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Links from Protein

Items: 11

1.

RTX C-terminal domain

This family describes the C-terminal region of various bacterial haemolysins and leukotoxins, which belong to the RTX family of toxins. These are produced by various Gram negative bacteria, such as E. coli (Swiss:P09983) and Actinobacillus pleuropneumoniae (Swiss:P15377). RTX toxins may interact with lipopolysaccharide (LPS) to functionally impair and eventually kill leukocytes [1]. This region is found in association with the RTX N-terminal domain (Pfam:PF02382) and multiple hemolysin-type calcium-binding repeats (Pfam:PF00353). [1]. 8800842. Biological effects of RTX toxins: the possible role of lipopolysaccharide. Czuprynski CJ, Welch RA;. Trends Microbiol 1995;3:480-483. (from Pfam)

Date:
2024-10-16
Family Accession:
NF019939.5
Method:
HMM
2.

N-terminal domain in RTX protein

The RTX family of bacterial toxins are a group of cytolysins and cytotoxins that have RTX (Repeat in ToXin repeats) Pfam:PF00353. This is a hydrophobic pore-forming domain found at the N-terminal of these proteins [2]. [1]. 9628576. Complete nucleotide sequences of 93-kb and 3.3-kb plasmids of an enterohemorrhagic Escherichia coli O157:H7 derived from Sakai outbreak. Makino K, Ishii K, Yasunaga T, Hattori M, Yokoyama K, Yutsudo CH, Kubota Y, Yamaichi Y, Iida T, Yamamoto K, Honda T, Han CG, Ohtsubo E, Kasamatsu M, Hayashi T, Kuhara S, Shinagawa H;. DNA Res 1998;5:1-9. [2]. 30405113. Cytotoxic activity of Kingella kingae RtxA toxin depends on post-translational acylation of lysine residues and cholesterol binding. Osickova A, Balashova N, Masin J, Sulc M, Roderova J, Wald T, Brown AC, Koufos E, Chang EH, Giannakakis A, Lally ET, Osicka R;. Emerg Microbes Infect. 2018;7:178. (from Pfam)

GO Terms:
Molecular Function:
calcium ion binding (GO:0005509)
Cellular Component:
extracellular region (GO:0005576)
Molecular Function:
channel activity (GO:0015267)
Date:
2024-10-16
Family Accession:
NF014440.5
Method:
HMM
3.

RTX calcium-binding repeat protein

GO Terms:
Molecular Function:
calcium ion binding (GO:0005509)
Date:
2024-08-14
Family Accession:
NF012573.5
Method:
HMM
4.
new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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9.
new record, indexing in progress
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10.

RTX family hemolysin

RTX family toxin are secreted from the bacteria and inserted into the membranes of infected cells, causing host cell rupture.

GO Terms:
Molecular Function:
calcium ion binding (GO:0005509)
Cellular Component:
extracellular region (GO:0005576)
Date:
2021-06-17
Family Accession:
NF033943.0
Method:
HMM
11.

RTX toxin hemolysin HlyA

The RTX toxin, one of several that has received the designation HlyA (hemolysin A), has been described in uropathogenic Escherichia coli (UPEC), and may be called HlyA-UPEC or alpha-hemolysin. Although a full-length homolog, it differs from the enterohemolysin EhxA, or EHEC-HlyA, or enteropathogenic Escherichia coli (EHEC).

Gene:
hlyA
Date:
2019-08-29
Family Accession:
NBR009556
Method:
BlastRule
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