O08387 (SECY_STAA8) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 81.
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 |
| ||||
| Organism | Staphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 93061 [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. |
| Sequence caution | The sequence AAB54022.1 differs from that shown. Reason: Frameshift at several positions. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein transport Translocation Transport |
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Technical term | Complete proteome Reference 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_0000131745 | |||||
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 | ||||||
Experimental info | |||||||||
| Sequence conflict | 159 | 1 | A → T in AAB54022. Ref.1 | ||||||
| Sequence conflict | 200 – 202 | 3 | GQT → YQQ in AAB54022. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | Segarra R.A., Iandolo J.J. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: NCTC 8325. |
| [2] | "The Staphylococcus aureus NCTC8325 genome." Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 8325. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U96620 Genomic DNA. Translation: AAB54022.1. Frameshift. CP000253 Genomic DNA. Translation: ABD31510.1. |
| RefSeq | YP_500959.1. NC_007795.1. |
3D structure databases | |
| ProteinModelPortal | O08387. |
| SMR | O08387. Positions 13-425. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 93061.SAOUHSC_02491. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABD31510; ABD31510; SAOUHSC_02491. |
| GeneID | 3920868. |
| KEGG | sao:SAOUHSC_02491. |
| PATRIC | 19582282. VBIStaAur99865_2247. |
Phylogenomic databases | |
| eggNOG | COG0201. |
| HOGENOM | HOG000080586. |
| KO | K03076. |
| OMA | FIMWLGE. |
| ProtClustDB | PRK09204. |
Enzyme and pathway databases | |
| BioCyc | SAUR93061:GIWJ-2427-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_STAA8 | ||||||||
| Accession | Primary (citable) accession number: O08387 Secondary accession number(s): Q2FW26 | ||||||||
| 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
