SSPC_BACSU
ID SSPC_BACSU Reviewed; 72 AA.
AC P02958;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Small, acid-soluble spore protein C;
DE Short=SASP;
GN Name=sspC; OrderedLocusNames=BSU19950;
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=2981806; DOI=10.1128/jb.161.1.333-339.1985;
RA Connors M.J., Setlow P.;
RT "Cloning of a small, acid-soluble spore protein gene from Bacillus subtilis
RT and determination of its complete nucleotide sequence.";
RL J. Bacteriol. 161:333-339(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9679200; DOI=10.1093/dnares/5.2.121;
RA Ghim S.-Y., Choi S.-K., Shin B.-S., Park S.-H.;
RT "An 8 kb nucleotide sequence at the 3' flanking region of the sspC gene
RT (184 degrees) on the Bacillus subtilis 168 chromosome containing an intein
RT and an intron.";
RL DNA Res. 5:121-126(1998).
RN [3]
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).
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; K02968; AAA22737.1; -; Genomic_DNA.
DR EMBL; AF012906; AAB92494.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13886.1; -; Genomic_DNA.
DR PIR; A03476; USBS1.
DR RefSeq; NP_389876.1; NC_000964.3.
DR RefSeq; WP_009967454.1; NZ_JNCM01000036.1.
DR PDB; 2Z3X; X-ray; 2.10 A; A/B/C=13-72.
DR PDBsum; 2Z3X; -.
DR AlphaFoldDB; P02958; -.
DR SMR; P02958; -.
DR DIP; DIP-29747N; -.
DR STRING; 224308.BSU19950; -.
DR PaxDb; P02958; -.
DR EnsemblBacteria; CAB13886; CAB13886; BSU_19950.
DR GeneID; 939473; -.
DR KEGG; bsu:BSU19950; -.
DR PATRIC; fig|224308.179.peg.2183; -.
DR eggNOG; ENOG5032YCI; Bacteria.
DR OMA; MMANQNG; -.
DR PhylomeDB; P02958; -.
DR BioCyc; BSUB:BSU19950-MON; -.
DR EvolutionaryTrace; P02958; -.
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 3D-structure; DNA-binding; Reference proteome; Sporulation.
FT CHAIN 1..72
FT /note="Small, acid-soluble spore protein C"
FT /id="PRO_0000196301"
FT SITE 30..31
FT /note="Cleavage; by spore protease"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:2Z3X"
FT HELIX 21..35
FT /evidence="ECO:0007829|PDB:2Z3X"
FT HELIX 45..65
FT /evidence="ECO:0007829|PDB:2Z3X"
SQ SEQUENCE 72 AA; 7758 MW; F1E1788E86F28F8D CRC64;
MAQQSRSRSN NNNDLLIPQA ASAIEQMKLE IASEFGVQLG AETTSRANGS VGGEITKRLV
RLAQQNMGGQ FH
