ID   GCCF_LACPN              Reviewed;          64 AA.
AC   E9K9Z1;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   25-MAY-2022, entry version 19.
DE   RecName: Full=Bacteriocin glycocin F {ECO:0000303|PubMed:21251913};
DE            Short=GccF {ECO:0000303|PubMed:21251913};
DE   Flags: Precursor;
GN   Name=gccF {ECO:0000312|EMBL:ADV57366.1};
OS   Lactiplantibacillus plantarum (Lactobacillus plantarum).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1590;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:ADV57366.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-64, FUNCTION,
RP   SUBCELLULAR LOCATION, MASS SPECTROMETRY, DISULFIDE BONDS, AND GLYCOSYLATION
RP   AT SER-39 AND CYS-64.
RC   STRAIN=KW30 {ECO:0000312|EMBL:ADV57366.1};
RX   PubMed=21251913; DOI=10.1016/j.febslet.2011.01.023;
RA   Stepper J., Shastri S., Loo T.S., Preston J.C., Novak P., Man P.,
RA   Moore C.H., Havlicek V., Patchett M.L., Norris G.E.;
RT   "Cysteine S-glycosylation, a new post-translational modification found in
RT   glycopeptide bacteriocins.";
RL   FEBS Lett. 585:645-650(2011).
RN   [2] {ECO:0000305}
RP   STRUCTURE BY NMR, DISULFIDE BONDS, AND GLYCOSYLATION AT SER-39 AND CYS-64.
RC   STRAIN=KW30 {ECO:0000269|PubMed:21395300};
RX   PubMed=21395300; DOI=10.1021/bi200217u;
RA   Venugopal H., Edwards P.J., Schwalbe M., Claridge J.K., Libich D.S.,
RA   Stepper J., Loo T., Patchett M.L., Norris G.E., Pascal S.M.;
RT   "Structural, dynamic, and chemical characterization of a novel s-
RT   glycosylated bacteriocin.";
RL   Biochemistry 50:2748-2755(2011).
CC   -!- FUNCTION: Has antibacterial activity against L.plantarum ATCC 8014. In
CC       purified form, the activity is bacteriostatic (IC(50)=2 nM) rather than
CC       bactericidal. {ECO:0000269|PubMed:21251913}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21251913}.
CC   -!- MASS SPECTROMETRY: Mass=5199.0488; Method=Electrospray; Note=Dual
CC       Electrospray/MALDI source.; Evidence={ECO:0000269|PubMed:21251913};
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DR   EMBL; GU552553; ADV57366.1; -; Genomic_DNA.
DR   PDB; 2KUY; NMR; -; A=22-64.
DR   PDBsum; 2KUY; -.
DR   AlphaFoldDB; E9K9Z1; -.
DR   BMRB; E9K9Z1; -.
DR   SMR; E9K9Z1; -.
DR   iPTMnet; E9K9Z1; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Bacteriocin;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:21251913"
FT   CHAIN           22..64
FT                   /note="Bacteriocin glycocin F"
FT                   /evidence="ECO:0000269|PubMed:21251913"
FT                   /id="PRO_5000706231"
FT   CARBOHYD        39
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000269|PubMed:21251913,
FT                   ECO:0000269|PubMed:21395300"
FT   CARBOHYD        64
FT                   /note="S-linked (GlcNAc) cysteine"
FT                   /evidence="ECO:0000269|PubMed:21251913,
FT                   ECO:0000269|PubMed:21395300"
FT   DISULFID        26..49
FT                   /evidence="ECO:0000269|PubMed:21251913,
FT                   ECO:0000269|PubMed:21395300"
FT   DISULFID        33..42
FT                   /evidence="ECO:0000269|PubMed:21251913,
FT                   ECO:0000269|PubMed:21395300"
FT   HELIX           26..31
FT                   /evidence="ECO:0007829|PDB:2KUY"
FT   STRAND          37..40
FT                   /evidence="ECO:0007829|PDB:2KUY"
FT   HELIX           41..50
FT                   /evidence="ECO:0007829|PDB:2KUY"
SQ   SEQUENCE   64 AA;  7002 MW;  C294FC72D49FB316 CRC64;
     MSKLVKTLTI SEISKAQNNG GKPAWCWYTL AMCGAGYDSG TCDYMYSHCF GIKHHSSGSS
     SYHC