ID   SAS1_HALH3              Reviewed;          72 AA.
AC   Q00213; I0JK69;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Small, acid-soluble spore protein 1;
DE            Short=SASP;
GN   Name=Sh-1; OrderedLocusNames=HBHAL_2184;
OS   Halobacillus halophilus (strain ATCC 35676 / DSM 2266 / JCM 20832 / KCTC
OS   3685 / LMG 17431 / NBRC 102448 / NCIMB 2269) (Sporosarcina halophila).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=866895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 / NBRC
RC   102448 / NCIMB 2269;
RX   PubMed=2083842; DOI=10.1016/0378-1097(90)90320-p;
RA   Magill N.G., Loshon C.A., Setlow P.;
RT   "Small, acid-soluble, spore proteins and their genes from two species of
RT   Sporosarcina.";
RL   FEMS Microbiol. Lett. 60:293-297(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35676 / DSM 2266 / JCM 20832 / KCTC 3685 / LMG 17431 / NBRC
RC   102448 / NCIMB 2269;
RX   PubMed=22583374; DOI=10.1111/j.1462-2920.2012.02770.x;
RA   Saum S.H., Pfeiffer F., Palm P., Rampp M., Schuster S.C., Muller V.,
RA   Oesterhelt D.;
RT   "Chloride and organic osmolytes: a hybrid strategy to cope with elevated
RT   salinities by the moderately halophilic, chloride-dependent bacterium
RT   Halobacillus halophilus.";
RL   Environ. Microbiol. 15:1619-1633(2013).
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; X55160; CAA38959.1; -; Genomic_DNA.
DR   EMBL; HE717023; CCG44538.1; -; Genomic_DNA.
DR   PIR; C48180; C48180.
DR   RefSeq; WP_014642441.1; NC_017668.1.
DR   AlphaFoldDB; Q00213; -.
DR   SMR; Q00213; -.
DR   STRING; 866895.HBHAL_2184; -.
DR   EnsemblBacteria; CCG44538; CCG44538; HBHAL_2184.
DR   KEGG; hhd:HBHAL_2184; -.
DR   PATRIC; fig|866895.3.peg.1199; -.
DR   eggNOG; ENOG5032YCI; Bacteria.
DR   HOGENOM; CLU_169738_2_0_9; -.
DR   OrthoDB; 2064087at2; -.
DR   Proteomes; UP000007397; 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   CHAIN           1..72
FT                   /note="Small, acid-soluble spore protein 1"
FT                   /id="PRO_0000196311"
FT   SITE            25..26
FT                   /note="Cleavage; by spore protease"
SQ   SEQUENCE   72 AA;  7790 MW;  E77771551D9EBE10 CRC64;
     MANNNSSNEL VVPGVQQALD QMKYEIAQEF GVQLGADSTS RANGSVGGEI TKRLVQMAEQ
     QFGGQQYGQQ QK