P0AGA2 · SECY_ECOLI
- ProteinProtein translocase subunit SecY
- GenesecY
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids443 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. SecY is required to insert newly synthesized SecY into the inner membrane. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true, overexpression also results in FtsH-mediated degradation of SecY.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell envelope Sec protein transport complex | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Molecular Function | protein transmembrane transporter activity | |
Molecular Function | signal sequence binding | |
Biological Process | intracellular protein transmembrane transport | |
Biological Process | intracellular protein transport | |
Biological Process | protein insertion into membrane from inner side | |
Biological Process | protein transport by the Sec complex | |
Biological Process | SRP-dependent cotranslational protein targeting to membrane, translocation |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProtein translocase subunit SecY
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0AGA2
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-22 | Cytoplasmic | ||||
Sequence: MAKQPGLDFQSAKGGLGELKRR | ||||||
Transmembrane | 23-35 | Helical; Name=1 | ||||
Sequence: LLFVIGALIVFRI | ||||||
Topological domain | 36-60 | Periplasmic | ||||
Sequence: GSFIPIPGIDAAVLAKLLEQQRGTI | ||||||
Intramembrane | 61-70 | Helical; Name=Helix 2A | ||||
Sequence: IEMFNMFSGG | ||||||
Transmembrane | 61-96 | Discontinuously helical; Name=2 | ||||
Sequence: IEMFNMFSGGALSRASIFALGIMPYISASIIIQLLT | ||||||
Intramembrane | 71-76 | |||||
Sequence: ALSRAS | ||||||
Intramembrane | 77-96 | Helical; Name=Helix 2B | ||||
Sequence: IFALGIMPYISASIIIQLLT | ||||||
Topological domain | 97-115 | Cytoplasmic | ||||
Sequence: VVHPTLAEIKKEGESGRRK | ||||||
Transmembrane | 116-131 | Helical; Name=3 | ||||
Sequence: ISQYTRYGTLVLAIFQ | ||||||
Topological domain | 132-164 | Periplasmic | ||||
Sequence: SIGIATGLPNMPGMQGLVINPGFAFYFTAVVSL | ||||||
Transmembrane | 165-178 | Helical; Name=4 | ||||
Sequence: VTGTMFLMWLGEQI | ||||||
Topological domain | 179-183 | Cytoplasmic | ||||
Sequence: TERGI | ||||||
Transmembrane | 184-200 | Helical; Name=5 | ||||
Sequence: GNGISIIIFAGIVAGLP | ||||||
Topological domain | 201-223 | Periplasmic | ||||
Sequence: PAIAHTIEQARQGDLHFLVLLLV | ||||||
Transmembrane | 224-237 | Helical; Name=6 | ||||
Sequence: AVLVFAVTFFVVFV | ||||||
Topological domain | 238-273 | Cytoplasmic | ||||
Sequence: ERGQRRIVVNYAKRQQGRRVYAAQSTHLPLKVNMAG | ||||||
Transmembrane | 274-287 | Helical; Name=7 | ||||
Sequence: VIPAIFASSIILFP | ||||||
Topological domain | 288-313 | Periplasmic | ||||
Sequence: ATIASWFGGGTGWNWLTTISLYLQPG | ||||||
Transmembrane | 314-329 | Helical; Name=8 | ||||
Sequence: QPLYVLLYASAIIFFC | ||||||
Topological domain | 330-380 | Cytoplasmic | ||||
Sequence: FFYTALVFNPRETADNLKKSGAFVPGIRPGEQTAKYIDKVMTRLTLVGALY | ||||||
Transmembrane | 381-395 | Helical; Name=9 | ||||
Sequence: ITFICLIPEFMRDAM | ||||||
Topological domain | 396 | Periplasmic | ||||
Sequence: K | ||||||
Transmembrane | 397-413 | Helical; Name=10 | ||||
Sequence: VPFYFGGTSLLIVVVVI | ||||||
Topological domain | 414-443 | Cytoplasmic | ||||
Sequence: MDFMAQVQTLMMSSQYESALKKANLKGYGR |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 40 | In secY100; temperature-sensitive. | ||||
Sequence: P → S | ||||||
Mutagenesis | 60-74 | Some loss of viability, supports protein translocation; strongly suppresses defective and missing signal sequences; transient transmembrane channels open. | ||||
Sequence: Missing | ||||||
Mutagenesis | 65-70 | Grows almost as well as wild-type, supports protein translocation; strongly suppresses defective and missing signal sequences; transient transmembrane channels open. | ||||
Sequence: Missing | ||||||
Mutagenesis | 67 | In prlA3; altered signal sequence interaction, transient channel opening and closing in presence of oxidant; massive ion flux when cross-linked to SecEC-120 mutation. | ||||
Sequence: F → C | ||||||
Mutagenesis | 167 | In secY100; temperature-sensitive. | ||||
Sequence: G → E | ||||||
Mutagenesis | 240 | In secY24; temperature-sensitive at 42 degrees Celsius, impairs interaction with SecE even at 30 degrees in vitro. | ||||
Sequence: G → D | ||||||
Mutagenesis | 282 | In prlA401; altered signal sequence interaction, transient transmembrane channels open. | ||||
Sequence: S → R | ||||||
Mutagenesis | 286 | In prlA4-1; altered signal sequence interaction. | ||||
Sequence: F → Y | ||||||
Mutagenesis | 287 | In secY161; altered signal sequence interaction. | ||||
Sequence: P → L | ||||||
Mutagenesis | 290 | In secY121; altered signal sequence interaction. | ||||
Sequence: I → T | ||||||
Mutagenesis | 357 | In secY39; cold-sensitive. | ||||
Sequence: R → H | ||||||
Mutagenesis | 363 | In secY40; cold-sensitive. | ||||
Sequence: A → S | ||||||
Mutagenesis | 408 | In prlA4-2; altered signal sequence interaction. | ||||
Sequence: I → N | ||||||
Mutagenesis | 424-443 | No longer complements secY24, a temperature-sensitive secY mutation. | ||||
Sequence: Missing |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000131721 | 1-443 | Protein translocase subunit SecY | |||
Sequence: MAKQPGLDFQSAKGGLGELKRRLLFVIGALIVFRIGSFIPIPGIDAAVLAKLLEQQRGTIIEMFNMFSGGALSRASIFALGIMPYISASIIIQLLTVVHPTLAEIKKEGESGRRKISQYTRYGTLVLAIFQSIGIATGLPNMPGMQGLVINPGFAFYFTAVVSLVTGTMFLMWLGEQITERGIGNGISIIIFAGIVAGLPPAIAHTIEQARQGDLHFLVLLLVAVLVFAVTFFVVFVERGQRRIVVNYAKRQQGRRVYAAQSTHLPLKVNMAGVIPAIFASSIILFPATIASWFGGGTGWNWLTTISLYLQPGQPLYVLLYASAIIFFCFFYTALVFNPRETADNLKKSGAFVPGIRPGEQTAKYIDKVMTRLTLVGALYITFICLIPEFMRDAMKVPFYFGGTSLLIVVVVIMDFMAQVQTLMMSSQYESALKKANLKGYGR |
Post-translational modification
SecY that is not part of the protein translocation apparatus is degraded by FtsH. Also degraded by FtsH when the SecYEG complex is jammed, or upon treatment with antibiotics that block translation elongation such as chloramphenicol.
Proteomic databases
Interaction
Subunit
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-YajC and YidC; YidC interacts with nascent inner membrane proteins after SecY. The SecDF-YidC-YajC translocase forms a supercomplex with SecYEG, called the holo-translocon (HTL) (PubMed:27435098).
The stoichiometry of the super complex may be SecYEG:YidC:SecDF 4:3:1, YajC is in the reconstituted complex (with SecDF) but as no antibody is available it could not be quantified (PubMed:27435098).
SecY probably contacts the 23S rRNA and possibly also ribosomal protein L23 during ribosome docking. A single SecY molecule forms the translocating pore, although interaction with SecA may require oligomers
The stoichiometry of the super complex may be SecYEG:YidC:SecDF 4:3:1, YajC is in the reconstituted complex (with SecDF) but as no antibody is available it could not be quantified (PubMed:27435098).
SecY probably contacts the 23S rRNA and possibly also ribosomal protein L23 during ribosome docking. A single SecY molecule forms the translocating pore, although interaction with SecA may require oligomers
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P0AGA2 | ompA P0A910 | 2 | EBI-761422, EBI-371347 | |
BINARY | P0AGA2 | secA P10408 | 6 | EBI-761422, EBI-543213 | |
BINARY | P0AGA2 | secE P0AG96 | 5 | EBI-761422, EBI-6404267 | |
BINARY | P0AGA2 | secG P0AG99 | 3 | EBI-761422, EBI-6404248 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length443
- Mass (Da)48,512
- Last updated1986-07-21 v1
- Checksum711CA63CD8809763
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X01563 EMBL· GenBank· DDBJ | CAA25725.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U18997 EMBL· GenBank· DDBJ | AAA58097.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC76325.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE77991.1 EMBL· GenBank· DDBJ | Genomic DNA |