CSP1_STREE
ID CSP1_STREE Reviewed; 41 AA.
AC P60242; Q54712;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Competence-stimulating peptide type 1;
DE Short=CSP-1;
DE Flags: Precursor;
GN Name=comC1; Synonyms=comC;
OS Streptococcus pneumoniae.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 25-41.
RC STRAIN=Rx / CP1200;
RX PubMed=7479953; DOI=10.1073/pnas.92.24.11140;
RA Haevarstein L.S., Coomaraswamy G., Morrison D.A.;
RT "An unmodified heptadecapeptide pheromone induces competence for genetic
RT transformation in Streptococcus pneumoniae.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:11140-11144(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=G376;
RA Iannelli F., Pozzi G., Morrison D.A.;
RT "The signalling domain of histidine kinase controls the specificity of
RT interaction with the competence stimulating peptide.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=29044, 41G, 670, 7731, 859, 871, 872, 873, 875, 878, 880, 881, 950,
RC 951, 952, 953, 954, 960, 964, 967, 9858, Col11, Col12, Col14, Col6, Col7,
RC Col8, Pn107, Pn108, Pn109, Pn110, Pn111, Pn112, Pn12, Pn148, Pn15, Pn16,
RC Pn5, Pn6, Pn60, Rst7, and VA1;
RX PubMed=10322016; DOI=10.1128/jb.181.10.3144-3154.1999;
RA Whatmore A.M.;
RT "Genetic diversity of the streptococcal competence (com) locus.";
RL J. Bacteriol. 181:3144-3154(1999).
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; U33315; AAC44440.1; -; Genomic_DNA.
DR EMBL; AF181270; AAK48419.1; -; Genomic_DNA.
DR EMBL; AJ240738; CAB39422.1; -; Genomic_DNA.
DR EMBL; AJ240739; CAB39424.1; -; Genomic_DNA.
DR EMBL; AJ240740; CAB39426.1; -; Genomic_DNA.
DR EMBL; AJ240741; CAB39428.1; -; Genomic_DNA.
DR EMBL; AJ240742; CAB39430.1; -; Genomic_DNA.
DR EMBL; AJ240743; CAB39432.1; -; Genomic_DNA.
DR EMBL; AJ240744; CAB39434.1; -; Genomic_DNA.
DR EMBL; AJ240745; CAB39436.1; -; Genomic_DNA.
DR EMBL; AJ240746; CAB39438.1; -; Genomic_DNA.
DR EMBL; AJ240747; CAB39440.1; -; Genomic_DNA.
DR EMBL; AJ240748; CAB39442.1; -; Genomic_DNA.
DR EMBL; AJ240749; CAB39444.1; -; Genomic_DNA.
DR EMBL; AJ240750; CAB39446.1; -; Genomic_DNA.
DR EMBL; AJ240751; CAB39448.1; -; Genomic_DNA.
DR EMBL; AJ240752; CAB39450.1; -; Genomic_DNA.
DR EMBL; AJ240753; CAB39452.1; -; Genomic_DNA.
DR EMBL; AJ240754; CAB39454.1; -; Genomic_DNA.
DR EMBL; AJ240755; CAB39456.1; -; Genomic_DNA.
DR EMBL; AJ240756; CAB39458.1; -; Genomic_DNA.
DR EMBL; AJ240757; CAB39460.1; -; Genomic_DNA.
DR EMBL; AJ240758; CAB39462.1; -; Genomic_DNA.
DR EMBL; AJ240761; CAB39468.1; -; Genomic_DNA.
DR EMBL; AJ240766; CAB39472.1; -; Genomic_DNA.
DR EMBL; AJ240768; CAB39476.1; -; Genomic_DNA.
DR EMBL; AJ240769; CAB39478.1; -; Genomic_DNA.
DR EMBL; AJ240770; CAB39480.1; -; Genomic_DNA.
DR EMBL; AJ240771; CAB39482.1; -; Genomic_DNA.
DR EMBL; AJ240772; CAB39484.1; -; Genomic_DNA.
DR EMBL; AJ240774; CAB39488.1; -; Genomic_DNA.
DR EMBL; AJ240775; CAB39490.1; -; Genomic_DNA.
DR EMBL; AJ240776; CAB39492.1; -; Genomic_DNA.
DR EMBL; AJ240777; CAB39494.1; -; Genomic_DNA.
DR EMBL; AJ240778; CAB39496.1; -; Genomic_DNA.
DR EMBL; AJ240779; CAB39498.1; -; Genomic_DNA.
DR EMBL; AJ240780; CAB39500.1; -; Genomic_DNA.
DR EMBL; AJ240781; CAB39502.1; -; Genomic_DNA.
DR EMBL; AJ240782; CAB39504.1; -; Genomic_DNA.
DR EMBL; AJ240783; CAB39506.1; -; Genomic_DNA.
DR EMBL; AJ240784; CAB39508.1; -; Genomic_DNA.
DR EMBL; AJ240785; CAB39510.1; -; Genomic_DNA.
DR EMBL; AJ240786; CAB39512.1; -; Genomic_DNA.
DR EMBL; AJ240789; CAB39518.1; -; Genomic_DNA.
DR PIR; H98126; H98126.
DR RefSeq; WP_000799686.1; NZ_WNIA01000009.1.
DR RefSeq; WP_000799689.1; NZ_WNIC01000003.1.
DR PDB; 6CJ8; NMR; -; A=25-41.
DR PDB; 6COO; NMR; -; A=26-41.
DR PDB; 6COP; NMR; -; A=25-41.
DR PDB; 6COQ; NMR; -; A=25-41.
DR PDB; 6COR; NMR; -; A=25-41.
DR PDB; 6COS; NMR; -; A=25-41.
DR PDB; 6COW; NMR; -; A=25-41.
DR PDB; 6OBW; NMR; -; A=25-41.
DR PDB; 6OC2; NMR; -; A=25-41.
DR PDB; 6OC4; NMR; -; A=25-41.
DR PDB; 6OLD; NMR; -; A=25-41.
DR PDB; 6V1N; NMR; -; A=25-41.
DR PDBsum; 6CJ8; -.
DR PDBsum; 6COO; -.
DR PDBsum; 6COP; -.
DR PDBsum; 6COQ; -.
DR PDBsum; 6COR; -.
DR PDBsum; 6COS; -.
DR PDBsum; 6COW; -.
DR PDBsum; 6OBW; -.
DR PDBsum; 6OC2; -.
DR PDBsum; 6OC4; -.
DR PDBsum; 6OLD; -.
DR PDBsum; 6V1N; -.
DR AlphaFoldDB; P60242; -.
DR BMRB; P60242; -.
DR SMR; P60242; -.
DR GeneID; 60232604; -.
DR GeneID; 66807309; -.
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; Direct protein sequencing; Pheromone; Secreted.
FT PROPEP 1..24
FT /evidence="ECO:0000269|PubMed:7479953"
FT /id="PRO_0000005881"
FT PEPTIDE 25..41
FT /note="Competence-stimulating peptide type 1"
FT /id="PRO_0000005882"
FT TURN 29..35
FT /evidence="ECO:0007829|PDB:6CJ8"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:6CJ8"
SQ SEQUENCE 41 AA; 4971 MW; 1448B414E980E86A CRC64;
MKNTVKLEQF VALKEKDLQK IKGGEMRLSK FFRDFILQRK K
