ID   CSP2_STRPN              Reviewed;          41 AA.
AC   P72507;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Competence-stimulating peptide type 2;
DE            Short=CSP-2;
DE   Flags: Precursor;
GN   Name=comC2; OrderedLocusNames=SP_2237;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A66 / Type 3;
RX   PubMed=8830714; DOI=10.1128/jb.178.20.6087-6090.1996;
RA   Pozzi G., Masala L., Iannelli F., Manganelli R., Haevarstein L.S.,
RA   Piccoli L., Simon D., Morrison D.A.;
RT   "Competence for genetic transformation in encapsulated strains of
RT   Streptococcus pneumoniae: two allelic variants of the peptide pheromone.";
RL   J. Bacteriol. 178:6087-6090(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
CC   -!- FUNCTION: Acts as a pheromone, induces cells to develop competence for
CC       genetic transformation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the ComC family. {ECO:0000305}.
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DR   EMBL; X95385; CAA64671.1; -; Genomic_DNA.
DR   EMBL; AE005672; AAK76284.1; -; Genomic_DNA.
DR   PIR; C95261; C95261.
DR   RefSeq; WP_000799686.1; NZ_AKVY01000001.1.
DR   PDB; 6COT; NMR; -; A=25-41.
DR   PDB; 6COU; NMR; -; A=26-41.
DR   PDB; 6COV; NMR; -; A=25-41.
DR   PDBsum; 6COT; -.
DR   PDBsum; 6COU; -.
DR   PDBsum; 6COV; -.
DR   AlphaFoldDB; P72507; -.
DR   BMRB; P72507; -.
DR   SMR; P72507; -.
DR   STRING; 170187.SP_2237; -.
DR   EnsemblBacteria; AAK76284; AAK76284; SP_2237.
DR   KEGG; spn:SP_2237; -.
DR   eggNOG; ENOG5032ASE; Bacteria.
DR   BioCyc; SPNE170187:G1FZB-2340-MON; -.
DR   Proteomes; UP000000585; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005186; F:pheromone activity; IEA:UniProtKB-KW.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   InterPro; IPR004288; Competence_ComC.
DR   Pfam; PF03047; ComC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Competence; Pheromone; Secreted.
FT   PROPEP          1..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000005885"
FT   PEPTIDE         25..41
FT                   /note="Competence-stimulating peptide type 2"
FT                   /id="PRO_0000005886"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:6COT"
FT   TURN            31..36
FT                   /evidence="ECO:0007829|PDB:6COT"
FT   HELIX           37..40
FT                   /evidence="ECO:0007829|PDB:6COT"
SQ   SEQUENCE   41 AA;  4907 MW;  0DA24BE92A63C96A CRC64;
     MKNTVKLEQF VALKEKDLQK IKGGEMRISR IILDFLFLRK K