#=GF ID   Antimicrobial17
#=GF AC   PF08129.14
#=GF DE   Alpha/beta enterocin family
#=GF AU   Lee SC;0000-0002-0504-0859
#=GF SE   Short protein clustering
#=GF GA   25.00 25.00;
#=GF TC   25.70 28.50;
#=GF NC   24.30 23.80;
#=GF BM   hmmbuild HMM.ann SEED.ann
#=GF SM   hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
#=GF TP   Family
#=GF WK   Class_II_bacteriocin
#=GF CL   CL0400
#=GF RN   [1]
#=GF RM   10742203
#=GF RT   Characterization and cloning of the genes encoding enterocin
#=GF RT   1071A and enterocin 1071B, two antimicrobial peptides produced
#=GF RT   by Enterococcus faecalis BFE 1071. 
#=GF RA   Balla E, Dicks LM, Du Toit M, Van Der Merwe MJ, Holzapfel WH; 
#=GF RL   Appl Environ Microbiol 2000;66:1298-1304.
#=GF DR   INTERPRO; IPR012950;
#=GF DR   TC; 1.C.25;
#=GF DR   SO; 0100021; polypeptide_conserved_region;
#=GF CC   This family consists of the alpha and beta enterocins and 
#=GF CC   lactococcin G peptides. These peptides have some antimicrobial 
#=GF CC   properties; they inhibit the growth of Enterococcus spp. and a 
#=GF CC   few other gram-positive bacteria. These peptides act as pore-
#=GF CC   forming toxins that create cell membrane channels through a 
#=GF CC   barrel-stave mechanism and thus produce an ionic imbalance in 
#=GF CC   the cell. These family of antimicrobial peptides belong to the 
#=GF CC   class II group of bacteriocin [1].
#=GF SQ   2
#=GS A0A371AXP5_9FIRM/6-57  AC A0A371AXP5.1
#=GS R2S5N8_9ENTE/3-49      AC R2S5N8.1
A0A371AXP5_9FIRM/6-57             celtines-------------RSINGGSAFNDIGNVVGKGLYYICKGLDASTTAGQMERWHKK--hn....
R2S5N8_9ENTE/3-49                 ........MEKTKVLNVKEMKKVIGGNDVSCAVGIAVGAGAGGVIGAIG----------------glltec
#=GC seq_cons                     .....................+sIsGsss.sslG.sVGtGhhhlhtuls................t.....
//