E3PJ86 · GSPD2_ECOH1
- ProteinSecretin GspD 2
- GenegspD2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids686 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Part of a type II secretion system (T2SS, formerly general secretion pathway, GSP) for the export of folded proteins across the outer membrane (Probable). This subunit forms the outer membrane channel (Probable).
Miscellaneous
Encoded in a type II secretion system (T2SS-beta); this strain encodes 2 T2SS but only this one (beta) is expressed under standard laboratory conditions.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 493 | May serve as a pivot that allows opening of the central gate for substrate egress | ||||
Sequence: G |
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 outer membrane | |
Cellular Component | type II protein secretion system complex | |
Biological Process | protein secretion by the type II secretion system |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameSecretin GspD 2
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionE3PJ86
Subcellular Location
UniProt Annotation
GO Annotation
Note: Some protein is also found in the cell inner membrane, the inner membrane protein does not form multimers and is unstable (PubMed:22585966).
Most of the protein is in the periplasm which it traverses to contact proteins of the cell inner membrane (Probable)
Most of the protein is in the periplasm which it traverses to contact proteins of the cell inner membrane (Probable)
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Severely disrupts assembly and function of T2SS-beta.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 675-681 | Binds AspS2 normally. | ||||
Sequence: EVRAFLN → AVRAAFLA | ||||||
Mutagenesis | 676 | Binds AspS2 normally. | ||||
Sequence: V → A | ||||||
Mutagenesis | 676-680 | No longer binds AspS2. | ||||
Sequence: VRAFL → ARAAA | ||||||
Mutagenesis | 679 | No longer binds AspS2, the AspS2-GspD2 complex no longer forms in vivo. | ||||
Sequence: F → A | ||||||
Mutagenesis | 680 | Binds AspS2 normally. | ||||
Sequence: L → A | ||||||
Mutagenesis | 684-686 | Binds AspS2 normally. | ||||
Sequence: RTR → AAA |
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-40 | |||||
Sequence: MFWRDITLSVWRKKTTGLKTKKRLLPLVLAAALCSSPVWA | ||||||
Chain | PRO_5003179632 | 41-686 | Secretin GspD 2 | |||
Sequence: EEATFTANFKDTDLKSFIETVGANLNKTIIMGPGVQGKVSIRTMTPLNERQYYQLFLNLLEAQGYAVVPMENDVLKVVKSSAAKVEPLPLVGEGSDNYAGDEMVTKVVPVRNVSVRELAPILRQMIDSAGSGNVVNYDPSNVIMLTGRASVVERLTEVIQRVDHAGNRTEEVIPLDNASASEIARVLESLTKNSGENQPATLKSQIVADERTNSVIVSGDPATRDKMRRLIRRLDSEMERSGNSQVFYLKYSKAEDLVDVLKQVSGTLTAAKEEAEGTVGSGREIVSIAASKHSNALIVTAPQDIMQSLQSVIEQLDIRRAQVHVEALIVEVAEGSNINFGVQWASKDAGLMQFANGTQIPIGTLGAAISQAKPQKGSTVISENGATTINPDTNGDLSTLAQLLSGFSGTAVGVVKGDWMALVQAVKNDSSSNVLSTPSITTLDNQEAFFMVGQDVPVLTGSTVGSNNSNPFNTVERKKVGIMLKVTPQINEGNAVQMVIEQEVSKVEGQTSLDVVFGERKLKTTVLANDGELIVLGGLMDDQAGESVAKVPLLGDIPLIGNLFKSTADKKEKRNLMVFIRPTILRDGMAADGVSQRKYNYMRAEQIYRDEQGLSLMPHTAQPVLPAQNQALPPEVRAFLNAGRTR |
Interaction
Subunit
Forms a cylindrical channel with 15 subunits, each of which interacts with the surrounding pilotin AspS2 proteins (also called GspS-beta) (PubMed:29632366).
Interacts with inner cell membrane protein GspC2 in the periplasm (PubMed:21931548).
Forms multimers in the outer membrane (PubMed:22585966).
The isolated N0 domain forms dimers that self-assemble into rings (PubMed:23820381).
Interacts with inner cell membrane protein GspC2 in the periplasm (PubMed:21931548).
Forms multimers in the outer membrane (PubMed:22585966).
The isolated N0 domain forms dimers that self-assemble into rings (PubMed:23820381).
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 41-140 | N0, contacts GspC2 | ||||
Sequence: EEATFTANFKDTDLKSFIETVGANLNKTIIMGPGVQGKVSIRTMTPLNERQYYQLFLNLLEAQGYAVVPMENDVLKVVKSSAAKVEPLPLVGEGSDNYAG | ||||||
Region | 142-206 | N1 | ||||
Sequence: EMVTKVVPVRNVSVRELAPILRQMIDSAGSGNVVNYDPSNVIMLTGRASVVERLTEVIQRVDHAG | ||||||
Region | 207-279 | N2 | ||||
Sequence: NRTEEVIPLDNASASEIARVLESLTKNSGENQPATLKSQIVADERTNSVIVSGDPATRDKMRRLIRRLDSEME | ||||||
Region | 282-357 | N3 | ||||
Sequence: GNSQVFYLKYSKAEDLVDVLKQVSGTLTAAKEEAEGTVGSGREIVSIAASKHSNALIVTAPQDIMQSLQSVIEQLD | ||||||
Region | 360-627 | Secretin | ||||
Sequence: RAQVHVEALIVEVAEGSNINFGVQWASKDAGLMQFANGTQIPIGTLGAAISQAKPQKGSTVISENGATTINPDTNGDLSTLAQLLSGFSGTAVGVVKGDWMALVQAVKNDSSSNVLSTPSITTLDNQEAFFMVGQDVPVLTGSTVGSNNSNPFNTVERKKVGIMLKVTPQINEGNAVQMVIEQEVSKVEGQTSLDVVFGERKLKTTVLANDGELIVLGGLMDDQAGESVAKVPLLGDIPLIGNLFKSTADKKEKRNLMVFIRPTILRD | ||||||
Region | 414-433 | Cap gate | ||||
Sequence: PQKGSTVISENGATTINPDT | ||||||
Region | 629-686 | S domain, contacts AspS2 | ||||
Sequence: MAADGVSQRKYNYMRAEQIYRDEQGLSLMPHTAQPVLPAQNQALPPEVRAFLNAGRTR |
Domain
The N0 region interacts in the periplasm with GspC (PubMed:21931548).
The S domain interacts with pilotin AspS2 (PubMed:29632366).
The N0, N1, N2 and N3 domains are periplasmic, while the secretin and S domains form a channel that is partially inserted in the outer membrane. The cap gate extends out on the extracellular side of the channel partially closing the channel. The secretin domain forms a double beta-barrel structure; the outer barrel has an outer diameter of about 110 Angstroms while the inner barrel forms the central gate with a small pore in the closed state (By similarity).
The S domain interacts with pilotin AspS2 (PubMed:29632366).
The N0, N1, N2 and N3 domains are periplasmic, while the secretin and S domains form a channel that is partially inserted in the outer membrane. The cap gate extends out on the extracellular side of the channel partially closing the channel. The secretin domain forms a double beta-barrel structure; the outer barrel has an outer diameter of about 110 Angstroms while the inner barrel forms the central gate with a small pore in the closed state (By similarity).
Sequence similarities
Belongs to the bacterial secretin family. GSP D subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length686
- Mass (Da)74,202
- Last updated2011-01-11 v1
- Checksum213BE2A98A043B4F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
FN649414 EMBL· GenBank· DDBJ | CBJ02737.1 EMBL· GenBank· DDBJ | Genomic DNA |