ID   SASG_BACIU              Reviewed;          82 AA.
AC   P84585;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 28.
DE   RecName: Full=Small, acid-soluble spore protein gamma-type;
DE            Short=SASP-gamma;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-82, AND MASS SPECTROMETRY.
RC   STRAIN=Globigii {ECO:0000269|PubMed:15468161};
RX   PubMed=15468161; DOI=10.1002/jms.668;
RA   Whiteaker J.R., Warscheid B., Pribil P., Hathout Y., Fenselau C.;
RT   "Complete sequences of small acid-soluble proteins from Bacillus
RT   globigii.";
RL   J. Mass Spectrom. 39:1113-1121(2004).
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 (By
CC       similarity). {ECO:0000250|UniProtKB:P07785}.
CC   -!- MASS SPECTROMETRY: Mass=8888.83; Mass_error=0.98; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15468161};
CC   -!- MASS SPECTROMETRY: Mass=8889.87; Mass_error=0.83; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:15468161};
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the gamma-type SASP family. {ECO:0000255}.
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DR   AlphaFoldDB; P84585; -.
DR   STRING; 483913.AN935_04500; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Repeat; Sporulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:15468161"
FT   CHAIN           2..82
FT                   /note="Small, acid-soluble spore protein gamma-type"
FT                   /id="PRO_0000196326"
FT   REPEAT          19..45
FT   REPEAT          46..72
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            30..31
FT                   /note="Cleavage; by spore protease"
FT                   /evidence="ECO:0000250"
FT   SITE            57..58
FT                   /note="Cleavage; by spore protease"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   82 AA;  9020 MW;  847052C6B13BB3CB CRC64;
     MANSNNKTNA QQVRKQNQQS ASGQGQFGTE FASETNVQQV RKQNQQSAAG QGQFGTEFAS
     ETDAQQVRQQ NQSAEQNKQQ NS