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8  structures 516  species 1  interaction 1139  sequences 3  architectures

Family: EntA_Immun (PF08951)

Summary: Enterocin A Immunity

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Enterocin A Immunity Provide feedback

Gram-positive lactobacilli produce bacteriocins to kill closely-related competitor species [1]. To protect themselves from the bacteriocidal activity of this molecule they co-express an immunity protein (for discussion of this operon see Bacteriocin_IIc PF10439). The immunity protein structure is a soluble, cytoplasmic, antiparallel four alpha-helical globular bundle with a fifth, more flexible and more divergent C-terminal helical hair-pin [2]. The C-terminal hair-pin recognises the C-terminus of the producer bacteriocin and this interaction is sufficient to dis-orient the bacteriocin within the membrane and close up the permeabilising pore that on its own the bacteriocin creates [3]. These immunity proteins interact in the same way with other bacteriocins, family Bacteriocin_II, PF01721. Since many enterococci can produce more than one bacteriocin it seems likely that the whole operon can be carried on transferable plasmids [4].

Literature references

  1. Johnsen L, Dalhus B, Leiros I, Nissen-Meyer J; , J Biol Chem. 2005;280:19045-19050.: 1.6-Angstroms crystal structure of EntA-im. A bacterial immunity protein conferring immunity to the antimicrobial activity of the pediocin-like bacteriocin enterocin A. PUBMED:15753083 EPMC:15753083

  2. Fimland G, Eijsink VG, Nissen-Meyer J; , Microbiology. 2002;148:3661-3670.: Comparative studies of immunity proteins of pediocin-like bacteriocins. PUBMED:12427956 EPMC:12427956

  3. Soliman W, Bhattacharjee S, Kaur K; , Biochim Biophys Acta. 2007;1774:1002-1013.: Molecular dynamics simulation study of interaction between a class IIa bacteriocin and its immunity protein. PUBMED:17586105 EPMC:17586105

  4. Johnsen L, Fimland G, Nissen-Meyer J; , J Biol Chem. 2005;280:9243-9250.: The C-terminal domain of pediocin-like antimicrobial peptides (class IIa bacteriocins) is involved in specific recognition of the C-terminal part of cognate immunity proteins and in determining the antimicrobial spectrum. PUBMED:15611086 EPMC:15611086


External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR015046

Gram-positive lactobacilli produce bacteriocins to kill closely-related competitor species [PUBMED:15753083]. To protect themselves from the bacteriocidal activity of this molecule they co-express an immunity protein (for discussion of this operon see Bacteriocin_IIc ). The immunity protein structure is a soluble, cytoplasmic, antiparallel four alpha-helical globular bundle with a fifth, more flexible and more divergent C-terminal helical hair-pin [PUBMED:12427956]. The C-terminal hair-pin recognises the C terminus of the producer bacteriocin and this interaction is sufficient to dis-orient the bacteriocin within the membrane and close up the permeabilising pore that on its own the bacteriocin creates [PUBMED:17586105]. These immunity proteins interact in the same way with other bacteriocins, family Bacteriocin_II, . Since many enterococci can produce more than one bacteriocin it seems likely that the whole operon can be carried on transferable plasmids [PUBMED:15611086].

Domain organisation

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Alignments

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(62)
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(559)
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RP35
(44)
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RP75
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  Seed
(62)
Full
(1139)
Representative proteomes NCBI
(559)
Meta
(0)
RP15
(24)
RP35
(44)
RP55
(81)
RP75
(131)
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  Seed
(62)
Full
(1139)
Representative proteomes NCBI
(559)
Meta
(0)
RP15
(24)
RP35
(44)
RP55
(81)
RP75
(131)
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

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HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: pdb_2bl8
Previous IDs: none
Type: Family
Author: Mistry J, Sammut SJ, Coggill P
Number in seed: 62
Number in full: 1139
Average length of the domain: 73.70 aa
Average identity of full alignment: 19 %
Average coverage of the sequence by the domain: 66.60 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.4 21.4
Trusted cut-off 21.4 21.5
Noise cut-off 21.1 21.3
Model length: 75
Family (HMM) version: 5
Download: download the raw HMM for this family

Species distribution

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Interactions

There is 1 interaction for this family. More...

EntA_Immun

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the EntA_Immun domain has been found. There are 8 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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