Cited by 69Bacterial Genetics and BiotechnologyBiochemical and Structural CharacterizationDrug Transport and Resistance Mechanisms

Selective transport by SecA2: An expanding family of customized motor proteins

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Bensing, Barbara A., Seepersaud, Ravin, Yen, Yihfen T., Sullam, Paul M.·2014·Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

Abstract

The SecA2 proteins are a special class of transport-associated ATPases that are related to the SecA component of the general Sec system, and are found in an increasingly large number of Gram-positive bacterial species. The SecA2 substrates are typically linked to the cell wall, but may be lipid-linked, peptidoglycan-linked, or non-covalently associated S-layer proteins. These substrates can have a significant impact on virulence of pathogenic organisms, but may also aid colonization by commensals. The SecA2 orthologues range from being highly similar to their SecA paralogues, to being distinctly different in apparent structure and function. Two broad classes of SecA2 are evident. One transports multiple substrates, and may interact with the general Sec system, or with an as yet unidentified transmembrane channel. The second type transports a single substrate, and is a component of the accessory Sec system, which includes the SecY paralogue SecY2 along with the accessory Sec proteins Asp1-3. Recent studies indicate that the latter three proteins may have a unique role in coordinating post-translational modification of the substrate with transport by SecA2. Comparative functional and phylogenetic analyses suggest that each SecA2 may be uniquely adapted for a specific type of substrate. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey.

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  • SecA2 is found in all species of Mycobacterium, other Actinobacteria, and also in several Gram-positive pathogens.

    “SecA2 is found in all species of Mycobacterium, other Actinobacteria, and also in several Gram-positive pathogens (78, 79).”

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Authors
Bensing, B. A., Seepersaud, R., Yen, Y. T., & Sullam, P. M.
Affiliations
San Francisco VA Medical Center (US)
Corresponding author
Bensing, Barbara A.
Venue
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Publisher
Elsevier BV
Published
2014-08
Volume
1843
Issue
8
Pages
1674-1686
ISSN
0167-4889 (ISSN-L)
OpenAlex
W1993356535
Cited by
68
References
97
Citations by year
2026: 2 · 2025: 3 · 2024: 3 · 2023: 3 · 2022: 4 · 2021: 3 · 2020: 9 · 2019: 12 · 2018: 5 · 2017: 5 · 2016: 7 · 2015: 6 · 2014: 6
FWCI
0.78
Type
journal article
Language
en
Open access
Locations
  • Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • eScholarship (California Digital Library) (submittedVersion)
Funders
  • Department of Veterans Affairs
  • VA Merit Review
  • Northern California Institute for Research and Education
  • NIH (R01-AI41513)
  • American Heart Association (AHA), Western Affiliate
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
  • Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
Keywords
SecA2, SecA, Sec system, bacterial protein secretion, S-layer proteins, peptidoglycan, post-translational modification, Gram-positive bacteria, virulence, commensal colonization, phylogenetic analysis
MeSH terms
SEC Translocation Channels, SecA Proteins, Adenosine Triphosphatases, Bacterial Proteins, Cell Wall, Gram-Positive Bacteria, Membrane Glycoproteins, Phylogeny, Molecular Motor Proteins, Protein Transport, Membrane Transport Proteins

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