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Protein

Protein translocase subunit SecY

Gene

secY

Organism
Corynebacterium glutamicum (strain R)
Status
Unreviewed-Annotation score: Annotation score: 2 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

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

Keywords - Biological processi

Protein transport, TranslocationUniRule annotation, Transport

Enzyme and pathway databases

BioCyciCGLU340322:GJBE-700-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein translocase subunit SecYUniRule annotation
Gene namesi
Name:secYUniRule annotation
Ordered Locus Names:cgR_0668Imported
OrganismiCorynebacterium glutamicum (strain R)Imported
Taxonomic identifieri340322 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000006698: Chromosome

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei17 – 3721HelicalUniRule annotationAdd
BLAST
Transmembranei74 – 9421HelicalUniRule annotationAdd
BLAST
Transmembranei116 – 13520HelicalUniRule annotationAdd
BLAST
Transmembranei155 – 17521HelicalUniRule annotationAdd
BLAST
Transmembranei178 – 19821HelicalUniRule annotationAdd
BLAST
Transmembranei213 – 23321HelicalUniRule annotationAdd
BLAST
Transmembranei270 – 29021HelicalUniRule annotationAdd
BLAST
Transmembranei316 – 33621HelicalUniRule annotationAdd
BLAST
Transmembranei374 – 39421HelicalUniRule annotationAdd
BLAST
Transmembranei403 – 42321HelicalUniRule annotationAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. intracellular Source: GOC
  3. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membraneUniRule annotation, Membrane

Interactioni

Subunit structurei

Component of the Sec protein translocase complex. Heterotrimer consisting of SecY, SecE and SecG subunits. The heterotrimers can form oligomers, although 1 heterotrimer is thought to be able to translocate proteins. Interacts with the ribosome. Interacts with SecDF, and other proteins may be involved. Interacts with SecA.UniRule annotation

Protein-protein interaction databases

STRINGi340322.cgR_0668.

Structurei

3D structure databases

ProteinModelPortaliA4QBP2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helixUniRule annotation

Phylogenomic databases

eggNOGiCOG0201.
HOGENOMiHOG000080586.
KOiK03076.
OMAiQTYVISQ.
OrthoDBiEOG651SWP.

Family and domain databases

Gene3Di1.10.3370.10. 1 hit.
HAMAPiMF_01465. SecY.
InterProiIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR023201. SecY_su_dom.
[Graphical view]
PANTHERiPTHR10906. PTHR10906. 1 hit.
PfamiPF00344. 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.

A4QBP2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAIIQAFKD ADLRKKIFFT IAMIVLYRIG AQIPSPGVDY ATISGRLRDL
60 70 80 90 100
TQDQSSVYSL INLFSGGALL QLSIFAIGIM PYITASIIVQ LLTVVIPHFE
110 120 130 140 150
ELKKEGQSGQ AKMMQYTRYL TVALALLQSS GIVALADREQ LLGAGIRVLS
160 170 180 190 200
ADRNFFDLIV LVITMTAGAV LVMWMGELIT EKGVGNGMSL LIFAGIATRL
210 220 230 240 250
PTDGMNILGN SGGVVFAVVL ASVLILVIGV VFVEQGQRRI PVQYAKRMVG
260 270 280 290 300
RRQYGGSSTY LPLKVNQAGV IPVIFASSLI YMPVLITQIV NSGSLEVSDN
310 320 330 340 350
WWQRNIIAHL QTPSSWQYIV LYFALTIFFS YFYVSVQYDP AEQAENMKKY
360 370 380 390 400
GGFIPGIRPG RPTAEYLGFV MNRLLFVGSL YLAVIAVLPN IMLDLGVDAG
410 420 430 440
SAGATPFGGT AILILVSVAL TTVKQIESQL LQSNYEGLLK
Length:440
Mass (Da):47,903
Last modified:May 15, 2007 - v1
Checksum:i3C8871F57A6825E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009044 Genomic DNA. Translation: BAF53639.1.
RefSeqiYP_001137541.1. NC_009342.1.

Genome annotation databases

EnsemblBacteriaiBAF53639; BAF53639; cgR_0668.
GeneIDi4992289.
KEGGicgt:cgR_0668.
PATRICi21505843. VBICorGlu58097_0696.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009044 Genomic DNA. Translation: BAF53639.1.
RefSeqiYP_001137541.1. NC_009342.1.

3D structure databases

ProteinModelPortaliA4QBP2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi340322.cgR_0668.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF53639; BAF53639; cgR_0668.
GeneIDi4992289.
KEGGicgt:cgR_0668.
PATRICi21505843. VBICorGlu58097_0696.

Phylogenomic databases

eggNOGiCOG0201.
HOGENOMiHOG000080586.
KOiK03076.
OMAiQTYVISQ.
OrthoDBiEOG651SWP.

Enzyme and pathway databases

BioCyciCGLU340322:GJBE-700-MONOMER.

Family and domain databases

Gene3Di1.10.3370.10. 1 hit.
HAMAPiMF_01465. SecY.
InterProiIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR023201. SecY_su_dom.
[Graphical view]
PANTHERiPTHR10906. PTHR10906. 1 hit.
PfamiPF00344. 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. "Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R."
    Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M., Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.
    Microbiology 153:1042-1058(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: RImported.

Entry informationi

Entry nameiA4QBP2_CORGB
AccessioniPrimary (citable) accession number: A4QBP2
Entry historyi
Integrated into UniProtKB/TrEMBL: May 15, 2007
Last sequence update: May 15, 2007
Last modified: January 7, 2015
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

External Data

Dasty 3

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 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.