CBB2_CARML
ID CBB2_CARML Reviewed; 66 AA.
AC P38580;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Bacteriocin carnobacteriocin B2;
DE AltName: Full=Carnocin CP52;
DE Flags: Precursor;
GN Name=cbnB2; Synonyms=canCP52;
OS Carnobacterium maltaromaticum (Carnobacterium piscicola).
OG Plasmid 61 kb.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=2751;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 19-53.
RC STRAIN=LV17B;
RX PubMed=8163526; DOI=10.1016/s0021-9258(17)32702-3;
RA Quadri L.E.N., Sailer M., Roy K.L., Vederas J.C., Stiles M.E.;
RT "Chemical and genetic characterization of bacteriocins produced by
RT Carnobacterium piscicola LV17B.";
RL J. Biol. Chem. 269:12204-12211(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CP5;
RX PubMed=9353214; DOI=10.1007/s002849900262;
RA Herbin S., Mathieu F., Brule F., Branlant C., Lefebvre G., Lebrihi A.;
RT "Characteristics and genetic determinants of bacteriocin activities
RT produced by Carnobacterium piscicola CP5 isolated from cheese.";
RL Curr. Microbiol. 35:319-326(1997).
RN [3]
RP STRUCTURE BY NMR OF 19-66.
RX PubMed=10569926; DOI=10.1021/bi991351x;
RA Wang Y., Henz M.E., Gallagher N.L.F., Chai S., Gibbs A.C., Yan L.Z.,
RA Stiles M.E., Wishart D.S., Vederas J.C.;
RT "Solution structure of carnobacteriocin B2 and implications for structure-
RT activity relationships among type IIa bacteriocins from lactic acid
RT bacteria.";
RL Biochemistry 38:15438-15447(1999).
CC -!- FUNCTION: Has antibacterial activity against Listeria and Enterococcus.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the bacteriocin class IIA/YGNGV family.
CC {ECO:0000305}.
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DR EMBL; L29059; AAA72431.1; -; Genomic_DNA.
DR EMBL; L47121; AAB81310.1; -; Genomic_DNA.
DR EMBL; U76763; AAB18989.1; -; Genomic_DNA.
DR PIR; C53589; C53589.
DR PDB; 1CW5; NMR; -; A=19-66.
DR PDB; 1RY3; NMR; -; A=1-63.
DR PDBsum; 1CW5; -.
DR PDBsum; 1RY3; -.
DR AlphaFoldDB; P38580; -.
DR BMRB; P38580; -.
DR SMR; P38580; -.
DR TCDB; 1.C.24.1.7; the pediocin (pediocin) family.
DR EvolutionaryTrace; P38580; -.
DR GO; GO:0005576; C:extracellular region; IDA:CAFA.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0001897; P:cytolysis by symbiont of host cells; IDA:CAFA.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0051712; P:positive regulation of killing of cells of another organism; IDA:CAFA.
DR Gene3D; 1.20.5.130; -; 1.
DR InterPro; IPR002633; Bacteriocin_IIa.
DR InterPro; IPR023384; Bacteriocin_IIa_CS.
DR InterPro; IPR023388; Bacteriocin_IIa_dom_sf.
DR Pfam; PF01721; Bacteriocin_II; 1.
DR PROSITE; PS60030; BACTERIOCIN_IIA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin;
KW Direct protein sequencing; Disulfide bond; Plasmid; Secreted.
FT PROPEP 1..18
FT /evidence="ECO:0000269|PubMed:8163526"
FT /id="PRO_0000002736"
FT CHAIN 19..66
FT /note="Bacteriocin carnobacteriocin B2"
FT /id="PRO_0000002737"
FT DISULFID 27..32
FT HELIX 4..13
FT /evidence="ECO:0007829|PDB:1RY3"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:1CW5"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1RY3"
FT HELIX 36..59
FT /evidence="ECO:0007829|PDB:1CW5"
SQ SEQUENCE 66 AA; 6994 MW; 6207236A146B168E CRC64;
MNSVKELNVK EMKQLHGGVN YGNGVSCSKT KCSVNWGQAF QERYTAGINS FVSGVASGAG
SIGRRP
