Bam complex inserts Hbp into outer membrane

Stable Identifier
R-HSA-9926981
Type
Reaction [transition]
Species
Homo sapiens
Related Species
Escherichia coli
Compartment
cell outer membrane, periplasmic space
ReviewStatus
3/5
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Bam complex inserts Hbp into outer membrane
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The bacterial β-Barrel Assembly Machinery (Bam) complex inserts Serine protease autotransporters of Enterobacteriaceae (SPATEs) like Hbp into the outer membrane (Jain et al., 2007; Ieva et al., 2009; Hagan et al., 2010; Rossiter et al., 2011; Hagan & Kahne, 2011; Iadanza et al., 2016; reviewed in Ruiz-Perez & Nataro, 2020; Xu et al., 2023). The SPATEs Hbp, EspP and EspC are previously bound to periplasmic chaperones (SurA, DegP, Skp, FkpA) (Sherlock et al., 2005; Ruiz-Perez et al., 2009; Orth et al., 2010; Ruiz-Perez et al., 2010; Abreu et al., 2015; reviewed in Ruiz-Perez & Nataro, 2020). SPATE expression is prevalent in extraintestinal E.coli (ExPEC) strains where the released proteases are responsible for tissue damage and cleavage of molecules of the complement system, which is a key feature for the establishment of infection in the bloodstream (Freire et al., 2020).
Literature References
PubMed ID Title Journal Year
20378773 Reconstitution of outer membrane protein assembly from purified components

Hagan, CL, Kim, S, Kahne, D

Science 2010
31965549 Serine protease autotransporters of Enterobacteriaceae (SPATEs) are largely distributed among Escherichia coli isolated from the bloodstream

Freire, CA, Santos, ACM, Pignatari, AC, Silva, RM, Elias, WP

Braz J Microbiol 2020
17513479 Requirement for YaeT in the outer membrane assembly of autotransporter proteins

Jain, S, Goldberg, MB

J Bacteriol 2007
21823654 The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of β-barrel assembly

Hagan, CL, Kahne, D

Biochemistry 2011
37175168 β-Barrel Assembly Machinery (BAM) Complex as Novel Antibacterial Drug Target

Xu, Q, Guo, M, Yu, F

Molecules 2023
21665980 The essential β-barrel assembly machinery complex components BamD and BamA are required for autotransporter biogenesis

Rossiter, AE, Leyton, DL, Tveen-Jensen, K, Browning, DF, Sevastsyanovich, Y, Knowles, TJ, Nichols, KB, Cunningham, AF, Overduin, M, Schembri, MA, Henderson, IR

J Bacteriol 2011
15784535 The TibA adhesin/invasin from enterotoxigenic Escherichia coli is self recognizing and induces bacterial aggregation and biofilm formation

Sherlock, O, Vejborg, RM, Klemm, P

Infect Immun 2005
25583166 The Serine Protease Pic From Enteroaggregative Escherichia coli Mediates Immune Evasion by the Direct Cleavage of Complement Proteins

Abreu, AG, Fraga, TR, Granados Martínez, AP, Kondo, MY, Juliano, MA, Juliano, L, Navarro-Garcia, F, Isaac, L, Barbosa, AS, Elias, WP

J Infect Dis 2015
19734313 Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae

Ruiz-Perez, F, Henderson, IR, Leyton, DL, Rossiter, AE, Zhang, Y, Nataro, JP

J Bacteriol 2009
23689588 Bacterial serine proteases secreted by the autotransporter pathway: classification, specificity, and role in virulence

Ruiz-Perez, F, Nataro, JP

Cell Mol Life Sci 2014
20643852 EspP, a serine protease of enterohemorrhagic Escherichia coli, impairs complement activation by cleaving complement factors C3/C3b and C5

Orth, D, Ehrlenbach, S, Brockmeyer, J, Khan, AB, Huber, G, Karch, H, Sarg, B, Lindner, H, Wurzner, R

Infect Immun 2010
21327044 Interaction of FkpA, a peptidyl-prolyl cis/trans isomerase with EspP autotransporter protein

Ruiz-Perez, F, Henderson, IR, Nataro, JP

Gut Microbes 2010
27686148 Lateral opening in the intact β-barrel assembly machinery captured by cryo-EM

Iadanza, MG, Higgins, AJ, Schiffrin, B, Calabrese, AN, Brockwell, DJ, Ashcroft, AE, Radford, SE, Ranson, NA

Nat Commun 2016
19850876 Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane

Ieva, R, Bernstein, HD

Proc Natl Acad Sci U S A 2009
Participants
Input
Output
Participates
as an event of
Catalyst Activity

membrane insertase activity of Bam complex [cell outer membrane]

Physical Entity
Bam complex [cell outer membrane] (Escherichia coli)
Activity
membrane insertase activity (GO:0032977)
Disease
Cross References
UniProt
Mondo
Authored
Stephan, R  (2024-10-31)
Created
Stephan, R  (2024-11-04)
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