Summary: Haemolysin expression modulating protein
This is the Wikipedia entry entitled "Haemolysin expression modulating protein family". More...
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Haemolysin expression modulating protein family Edit Wikipedia article
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solution structure of hemolysin expression modulating protein hha from escherichia coli. ontario centre for structural proteomics target ec0308_1_72; northeast structural genomics target et88
In molecular biology, the haemolysin expression modulating protein family is a family of proteins. This family consists of haemolysin expression modulating protein (Hha) from Escherichia coli and its enterobacterial homologues, such as YmoA from Yersinia enterocolitica, and RmoA encoded on the R100 plasmid. These proteins act as modulators of bacterial gene expression. Members of this family act in conjunction with members of the H-NS family, participating in the thermoregulation of different virulence factors and in plasmid transfer. Hha, along with the chromatin-associated protein H-NS, is involved in the regulation of expression of the toxin alpha-haemolysin in response to osmolarity and temperature. YmoA modulates the expression of various virulence factors, such as Yop proteins and YadA adhesin, in response to temperature. RmoA is a plasmid R100 modulator involved in plasmid transfer. The HHA family of proteins display striking similarity to the oligomerisation domain of the H-NS proteins.
- Madrid C, Nieto JM, Juarez A (February 2002). "Role of the Hha/YmoA family of proteins in the thermoregulation of the expression of virulence factors". Int. J. Med. Microbiol. 291 (6-7): 425–32. PMID 11890540.
- Nieto JM, Madrid C, Miquelay E, Parra JL, Rodriguez S, Juarez A (February 2002). "Evidence for direct protein-protein interaction between members of the enterobacterial Hha/YmoA and H-NS families of proteins". J. Bacteriol. 184 (3): 629–35. PMC 139531. PMID 11790731.
- Nieto JM, Prenafeta A, Miquelay E, Torrades S, Juarez A (December 1998). "Sequence, identification and effect on conjugation of the rmoA gene of plasmid R100-1". FEMS Microbiol. Lett. 169 (1): 59–66. PMID 9851035.
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This family consists of haemolysin expression modulating protein (HHA) homologues. YmoA and Hha are highly similar bacterial proteins downregulating gene expression in Yersinia enterocolitica and Escherichia coli, respectively.
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR007985
This family consists of haemolysin expression modulating protein (Hha) from Escherichia coli and its enterobacterial homologues, such as YmoA from Yersinia enterocolitica, and RmoA encoded on the R100 plasmid. These proteins act as modulators of bacterial gene expression. Members of the Hha/YmoA/RmoA family act in conjunction with members of the H-NS family, participating in the thermoregulation of different virulence factors and in plasmid transfer [PUBMED:11890540]. Hha, along with the chromatin-associated protein H-NS, is involved in the regulation of expression of the toxin alpha-haemolysin in response to osmolarity and temperature [PUBMED:11790731]. YmoA modulates the expression of various virulence factors, such as Yop proteins and YadA adhesin, in response to temperature. RmoA is a plasmid R100 modulator involved in plasmid transfer [PUBMED:9851035]. The HHA family of proteins display striking similarity to the oligomerization domain of the H-NS proteins.
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This example describes an architecture with one
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_7025 (release 7.7)|
|Number in seed:||14|
|Number in full:||1466|
|Average length of the domain:||56.20 aa|
|Average identity of full alignment:||58 %|
|Average coverage of the sequence by the domain:||82.15 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||6|
|Download:||download the raw HMM for this family|
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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 HHA domain has been found. There are 3 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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