A0PXW6 (A0PXW6_CLONN) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 48.
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 RuleBase RU000537 HAMAP-Rule MF_01465 | ||||
| Gene names |
| ||||
| Organism | Clostridium novyi (strain NT) [Complete proteome] [HAMAP] EMBL ABK61359.1 | ||||
| Taxonomic identifier | 386415 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium › ![]() |
Protein attributes
| Sequence length | 424 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. 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 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 |
| 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 | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transmembrane | 17 – 37 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 69 – 89 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 114 – 131 | 18 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 143 – 163 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 165 – 185 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 208 – 228 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 262 – 282 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 306 – 326 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 364 – 384 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
| Transmembrane | 386 – 406 | 21 | Helical; By similarity HAMAP-Rule MF_01465 | ||||||
Sequences
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References
| [1] | "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-NT." Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B., Zhou S. Nat. Biotechnol. 24:1573-1580(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NT. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000382 Genomic DNA. Translation: ABK61359.1. |
| RefSeq | YP_877218.1. NC_008593.1. |
3D structure databases | |
| ProteinModelPortal | A0PXW6. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 386415.NT01CX_1135. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABK61359; ABK61359; NT01CX_1135. |
| GeneID | 4541675. |
| KEGG | cno:NT01CX_1135. |
| PATRIC | 19477932. VBICloNov112828_0245. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0201. |
| HOGENOM | HOG000080586. |
| KO | K03076. |
| OMA | FIMWLGE. |
| ProtClustDB | PRK09204. |
Enzyme and pathway databases | |
| BioCyc | CNOV386415:GH98-356-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 | A0PXW6_CLONN | ||||||||
| Accession | Primary (citable) accession number: A0PXW6 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
