Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0AG96 (SECE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein translocase subunit SecE
Gene names
Name:secE
Synonyms:prlG
Ordered Locus Names:b3981, JW3944
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length127 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of SecY. Ref.9

Subunit structure

Part of the essential Sec protein translocation complex which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and YidC/OxaA. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. The channel interacts with SecA via subunit SecY. SecE might contact ribosomal protein L23 and/or L29 when the translocation complex is docked with the ribosome. Ref.7 Ref.8

Subcellular location

Cell inner membrane; Multi-pass membrane protein Ref.10.

Post-translational modification

Degraded by FtsH when the SecYEG complex is jammed or upon treatment with antibiotics that block translation elongation such as chloramphenicol. HAMAP-Rule MF_00422

Disruption phenotype

Essential; deletion experiments lead to loss of the SecYEG tranlocation channel. Leads to loss of translocation of lipoproteins Lpp and BRP (Ref.9) and accumulation of signal peptidase I (lepB) in a soluble fraction (Ref.14). Ref.9 Ref.14

Sequence similarities

Belongs to the SecE/SEC61-gamma family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 127127Protein translocase subunit SecE HAMAP-Rule MF_00422
PRO_0000104163

Regions

Topological domain1 – 1919Cytoplasmic Probable
Transmembrane20 – 3213Helical; Probable
Topological domain33 – 4816Periplasmic Probable
Transmembrane49 – 6012Helical; Probable
Topological domain61 – 9737Cytoplasmic Probable
Transmembrane98 – 11518Helical; Probable
Topological domain116 – 12712Periplasmic Probable

Experimental info

Mutagenesis1201S → C: Massive ion flux when cross-linked to SecY C-67 mutation. Ref.12

Sequences

Sequence LengthMass (Da)Tools
P0AG96 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 94D37280522875CE

FASTA12713,643
        10         20         30         40         50         60 
MSANTEAQGS GRGLEAMKWV VVVALLLVAI VGNYLYRDIM LPLRALAVVI LIAAAGGVAL 

        70         80         90        100        110        120 
LTTKGKATVA FAREARTEVR KVIWPTRQET LHTTLIVAAV TAVMSLILWG LDGILVRLVS 


FITGLRF 

« Hide

References

« Hide 'large scale' references
[1]"The secE gene encodes an integral membrane protein required for protein export in Escherichia coli."
Schatz P.J., Riggs P.D., Jacq A., Fath M.J., Beckwith J.
Genes Dev. 3:1035-1044(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence and transcriptional pattern of the essential Escherichia coli secE-nusG operon."
Downing W.L., Sullivan S.L., Gottesman M.E., Dennis P.P.
J. Bacteriol. 172:1621-1627(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery."
Schatz P.J., Bieker K.L., Ottemann K.M., Silhavy T.J., Beckwith J.
EMBO J. 10:1749-1757(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY.
[7]"Evaluating the oligomeric state of SecYEG in preprotein translocase."
Yahr T.L., Wickner W.T.
EMBO J. 19:4393-4401(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[8]"SecYEG assembles into a tetramer to form the active protein translocation channel."
Manting E.H., van Der Does C., Remigy H., Engel A., Driessen A.J.
EMBO J. 19:852-861(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[9]"Targeting and translocation of two lipoproteins in Escherichia coli via the SRP/Sec/YidC pathway."
Froderberg L., Houben E.N., Baars L., Luirink J., de Gier J.W.
J. Biol. Chem. 279:31026-31032(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN LIPOPROTEIN EXPORT, DISRUPTION PHENOTYPE.
[10]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: K12 / MG1655 / ATCC 47076.
[11]"The allele-specific synthetic lethality of prlA-prlG double mutants predicts interactive domains of SecY and SecE."
Flower A.M., Osborne R.S., Silhavy T.J.
EMBO J. 14:884-893(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTANTS.
[12]"Determining the conductance of the SecY protein translocation channel for small molecules."
Saparov S.M., Erlandson K., Cannon K., Schaletzky J., Schulman S., Rapoport T.A., Pohl P.
Mol. Cell 26:501-509(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF CHANNEL OPENING, MUTAGENESIS OF SER-120.
[13]"Effects of antibiotics and a proto-oncogene homolog on destruction of protein translocator SecY."
van Stelten J., Silva F., Belin D., Silhavy T.J.
Science 325:753-756(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: COMPLEX DEGRADATION.
Strain: K12 / MC4100.
[14]"Membrane localization of small proteins in Escherichia coli."
Fontaine F., Fuchs R.T., Storz G.
J. Biol. Chem. 286:32464-32474(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
Strain: K12 / MG1655 / ATCC 47076.
[15]"Structure of the E. coli protein-conducting channel bound to a translating ribosome."
Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III, Ban N., Frank J.
Nature 438:318-324(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (14.9 ANGSTROMS) OF 17-127 IN COMPLEX WITH THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAIN.
Strain: MRE-600.
[16]"Cryo-EM structure of the ribosome-SecYE complex in the membrane environment."
Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M., Beatrix B., Mielke T., Berninghausen O., Becker T., Schulten K., Beckmann R.
Nat. Struct. Mol. Biol. 18:614-621(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH THE RIBOSOME AND A NASCENT POLYPEPTIDE CHAIN.
[17]"Protein translocation across the bacterial cytoplasmic membrane."
Driessen A.J., Nouwen N.
Annu. Rev. Biochem. 77:643-667(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M30610 Genomic DNA. Translation: AAA24621.1.
U00006 Genomic DNA. Translation: AAC43079.1.
U00096 Genomic DNA. Translation: AAC76955.1.
AP009048 Genomic DNA. Translation: BAE77339.1.
PIRVXECSE. A35139.
RefSeqNP_418408.1. NC_000913.3.
YP_491480.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AKHelectron microscopy14.90C/Z17-127[»]
2AKIelectron microscopy14.90C/Z17-127[»]
3J01electron microscopy-B12-127[»]
3J45electron microscopy9.50E74-127[»]
3J46electron microscopy10.10E74-127[»]
ProteinModelPortalP0AG96.
SMRP0AG96. Positions 12-127.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59303N.
IntActP0AG96. 2 interactions.
STRING511145.b3981.

Protein family/group databases

TCDB3.A.5.1.1. the general secretory pathway (sec) family.

Proteomic databases

PaxDbP0AG96.
PRIDEP0AG96.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76955; AAC76955; b3981.
BAE77339; BAE77339; BAE77339.
GeneID12930517.
948486.
KEGGecj:Y75_p3216.
eco:b3981.
PATRIC32123483. VBIEscCol129921_4094.

Organism-specific databases

EchoBASEEB0932.
EcoGeneEG10939. secE.

Phylogenomic databases

eggNOGCOG0690.
HOGENOMHOG000219148.
KOK03073.
OMATRPEATQ.
OrthoDBEOG6DRPR4.
ProtClustDBPRK05740.

Enzyme and pathway databases

BioCycEcoCyc:SECE.
ECOL316407:JW3944-MONOMER.

Gene expression databases

GenevestigatorP0AG96.

Family and domain databases

HAMAPMF_00422. SecE.
InterProIPR022943. SecE.
IPR005807. SecE_bac.
IPR001901. Translocase_SecE/Sec61-g.
[Graphical view]
PfamPF00584. SecE. 1 hit.
[Graphical view]
PRINTSPR01650. SECETRNLCASE.
TIGRFAMsTIGR00964. secE_bact. 1 hit.
PROSITEPS01067. SECE_SEC61G. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AG96.
PROP0AG96.

Entry information

Entry nameSECE_ECOLI
AccessionPrimary (citable) accession number: P0AG96
Secondary accession number(s): P16920, Q2M8R7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene