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Protein

Protein translocase subunit SecY

Gene

secY

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.UniRule annotation

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Translocation, Transport

Enzyme and pathway databases

BioCyciMTHE187420:GJNM-26-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocase subunit SecYUniRule annotation
Alternative name(s):
Protein transport protein SEC61 subunit alpha homologUniRule annotation
Gene namesi
Name:secYUniRule annotation
Ordered Locus Names:MTH_26
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000005223 Componenti: Chromosome

Subcellular locationi

  • Cell membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2121CytoplasmicBy similarityAdd
BLAST
Transmembranei22 – 4827Helical; Name=Helix 1UniRule annotationAdd
BLAST
Topological domaini49 – 5911ExtracellularBy similarityAdd
BLAST
Transmembranei60 – 8829Discontinuously helical; Name=Helix 2By similarityAdd
BLAST
Intramembranei60 – 678Helical; Name=Helix 2ABy similarity
Intramembranei68 – 7912By similarityAdd
BLAST
Intramembranei80 – 889Helical; Name=Helix 2BBy similarity
Topological domaini89 – 10921CytoplasmicBy similarityAdd
BLAST
Transmembranei110 – 13425Helical; Name=Helix 3UniRule annotationAdd
BLAST
Topological domaini135 – 1417ExtracellularBy similarity
Transmembranei142 – 16625Helical; Name=Helix 4UniRule annotationAdd
BLAST
Topological domaini167 – 1726CytoplasmicBy similarity
Transmembranei173 – 19119Helical; Name=Helix 5UniRule annotationAdd
BLAST
Topological domaini192 – 22433ExtracellularBy similarityAdd
BLAST
Transmembranei225 – 24622Helical; Name=Helix 6UniRule annotationAdd
BLAST
Topological domaini247 – 27529CytoplasmicBy similarityAdd
BLAST
Transmembranei276 – 29722Helical; Name=Helix 7UniRule annotationAdd
BLAST
Topological domaini298 – 33437ExtracellularBy similarityAdd
BLAST
Transmembranei335 – 35420Helical; Name=Helix 8UniRule annotationAdd
BLAST
Topological domaini355 – 39743CytoplasmicBy similarityAdd
BLAST
Transmembranei398 – 41619Helical; Name=Helix 9UniRule annotationAdd
BLAST
Topological domaini417 – 4193ExtracellularBy similarity
Transmembranei420 – 43415Helical; Name=Helix 10UniRule annotationAdd
BLAST
Topological domaini435 – 45622CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456Protein translocase subunit SecYPRO_0000131765Add
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.UniRule annotation

Protein-protein interaction databases

STRINGi187420.MTH26.

Structurei

3D structure databases

ProteinModelPortaliO26134.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SecY/SEC61-alpha family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiarCOG04169. Archaea.
COG0201. LUCA.
OMAiRYIPYVT.

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.

O26134-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEQLKEKFEP LFSVLPQVKS PGYRVPFREK LKWTGIILVL YFFLAQIPLY
60 70 80 90 100
GLSANAVDQF AQFRAVLAGN FGSILTLGIG PIVSASIILQ LLVGGKILKL
110 120 130 140 150
DLSRHEDKAF FQGLQKLLAI VFTFFEALIF VLTGSLAPSA PQFVWVLILQ
160 170 180 190 200
LTIGGILIIF LDEVVSKWGF GSGVGLFIAA GVSQEIIVGA FNPLSAPTQP
210 220 230 240 250
GVPAGRITGF LYLLFTGQSP DFQYYVLPVL ALIAVFLVVV YAESMRVEIP
260 270 280 290 300
ISMGGGKRLS RGAVGKYPLR FIYASNMPVI LTSALLLNVQ LLANVFQKLG
310 320 330 340 350
YPILGTVSNG QAVDGLAYLL TAPRSIDALI LDPFRVVFYA VVFIGLCVLF
360 370 380 390 400
AWLWVEISNI GPRHVARQLY QMGMQIPGFR SSRGQFEKIL KRYIPTITIL
410 420 430 440 450
GGAFVGLLAF VADLTGSLGG GTGVLLTVGI VYRLYEEIAQ EQLMDMHPIL

RSFLGD
Length:456
Mass (Da):49,790
Last modified:January 1, 1998 - v1
Checksum:i134C8FBF97251859
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB84535.1.
PIRiF69132.

Genome annotation databases

EnsemblBacteriaiAAB84535; AAB84535; MTH_26.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB84535.1.
PIRiF69132.

3D structure databases

ProteinModelPortaliO26134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi187420.MTH26.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB84535; AAB84535; MTH_26.

Phylogenomic databases

eggNOGiarCOG04169. Archaea.
COG0201. LUCA.
OMAiRYIPYVT.

Enzyme and pathway databases

BioCyciMTHE187420:GJNM-26-MONOMER.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H.

Entry informationi

Entry nameiSECY_METTH
AccessioniPrimary (citable) accession number: O26134
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 1, 1998
Last modified: December 9, 2015
This is version 105 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

Complete proteome, Reference proteome

Documents

  1. 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.