Q6GEK3 (SECY_STAAR) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 61.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Protein translocase subunit SecY | ||||
| Gene names |
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| Organism | Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 282458 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 430 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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. 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. |
| Subcellular location | Cell membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_01465. |
| Sequence similarities | Belongs to the SecY/SEC61-alpha family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein transport Translocation Transport |
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | intracellular protein transmembrane transport Inferred from electronic annotation. Source: HAMAP protein targetingInferred from electronic annotation. Source: HAMAP protein transport by the Sec complexInferred from electronic annotation. Source: HAMAP |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 430 | 430 | Protein translocase subunit SecY HAMAP-Rule MF_01465 | PRO_0000131743 | |||||
Regions | |||||||||
| Transmembrane | 18 – 38 | 21 | Helical; Potential | ||||||
| Transmembrane | 68 – 88 | 21 | Helical; Potential | ||||||
| Transmembrane | 117 – 137 | 21 | Helical; Potential | ||||||
| Transmembrane | 147 – 167 | 21 | Helical; Potential | ||||||
| Transmembrane | 179 – 199 | 21 | Helical; Potential | ||||||
| Transmembrane | 217 – 237 | 21 | Helical; Potential | ||||||
| Transmembrane | 269 – 289 | 21 | Helical; Potential | ||||||
| Transmembrane | 308 – 328 | 21 | Helical; Potential | ||||||
| Transmembrane | 368 – 388 | 21 | Helical; Potential | ||||||
| Transmembrane | 389 – 409 | 21 | Helical; Potential | ||||||
Sequences
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References
| [1] | "Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C. Parkhill J.Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MRSA252. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX571856 Genomic DNA. Translation: CAG41296.1. |
| RefSeq | YP_041670.1. NC_002952.2. |
3D structure databases | |
| ProteinModelPortal | Q6GEK3. |
| SMR | Q6GEK3. Positions 13-425. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 282458.SAR2315. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAG41296; CAG41296; SAR2315. |
| GeneID | 2859137. |
| KEGG | sar:SAR2315. |
| PATRIC | 19548301. VBIStaAur71814_2327. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0201. |
| HOGENOM | HOG000080586. |
| KO | K03076. |
| OMA | FIMWLGE. |
| ProtClustDB | PRK09204. |
Enzyme and pathway databases | |
| BioCyc | SAUR282458:GJA5-2358-MONOMER. |
Family and domain databases | |
| Gene3D | 1.10.3370.10. 1 hit. |
| HAMAP | MF_01465. SecY. |
| InterPro | IPR026593. SecY. IPR002208. SecY/SEC61-alpha. IPR023201. SecY_su_dom. [Graphical view] |
| PANTHER | PTHR10906. PTHR10906. 1 hit. |
| Pfam | PF00344. SecY. 1 hit. [Graphical view] |
| PIRSF | PIRSF004557. SecY. 1 hit. |
| SUPFAM | SSF103491. SecY. 1 hit. |
| TIGRFAMs | TIGR00967. 3a0501s007. 1 hit. |
| PROSITE | PS00755. SECY_1. 1 hit. PS00756. SECY_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SECY_STAAR | ||||||||
| Accession | Primary (citable) accession number: Q6GEK3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
