B1F6N9 (B1F6N9_BACAN) Unreviewed, UniProtKB/TrEMBL
Last modified
April 3, 2013.
Version 33.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Protein translocase subunit SecY HAMAP-Rule MF_01465 | ||||||
| Gene names |
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| Organism | Bacillus anthracis str. A0389 EMBL EDS94559.1 | ||||||
| Taxonomic identifier | 486623 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › ![]() |
Protein attributes
| Sequence length | 433 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 RuleBase RU000537 |
| 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 RuleBase RU003484. |
| Sequence similarities | Belongs to the SecY/SEC61-alpha family. HAMAP-Rule MF_01465 RuleBase RU004349 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein transport Translocation HAMAP-Rule MF_01465 RuleBase RU003484 Transport |
| Cellular component | Cell membrane HAMAP-Rule MF_01465 Membrane |
| Domain | Transmembrane Transmembrane helix HAMAP-Rule MF_01465 |
| 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 | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transmembrane | 18 – 38 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 67 – 87 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 116 – 136 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 146 – 166 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 175 – 195 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 214 – 234 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 273 – 293 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 311 – 331 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 371 – 391 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 393 – 413 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
Sequences
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References
| [1] | "Genome sequence of Bacillus anthracis A0389." Dodson R.J., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., Sutton G., Brettin T.S. Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: A0389 EMBL EDS94559.1. |
| [2] | Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D., Brettin T.S. Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: A0389 EMBL EDS94559.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | ABLB01000062 Genomic DNA. Translation: EDS94559.1. |
3D structure databases | |
| ProteinModelPortal | B1F6N9. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EDS94559; EDS94559; BAK_0152. |
| PATRIC | 24613063. VBIBacAnt25810_5601. |
Phylogenomic databases | |
| OMA | FIMWLGE. |
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 | B1F6N9_BACAN | ||||||||
| Accession | Primary (citable) accession number: B1F6N9 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
