0  structures 776  species 0  interactions 2916  sequences 13  architectures

Family: SecD_SecF (PF02355)

Summary

Protein export membrane protein Add an annotation

This family consists of various prokaryotic SecD and SecF protein export membrane proteins. This SecD and SecF proteins are part of the multimeric protein export complex comprising SecA, D, E, F, G, Y, and YajC [1]. SecD and SecF are required to maintain a proton motive force [2].


Literature references

  1. Bolhuis A, Broekhuizen CP, Sorokin A, van Roosmalen ML, Venema G, Bron S, Quax WJ, van Dijl JM; , J Biol Chem 1998;273:21217-21224.: SecDF of Bacillus subtilis, a molecular Siamese twin required for the efficient secretion of proteins. PUBMED:9694879

  2. Arkowitz RA, Wickner W; , EMBO J 1994;13:954-963.: SecD and SecF are required for the proton electrochemical gradient stimulation of preprotein translocation. PUBMED:8112309


InterPro entry IPR003335

Secretion across the inner membrane in some Gram-negative bacteria occurs via the preprotein translocase pathway. Proteins are produced in the cytoplasm as precursors, and require a chaperone subunit to direct them to the translocase component PUBMED:2202721. From there, the mature proteins are either targeted to the outer membrane, or remain as periplasmic proteins. The translocase protein subunits are encoded on the bacterial chromosome.

The translocase itself comprises 7 proteins, including a chaperone protein (SecB), an ATPase (SecA), an integral membrane complex (SecCY, SecE and SecG), and two additional membrane proteins that promote the release of the mature peptide into the periplasm (SecD and SecF) PUBMED:2202721. The chaperone protein SecB PUBMED:11336818 is a highly acidic homotetrameric protein that exists as a "dimer of dimers" in the bacterial cytoplasm. SecB maintains preproteins in an unfolded state after translation, and targets these to the peripheral membrane protein ATPase SecA for secretion PUBMED:10418149. Together with SecY and SecG, SecE forms a multimeric channel through which preproteins are translocated, using both proton motive forces and ATP-driven secretion. The latter is mediated by SecA. The structure of the Escherichia coli SecYEG assembly revealed a sandwich of two membranes interacting through the extensive cytoplasmic domains PUBMED:12167867. Each membrane is composed of dimers of SecYEG. The monomeric complex contains 15 transmembrane helices.

This family consists of various prokaryotic SecD and SecF protein export membrane proteins. The SecD and SecF equivalents of the Gram-positive bacterium Bacillus subtilis are jointly present in one polypeptide, denoted SecDF, that is required to maintain a high capacity for protein secretion. Unlike the SecD subunit of the pre-protein translocase of E. coli, SecDF of B. subtilis was not required for the release of a mature secretory protein from the membrane, indicating that SecDF is involved in earlier translocation steps PUBMED:9694879. Comparison with SecD and SecF proteins from other organisms revealed the presence of 10 conserved regions in SecDF, some of which appear to be important for SecDF function. Interestingly, the SecDF protein of B. subtilis has 12 putative transmembrane domains. Thus, SecDF does not only show sequence similarity but also structural similarity to secondary solute transporters PUBMED:9694879.

Clan

This family is a member of clan RND_permease (CL0322), which contains the following 6 members:

ACR_tran GerA MMPL Patched SecD_SecF Sterol-sensing

Gene Ontology

External database links

Domain organisation

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Alignments

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Full length sequences

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.

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Trees

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Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Pfam-B_844 (release 5.2)
Previous IDs: none
Type: Family
Author: Bashton M, Bateman A
Number in seed: 19
Number in full: 2916
Average length of the domain: 184.50 aa
Average identity of full alignment: 29 %
Average coverage of the sequence by the domain: 34.17 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.5 20.5
Trusted cut-off 20.5 20.5
Noise cut-off 20.4 20.4
Model length: 189
Family (HMM) version: 9
Download: download the raw HMM for this family

Species distribution

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