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P0AG96

- SECE_ECOLI

UniProt

P0AG96 - SECE_ECOLI

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Protein

Protein translocase subunit SecE

Gene

secE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. P-P-bond-hydrolysis-driven protein transmembrane transporter activity Source: InterPro

GO - Biological processi

  1. intracellular protein transmembrane transport Source: EcoliWiki
  2. intracellular protein transport Source: EcoliWiki
  3. protein secretion Source: UniProtKB-HAMAP
  4. protein targeting Source: UniProtKB-HAMAP
  5. protein transport by the Sec complex Source: EcoliWiki
Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciEcoCyc:SECE.
ECOL316407:JW3944-MONOMER.

Protein family/group databases

TCDBi3.A.5.1.1. the general secretory pathway (sec) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocase subunit SecEUniRule annotation
Gene namesi
Name:secEUniRule annotation
Synonyms:prlG
Ordered Locus Names:b3981, JW3944
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10939. secE.

Subcellular locationi

Cell inner membrane 1 PublicationUniRule annotation; Multi-pass membrane protein 1 PublicationUniRule annotation

GO - Cellular componenti

  1. cell envelope Sec protein transport complex Source: EcoCyc
  2. integral component of membrane Source: EcoliWiki
  3. integral component of plasma membrane Source: EcoCyc
  4. intracellular Source: GOC
  5. plasma membrane Source: EcoliWiki
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Essential; deletion experiments lead to loss of the SecYEG tranlocation channel. Leads to loss of translocation of lipoproteins Lpp and BRP (PubMed:15140892) and accumulation of signal peptidase I (lepB) in a soluble fraction (PubMed:21778229).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi120 – 1201S → C: Massive ion flux when cross-linked to SecY C-67 mutation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 127127Protein translocase subunit SecEPRO_0000104163Add
BLAST

Post-translational modificationi

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

Proteomic databases

PaxDbiP0AG96.
PRIDEiP0AG96.

Expressioni

Gene expression databases

GenevestigatoriP0AG96.

Interactioni

Subunit structurei

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.2 Publications

Protein-protein interaction databases

DIPiDIP-59303N.
IntActiP0AG96. 2 interactions.
STRINGi511145.b3981.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP0AG96.
SMRiP0AG96. Positions 12-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG96.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919Cytoplasmic1 PublicationAdd
BLAST
Topological domaini33 – 4816Periplasmic1 PublicationAdd
BLAST
Topological domaini61 – 9737Cytoplasmic1 PublicationAdd
BLAST
Topological domaini116 – 12712Periplasmic1 PublicationAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei20 – 3213HelicalCuratedAdd
BLAST
Transmembranei49 – 6012HelicalCuratedAdd
BLAST
Transmembranei98 – 11518HelicalCuratedAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the SecE/SEC61-gamma family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0690.
HOGENOMiHOG000219148.
InParanoidiP0AG96.
KOiK03073.
OMAiTRPEATQ.
OrthoDBiEOG6DRPR4.

Family and domain databases

HAMAPiMF_00422. SecE.
InterProiIPR022943. SecE.
IPR005807. SecE_bac.
IPR001901. Translocase_SecE/Sec61-g.
[Graphical view]
PfamiPF00584. SecE. 1 hit.
[Graphical view]
PRINTSiPR01650. SECETRNLCASE.
TIGRFAMsiTIGR00964. secE_bact. 1 hit.
PROSITEiPS01067. SECE_SEC61G. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AG96-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSANTEAQGS GRGLEAMKWV VVVALLLVAI VGNYLYRDIM LPLRALAVVI
60 70 80 90 100
LIAAAGGVAL LTTKGKATVA FAREARTEVR KVIWPTRQET LHTTLIVAAV
110 120
TAVMSLILWG LDGILVRLVS FITGLRF
Length:127
Mass (Da):13,643
Last modified:December 20, 2005 - v1
Checksum:i94D37280522875CE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30610 Genomic DNA. Translation: AAA24621.1.
U00006 Genomic DNA. Translation: AAC43079.1.
U00096 Genomic DNA. Translation: AAC76955.1.
AP009048 Genomic DNA. Translation: BAE77339.1.
PIRiA35139. VXECSE.
RefSeqiNP_418408.1. NC_000913.3.
YP_491480.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76955; AAC76955; b3981.
BAE77339; BAE77339; BAE77339.
GeneIDi12930517.
948486.
KEGGiecj:Y75_p3216.
eco:b3981.
PATRICi32123483. VBIEscCol129921_4094.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M30610 Genomic DNA. Translation: AAA24621.1 .
U00006 Genomic DNA. Translation: AAC43079.1 .
U00096 Genomic DNA. Translation: AAC76955.1 .
AP009048 Genomic DNA. Translation: BAE77339.1 .
PIRi A35139. VXECSE.
RefSeqi NP_418408.1. NC_000913.3.
YP_491480.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AKH electron microscopy 14.90 C/Z 17-127 [» ]
2AKI electron microscopy 14.90 C/Z 17-127 [» ]
3J01 electron microscopy - B 12-127 [» ]
3J45 electron microscopy 9.50 E 74-127 [» ]
3J46 electron microscopy 10.10 E 74-127 [» ]
ProteinModelPortali P0AG96.
SMRi P0AG96. Positions 12-127.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-59303N.
IntActi P0AG96. 2 interactions.
STRINGi 511145.b3981.

Protein family/group databases

TCDBi 3.A.5.1.1. the general secretory pathway (sec) family.

Proteomic databases

PaxDbi P0AG96.
PRIDEi P0AG96.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76955 ; AAC76955 ; b3981 .
BAE77339 ; BAE77339 ; BAE77339 .
GeneIDi 12930517.
948486.
KEGGi ecj:Y75_p3216.
eco:b3981.
PATRICi 32123483. VBIEscCol129921_4094.

Organism-specific databases

EchoBASEi EB0932.
EcoGenei EG10939. secE.

Phylogenomic databases

eggNOGi COG0690.
HOGENOMi HOG000219148.
InParanoidi P0AG96.
KOi K03073.
OMAi TRPEATQ.
OrthoDBi EOG6DRPR4.

Enzyme and pathway databases

BioCyci EcoCyc:SECE.
ECOL316407:JW3944-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AG96.
PROi P0AG96.

Gene expression databases

Genevestigatori P0AG96.

Family and domain databases

HAMAPi MF_00422. SecE.
InterProi IPR022943. SecE.
IPR005807. SecE_bac.
IPR001901. Translocase_SecE/Sec61-g.
[Graphical view ]
Pfami PF00584. SecE. 1 hit.
[Graphical view ]
PRINTSi PR01650. SECETRNLCASE.
TIGRFAMsi TIGR00964. secE_bact. 1 hit.
PROSITEi PS01067. SECE_SEC61G. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiSECE_ECOLI
AccessioniPrimary (citable) accession number: P0AG96
Secondary accession number(s): P16920, Q2M8R7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: October 29, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3