3C12894 CRC64;
MARTNKLLTP GVEQFLDQYK YEIAQEFGVT LGSDTAARSN GSVGGEITKR LVQQAQAHLS
GSTQK