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A4QBP2 (A4QBP2_CORGB) Unreviewed, UniProtKB/TrEMBL

Last modified May 14, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Protein translocase subunit SecY RuleBase RU000537 HAMAP-Rule MF_01465
Gene names
Name:secY HAMAP-Rule MF_01465
Ordered Locus Names:cgR_0668 EMBL BAF53639.1
OrganismCorynebacterium glutamicum (strain R) [Complete proteome] [HAMAP] EMBL BAF53639.1
Taxonomic identifier340322 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length440 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. RuleBase RU000537 HAMAP-Rule MF_01465

Subunit structure

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 By similarity. HAMAP-Rule MF_01465

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01465.

Membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the SecY/SEC61-alpha family. HAMAP-Rule MF_01465 RuleBase RU004349

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Transmembrane17 – 3721Helical; By similarity HAMAP-Rule MF_01465
Transmembrane74 – 9421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane116 – 13520Helical; By similarity HAMAP-Rule MF_01465
Transmembrane155 – 17521Helical; By similarity HAMAP-Rule MF_01465
Transmembrane178 – 19821Helical; By similarity HAMAP-Rule MF_01465
Transmembrane213 – 23321Helical; By similarity HAMAP-Rule MF_01465
Transmembrane270 – 29021Helical; By similarity HAMAP-Rule MF_01465
Transmembrane316 – 33621Helical; By similarity HAMAP-Rule MF_01465
Transmembrane374 – 39421Helical; By similarity HAMAP-Rule MF_01465
Transmembrane403 – 42321Helical; By similarity HAMAP-Rule MF_01465

Sequences

Sequence LengthMass (Da)Tools
A4QBP2 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 3C8871F57A6825E2

FASTA44047,903
        10         20         30         40         50         60 
MSAIIQAFKD ADLRKKIFFT IAMIVLYRIG AQIPSPGVDY ATISGRLRDL TQDQSSVYSL 

        70         80         90        100        110        120 
INLFSGGALL QLSIFAIGIM PYITASIIVQ LLTVVIPHFE ELKKEGQSGQ AKMMQYTRYL 

       130        140        150        160        170        180 
TVALALLQSS GIVALADREQ LLGAGIRVLS ADRNFFDLIV LVITMTAGAV LVMWMGELIT 

       190        200        210        220        230        240 
EKGVGNGMSL LIFAGIATRL PTDGMNILGN SGGVVFAVVL ASVLILVIGV VFVEQGQRRI 

       250        260        270        280        290        300 
PVQYAKRMVG RRQYGGSSTY LPLKVNQAGV IPVIFASSLI YMPVLITQIV NSGSLEVSDN 

       310        320        330        340        350        360 
WWQRNIIAHL QTPSSWQYIV LYFALTIFFS YFYVSVQYDP AEQAENMKKY GGFIPGIRPG 

       370        380        390        400        410        420 
RPTAEYLGFV MNRLLFVGSL YLAVIAVLPN IMLDLGVDAG SAGATPFGGT AILILVSVAL 

       430        440 
TTVKQIESQL LQSNYEGLLK 

« Hide

References

[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: R EMBL BAF53639.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009044 Genomic DNA. Translation: BAF53639.1.
RefSeqYP_001137541.1. NC_009342.1.

3D structure databases

ProteinModelPortalA4QBP2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING340322.cgR_0668.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF53639; BAF53639; cgR_0668.
GeneID4992289.
KEGGcgt:cgR_0668.
PATRIC21505843. VBICorGlu58097_0696.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0201.
HOGENOMHOG000080586.
KOK03076.
OMAAWNVQFY.
OrthoDBEOG651SWP.

Enzyme and pathway databases

BioCycCGLU340322:GJBE-700-MONOMER.

Family and domain databases

Gene3D1.10.3370.10. 1 hit.
HAMAPMF_01465. SecY.
InterProIPR026593. SecY.
IPR002208. SecY/SEC61-alpha.
IPR023201. SecY_su_dom.
[Graphical view]
PANTHERPTHR10906. PTHR10906. 1 hit.
PfamPF00344. SecY. 1 hit.
[Graphical view]
PIRSFPIRSF004557. SecY. 1 hit.
SUPFAMSSF103491. SSF103491. 1 hit.
TIGRFAMsTIGR00967. 3a0501s007. 1 hit.
PROSITEPS00755. SECY_1. 1 hit.
PS00756. SECY_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA4QBP2_CORGB
AccessionPrimary (citable) accession number: A4QBP2
Entry history
Integrated into UniProtKB/TrEMBL: May 15, 2007
Last sequence update: May 15, 2007
Last modified: May 14, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)