Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protein translocase subunit SecY

Gene

secY

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei75 – 751Pore ring
Sitei79 – 791Pore ring
Sitei174 – 1741Pore ring
Sitei179 – 1791Pore ring
Sitei260 – 2601Pore ring
Sitei406 – 4061Pore ring

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocase subunit SecY
Alternative name(s):
Protein transport protein SEC61 subunit alpha homolog
Gene namesi
Name:secY
Ordered Locus Names:MJ0478
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 – 2828CytoplasmicAdd
BLAST
Transmembranei29 – 4618Helical; Name=Helix 1Add
BLAST
Topological domaini47 – 559Extracellular
Transmembranei56 – 8833Discontinuously helical; Name=Helix 2Add
BLAST
Intramembranei56 – 638Helical; Name=Helix 2A
Intramembranei64 – 696
Intramembranei70 – 8819Helical; Name=Helix 2BAdd
BLAST
Topological domaini89 – 11022CytoplasmicAdd
BLAST
Transmembranei111 – 12919Helical; Name=Helix 3Add
BLAST
Topological domaini130 – 14011ExtracellularAdd
BLAST
Transmembranei141 – 16121Helical; Name=Helix 4Add
BLAST
Topological domaini162 – 1687Cytoplasmic
Transmembranei169 – 19123Helical; Name=Helix 5Add
BLAST
Topological domaini192 – 20918ExtracellularAdd
BLAST
Transmembranei210 – 22718Helical; Name=Helix 6Add
BLAST
Topological domaini228 – 25528CytoplasmicAdd
BLAST
Transmembranei256 – 27722Helical; Name=Helix 7Add
BLAST
Topological domaini278 – 31235ExtracellularAdd
BLAST
Transmembranei313 – 33119Helical; Name=Helix 8Add
BLAST
Topological domaini332 – 38251CytoplasmicAdd
BLAST
Transmembranei383 – 39715Helical; Name=Helix 9Add
BLAST
Topological domaini398 – 3981Extracellular
Transmembranei399 – 41214Helical; Name=Helix 10Add
BLAST
Topological domaini413 – 43624CytoplasmicAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Protein translocase subunit SecYPRO_0000131764Add
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

STRINGi243232.MJ_0478.

Structurei

Secondary structure

1
436
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 106Combined sources
Helixi23 – 4018Combined sources
Helixi54 – 574Combined sources
Helixi59 – 635Combined sources
Turni70 – 756Combined sources
Helixi76 – 9116Combined sources
Helixi101 – 12828Combined sources
Beta strandi131 – 1333Combined sources
Helixi137 – 16428Combined sources
Beta strandi165 – 1673Combined sources
Helixi169 – 18719Combined sources
Helixi192 – 1998Combined sources
Turni200 – 2034Combined sources
Helixi207 – 2093Combined sources
Helixi211 – 22616Combined sources
Beta strandi230 – 2345Combined sources
Beta strandi238 – 2403Combined sources
Beta strandi246 – 2516Combined sources
Helixi253 – 2553Combined sources
Helixi257 – 27721Combined sources
Beta strandi289 – 2957Combined sources
Helixi298 – 3003Combined sources
Beta strandi305 – 3073Combined sources
Helixi313 – 33826Combined sources
Helixi342 – 3487Combined sources
Beta strandi356 – 3594Combined sources
Helixi363 – 39533Combined sources
Helixi402 – 41918Combined sources
Beta strandi427 – 4293Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RH5X-ray3.20A1-436[»]
1RHZX-ray3.50A1-436[»]
2YXQX-ray3.50A1-436[»]
2YXRX-ray3.60A1-436[»]
3BO0electron microscopy9.60A2-433[»]
3BO1electron microscopy9.60A2-433[»]
3DKNelectron microscopy8.70A2-433[»]
4V4Nelectron microscopy9.00AX1-436[»]
4V7Ielectron microscopy-A2-433[»]
ProteinModelPortaliQ60175.
SMRiQ60175. Positions 2-433.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60175.

Family & Domainsi

Sequence similaritiesi

Belongs to the SecY/SEC61-alpha family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG04169. Archaea.
COG0201. LUCA.
InParanoidiQ60175.
KOiK03076.
OMAiRYIPYVT.
PhylomeDBiQ60175.

Family and domain databases

Gene3Di1.10.3370.10. 1 hit.
HAMAPiMF_01465. SecY.
InterProiIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR030659. SecY_CS.
IPR023201. SecY_su_dom.
IPR019561. Translocon_Sec61/SecY_plug_dom.
[Graphical view]
PANTHERiPTHR10906. PTHR10906. 1 hit.
PfamiPF10559. Plug_translocon. 1 hit.
PF00344. SecY. 1 hit.
[Graphical view]
PIRSFiPIRSF004557. SecY. 1 hit.
SUPFAMiSSF103491. SSF103491. 1 hit.
TIGRFAMsiTIGR00967. 3a0501s007. 1 hit.
PROSITEiPS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60175-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLIPILEK IPEVELPVKE ITFKEKLKWT GIVLVLYFIM GCIDVYTAGA
60 70 80 90 100
QIPAIFEFWQ TITASRIGTL ITLGIGPIVT AGIIMQLLVG SGIIQMDLSI
110 120 130 140 150
PENRALFQGC QKLLSIIMCF VEAVLFVGAG AFGILTPLLA FLVIIQIAFG
160 170 180 190 200
SIILIYLDEI VSKYGIGSGI GLFIAAGVSQ TIFVGALGPE GYLWKFLNSL
210 220 230 240 250
IQGVPNIEYI APIIGTIIVF LMVVYAECMR VEIPLAHGRI KGAVGKYPIK
260 270 280 290 300
FVYVSNIPVI LAAALFANIQ LWGLALYRMG IPILGHYEGG RAVDGIAYYL
310 320 330 340 350
STPYGLSSVI SDPIHAIVYM IAMIITCVMF GIFWVETTGL DPKSMAKRIG
360 370 380 390 400
SLGMAIKGFR KSEKAIEHRL KRYIPPLTVM SSAFVGFLAT IANFIGALGG
410 420 430
GTGVLLTVSI VYRMYEQLLR EKVSELHPAI AKLLNK
Length:436
Mass (Da):47,444
Last modified:December 15, 1998 - v2
Checksum:i3E67747A7B5BDC0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98469.1.

Genome annotation databases

EnsemblBacteriaiAAB98469; AAB98469; MJ_0478.
KEGGimja:MJ_0478.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98469.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RH5X-ray3.20A1-436[»]
1RHZX-ray3.50A1-436[»]
2YXQX-ray3.50A1-436[»]
2YXRX-ray3.60A1-436[»]
3BO0electron microscopy9.60A2-433[»]
3BO1electron microscopy9.60A2-433[»]
3DKNelectron microscopy8.70A2-433[»]
4V4Nelectron microscopy9.00AX1-436[»]
4V7Ielectron microscopy-A2-433[»]
ProteinModelPortaliQ60175.
SMRiQ60175. Positions 2-433.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_0478.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98469; AAB98469; MJ_0478.
KEGGimja:MJ_0478.

Phylogenomic databases

eggNOGiarCOG04169. Archaea.
COG0201. LUCA.
InParanoidiQ60175.
KOiK03076.
OMAiRYIPYVT.
PhylomeDBiQ60175.

Miscellaneous databases

EvolutionaryTraceiQ60175.

Family and domain databases

Gene3Di1.10.3370.10. 1 hit.
HAMAPiMF_01465. SecY.
InterProiIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR030659. SecY_CS.
IPR023201. SecY_su_dom.
IPR019561. Translocon_Sec61/SecY_plug_dom.
[Graphical view]
PANTHERiPTHR10906. PTHR10906. 1 hit.
PfamiPF10559. Plug_translocon. 1 hit.
PF00344. SecY. 1 hit.
[Graphical view]
PIRSFiPIRSF004557. SecY. 1 hit.
SUPFAMiSSF103491. SSF103491. 1 hit.
TIGRFAMsiTIGR00967. 3a0501s007. 1 hit.
PROSITEiPS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view]
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 1-423 IN COMPLEX WITH SECE 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) OF PLUG DELETION MUTANTS.
  4. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (9.6 ANGSTROMS) OF 2-433 DOCKED ONTO E.COLI RIBOSOMES.
  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 2-433 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 2-433 DOCKED ONTO E.COLI RIBOSOMES.

Entry informationi

Entry nameiSECY_METJA
AccessioniPrimary (citable) accession number: Q60175
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 1998
Last modified: November 11, 2015
This is version 111 of the entry and version 2 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.