BioReason SFT deep research for secF
Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features
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UniRule transfers provide annotations for protein targeting, protein transport by the Sec complex, and intracellular protein transmembrane transport, all appropriate for SecF.
Combined Automated Annotation using Multiple IEA Methods
Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen
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Reports the complete genome sequence of P. aeruginosa PAO1, which includes the secF gene at ordered locus PA3820.
"Here we report the complete sequence of P. aeruginosa strain PAO1"
Structure and function of a membrane component SecDF that enhances protein export
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Landmark study determining the crystal structure of T. thermophilus SecDF at 3.3 A, revealing a 12-helix TM domain (RND superfamily) and two periplasmic domains. Demonstrates SecDF is a PMF-driven membrane-integrated chaperone for ATP-independent translocation.
"we propose that SecDF functions as a membrane-integrated chaperone, powered by proton motive force, to achieve ATP-independent protein translocation"
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Conserved Asp and Arg residues at the SecD/SecF TM interface are essential for proton conduction and preprotein movement.
"Electrophysiological analyses revealed that SecDF conducts protons in a manner dependent on pH and the presence of an unfolded protein, with conserved Asp and Arg residues at the transmembrane interface between SecD and SecF playing essential roles in the movements of protons and preproteins"
Structure-based working model of SecDF, a proton-driven bacterial protein translocation factor
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Review of SecDF structural studies. SecDF is a protein-translocation motor working independently of SecA, powered by the proton gradient.
"Once SecDF captures the precursor protein on the periplasmic surface, SecDF can complete protein translocation even if SecA function is inactivated by ATP depletion, implying that SecDF is a protein-translocation motor that works independent of SecA"
Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven Protein Secretion Motor SecDF
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I-form crystal structures at 2.6-2.8 A reveal a proton-conducting tunnel in the SecDF transmembrane region regulated by a conserved Asp residue.
"SecDF in I form can generate a tunnel that penetrates the transmembrane region and functions as a proton pathway regulated by a conserved Asp residue"
Membrane protein insertion and proton-motive-force-dependent secretion through the bacterial holo-translocon SecYEG-SecDF-YajC-YidC
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The holo-translocon (HTL) comprising SecYEG-SecDF-YajC-YidC is more effective in co-translational membrane protein insertion and makes post-translational secretion more PMF-dependent.
"It is more effective in cotranslational insertion of membrane proteins and the posttranslational secretion of a beta-barreled outer-membrane protein driven by SecA and ATP becomes much more dependent on the proton-motive force"
Inter-membrane association of the Sec and BAM translocons for bacterial outer-membrane biogenesis
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SecDF periplasmic domains connect the inner membrane Sec machinery to the outer membrane BAM complex, enabling inter-membrane communication driven by PMF.
"the proton-motive force (PMF) across the inner-membrane acts at distinct stages of protein secretion: (1) SecA-driven translocation through SecYEG and (2) communication of conformational changes via SecDF across the periplasm to BAM"
Probing the protein interaction network of Pseudomonas aeruginosa cells by chemical cross-linking mass spectrometry
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In vivo cross-linking in P. aeruginosa directly demonstrates the SecD-SecF physical interaction and provides structural constraints for the complex.
"Structures of three membrane proteins, namely, SecD-SecF, OprF, and OprI are predicted using in vivo cross-linked sites"
Genetic and molecular characterization of the Escherichia coli secD operon and its products
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Characterization of the secD operon in E. coli, establishing that it contains yajC, secD, and secF. SecD and SecF are present at fewer than 30 molecules per cell.
"in addition to secD and secF, it contains the upstream gene yajC ...there are fewer than 30 SecD and SecF molecules per cell"
Electric-Field-Induced Protein Translocation via a Conformational Transition in SecDF: An MD Study.
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Molecular dynamics simulations show that the transmembrane electrical potential lowers the free-energy barrier for the F-form to I-form conformational transition in SecDF, providing a mechanistic link between PMF and SecDF function.
"the interaction of the P1 domain dipole moment with the TM electrical field considerably lowers the free-energy barrier in the direction of F-form to I-form transition"