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Protein

Protein translocase subunit SecE

Gene

secE

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 3 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.

GO - Molecular functioni

Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocase subunit SecEUniRule annotation
Alternative name(s):
Protein transport protein Sec61 gamma subunit homologUniRule annotation
Gene namesi
Name:secEUniRule annotation
Ordered Locus Names:MJ0371
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3636CytoplasmicAdd
BLAST
Transmembranei37 – 6226HelicalAdd
BLAST
Topological domaini63 – 7412ExtracellularAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7474Protein translocase subunit SecEPRO_0000104219Add
BLAST

Interactioni

Subunit structurei

Component of the Sec protein translocase complex. Heterotrimer consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. May interact with SecDF, and other proteins may be involved.1 Publication

Protein-protein interaction databases

IntActiQ57817. 2 interactions.
MINTiMINT-8378567.
STRINGi243232.MJ_0371.

Structurei

Secondary structure

1
74
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 2411Combined sources
Beta strandi25 – 273Combined sources
Helixi31 – 6636Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RH5X-ray3.20B1-74[»]
1RHZX-ray3.50B1-74[»]
2YXQX-ray3.50B1-74[»]
2YXRX-ray3.60B1-74[»]
3BO0electron microscopy9.60B28-67[»]
3BO1electron microscopy9.60B28-67[»]
3DKNelectron microscopy8.70B3-67[»]
4V4Nelectron microscopy9.00A71-67[»]
4V7Ielectron microscopy-B28-67[»]
ProteinModelPortaliQ57817.
SMRiQ57817. Positions 3-67.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ57817.

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG02204. Archaea.
COG2443. LUCA.
InParanoidiQ57817.
KOiK07342.
OMAiVLMISRK.

Family and domain databases

Gene3Di1.20.5.820. 1 hit.
HAMAPiMF_00422. SecE.
InterProiIPR023391. Prot_translocase_SecE_dom.
IPR022943. SecE.
IPR008158. Translocase_Sec61-g.
[Graphical view]
SUPFAMiSSF103456. SSF103456. 1 hit.
TIGRFAMsiTIGR00327. secE_euk_arch. 1 hit.

Sequencei

Sequence statusi: Complete.

Q57817-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTDFNQKIE QLKEFIEECR RVWLVLKKPT KDEYLAVAKV TALGISLLGI
60 70
IGYIIHVPAT YIKGILKPPT TPRV
Length:74
Mass (Da):8,438
Last modified:November 1, 1996 - v1
Checksum:i10474AE938CC0ECD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98360.1.
PIRiC64346.

Genome annotation databases

EnsemblBacteriaiAAB98360; AAB98360; MJ_0371.
KEGGimja:MJ_0371.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98360.1.
PIRiC64346.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RH5X-ray3.20B1-74[»]
1RHZX-ray3.50B1-74[»]
2YXQX-ray3.50B1-74[»]
2YXRX-ray3.60B1-74[»]
3BO0electron microscopy9.60B28-67[»]
3BO1electron microscopy9.60B28-67[»]
3DKNelectron microscopy8.70B3-67[»]
4V4Nelectron microscopy9.00A71-67[»]
4V7Ielectron microscopy-B28-67[»]
ProteinModelPortaliQ57817.
SMRiQ57817. Positions 3-67.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ57817. 2 interactions.
MINTiMINT-8378567.
STRINGi243232.MJ_0371.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98360; AAB98360; MJ_0371.
KEGGimja:MJ_0371.

Phylogenomic databases

eggNOGiarCOG02204. Archaea.
COG2443. LUCA.
InParanoidiQ57817.
KOiK07342.
OMAiVLMISRK.

Miscellaneous databases

EvolutionaryTraceiQ57817.

Family and domain databases

Gene3Di1.20.5.820. 1 hit.
HAMAPiMF_00422. SecE.
InterProiIPR023391. Prot_translocase_SecE_dom.
IPR022943. SecE.
IPR008158. Translocase_Sec61-g.
[Graphical view]
SUPFAMiSSF103456. SSF103456. 1 hit.
TIGRFAMsiTIGR00327. secE_euk_arch. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 11-66 IN COMPLEX WITH SECY AND SECG.
  3. "The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal."
    Li W., Schulman S., Boyd D., Erlandson K., Beckwith J., Rapoport T.A.
    Mol. Cell 26:511-521(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
  4. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (9.6 ANGSTROMS) OF 2-433 DOCKED ONTO THE E.COLI RIBOSOME.
  5. "Single copies of Sec61 and TRAP associate with a nontranslating mammalian ribosome."
    Menetret J.F., Hegde R.S., Aguiar M., Gygi S.P., Park E., Rapoport T.A., Akey C.W.
    Structure 16:1126-1137(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (8.7 ANGSTROMS) OF 3-67 DOCKED ONTO DOG RIBOSOMES.
  6. "Regulation of the protein-conducting channel by a bound ribosome."
    Gumbart J., Trabuco L.G., Schreiner E., Villa E., Schulten K.
    Structure 17:1453-1464(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY OF 28-67 DOCKED ONTO E.COLI RIBOSOMES.

Entry informationi

Entry nameiSECE_METJA
AccessioniPrimary (citable) accession number: Q57817
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 116 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. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.