#=GF ID Pesticin_RB
#=GF AC PF21613.1
#=GF DE Pesticin, receptor binding domain
#=GF AU Bateman A;0000-0002-6982-4660
#=GF AU Lazaro Pinto Beatriz;0000-0001-6837-2941
#=GF SE ECOD:EF19592
#=GF GA 27.00 27.00;
#=GF TC 27.00 311.70;
#=GF NC 26.80 20.50;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -E 1000 --cpu 4 -Z 75585367 HMM pfamseq
#=GF TP Domain
#=GF RC Paper describing PDB structure 4aqn
#=GF RN [1]
#=GF RM 22593569
#=GF RT Structural and mechanistic studies of pesticin, a bacterial
#=GF RT homolog of phage lysozymes.
#=GF RA Patzer SI, Albrecht R, Braun V, Zeth K;
#=GF RL J Biol Chem. 2012;287:23381-23396.
#=GF RC Paper describing PDB structure 4epf
#=GF RN [2]
#=GF RM 22679291
#=GF RT Structural engineering of a phage lysin that targets
#=GF RT gram-negative pathogens.
#=GF RA Lukacik P, Barnard TJ, Keller PW, Chaturvedi KS, Seddiki N,
#=GF RA Fairman JW, Noinaj N, Kirby TL, Henderson JP, Steven AC,
#=GF RA Hinnebusch BJ, Buchanan SK;
#=GF RL Proc Natl Acad Sci U S A. 2012;109:9857-9862.
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC This domain is found at the N-terminal end of Pesticin from
#=GF CC Yersinia pestis (Pst). Pst is a toxin that kills related
#=GF CC bacteria of the same niche as Y.pestis. It is organised into
#=GF CC three domains: an N-terminal translocation domain, the
#=GF CC intermediate receptor binding domain (RB, this entry), and a
#=GF CC C-terminal activity domain (Pfam:PF16754). This domain shows a
#=GF CC beta-sheet of seven anti-parallel beta-strands together with
#=GF CC three helices. It is essential for the intimate contact with the
#=GF CC outer membrane protein receptor [1,2].
#=GF SQ 1
#=GS Q57159_YERPE/17-152 AC Q57159.1
Q57159_YERPE/17-152 LFSGSTLSSYRPNFEANSITIALPHYVDLPGRSNFKLMYIMGFPIDTEMEKDSEYSNKIRQESKISKTEGTVSYEQKITVETGQEKDGVKVYRVMVLEGTIAESIEHLDKKENEDILNNNRNRIVLADNTVINFDN
#=GC seq_cons LFSGSTLSSYRPNFEANSITIALPHYVDLPGRSNFKLMYIMGFPIDTEMEKDSEYSNKIRQESKISKTEGTVSYEQKITVETGQEKDGVKVYRVMVLEGTIAESIEHLDKKENEDILNNNRNRIVLADNTVINFDN
//
