ID   SASG_BACCE              Reviewed;          93 AA.
AC   P07787;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Small, acid-soluble spore protein gamma-type;
DE            Short=SASP;
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3036769; DOI=10.1128/jb.169.7.3088-3093.1987;
RA   Sun D., Setlow P.;
RT   "Cloning and nucleotide sequencing of genes for a second type of small,
RT   acid-soluble spore proteins of Bacillus cereus, Bacillus
RT   stearothermophilus, and 'Thermoactinomyces thalpophilus'.";
RL   J. Bacteriol. 169:3088-3093(1987).
CC   -!- FUNCTION: SASP are proteins degraded in the first minutes of spore
CC       germination and provide amino acids for both new protein synthesis and
CC       metabolism. These proteins may be involved in dormant spore's high
CC       resistance to UV light.
CC   -!- SIMILARITY: Belongs to the gamma-type SASP family. {ECO:0000305}.
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DR   EMBL; M16813; AAA22736.1; -; Genomic_DNA.
DR   PIR; A27086; A27086.
DR   RefSeq; WP_000039046.1; NZ_VTRD01000009.1.
DR   AlphaFoldDB; P07787; -.
DR   SMR; P07787; -.
DR   STRING; 1396.DJ87_5621; -.
DR   eggNOG; ENOG5033E7P; Bacteria.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR006341; Spore_gamma.
DR   Pfam; PF04259; SASP_gamma; 1.
DR   TIGRFAMs; TIGR01442; SASP_gamma; 1.
PE   3: Inferred from homology;
KW   Repeat; Sporulation.
FT   CHAIN           1..93
FT                   /note="Small, acid-soluble spore protein gamma-type"
FT                   /id="PRO_0000196321"
FT   REPEAT          18..52
FT   REPEAT          55..89
FT   REGION          1..93
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            27..28
FT                   /note="Cleavage; by spore protease"
FT                   /evidence="ECO:0000269|PubMed:3036769"
FT   SITE            64..65
FT                   /note="Cleavage; by spore protease"
FT                   /evidence="ECO:0000269|PubMed:3036769"
SQ   SEQUENCE   93 AA;  9671 MW;  BDD60651043C5A50 CRC64;
     MSKKQQGYNK ATSGASIQST NASYGTEFST ETDVQAVKQA NAQSEAKKAQ ASGAQSANAS
     YGTEFATETD VHSVKKQNAK SAAKQSQSSS SNQ