ID   SSPD_BACSU              Reviewed;          64 AA.
AC   P04833;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Small, acid-soluble spore protein D;
DE            Short=SASP;
GN   Name=sspD; OrderedLocusNames=BSU13470;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3009398; DOI=10.1128/jb.166.2.417-425.1986;
RA   Connors M.J., Mason J.M., Setlow P.;
RT   "Cloning and nucleotide sequencing of genes for three small, acid-soluble
RT   proteins from Bacillus subtilis spores.";
RL   J. Bacteriol. 166:417-425(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-13.
RX   PubMed=9852018; DOI=10.1128/jb.180.24.6704-6712.1998;
RA   Bagyan I., Setlow B., Setlow P.;
RT   "New small, acid-soluble proteins unique to spores of Bacillus subtilis:
RT   identification of the coding genes and regulation and function of two of
RT   these genes.";
RL   J. Bacteriol. 180:6704-6712(1998).
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; M12622; AAA22835.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13220.1; -; Genomic_DNA.
DR   PIR; D24546; D24546.
DR   RefSeq; NP_389230.1; NC_000964.3.
DR   RefSeq; WP_003218568.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; P04833; -.
DR   SMR; P04833; -.
DR   STRING; 224308.BSU13470; -.
DR   PaxDb; P04833; -.
DR   EnsemblBacteria; CAB13220; CAB13220; BSU_13470.
DR   GeneID; 64303235; -.
DR   GeneID; 939362; -.
DR   KEGG; bsu:BSU13470; -.
DR   PATRIC; fig|224308.179.peg.1462; -.
DR   eggNOG; ENOG5032YR8; Bacteria.
DR   OMA; WTVANEM; -.
DR   PhylomeDB; P04833; -.
DR   BioCyc; BSUB:BSU13470-MON; -.
DR   PRO; PR:P04833; -.
DR   Proteomes; UP000001570; 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                   /evidence="ECO:0000269|PubMed:9852018"
FT   CHAIN           2..64
FT                   /note="Small, acid-soluble spore protein D"
FT                   /id="PRO_0000196302"
FT   SITE            22..23
FT                   /note="Cleavage; by spore protease"
SQ   SEQUENCE   64 AA;  6804 MW;  CA4D44350707DC35 CRC64;
     MASRNKLVVP GVEQALDQFK LEVAQEFGVN LGSDTVARAN GSVGGEMTKR LVQQAQSQLN
     GTTK