B2IZD3 · BDLP_NOSP7
- ProteinBacterial dynamin-like protein
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids693 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Dynamin-related GTPase probably involved in membrane remodeling. Lipid and nucleotide-binding are thought to induce a large intramolecular rearrangement, leading to assembly on lipid bilayers and possible membrane curving. In the presence of the non-hydrolyzable GTP analog GMP-PNP self-assembles on a lipid bilayer; this does not stimulate subsequent GTPase activity. Does not bind lipids in the presence of GDP; perhaps GTP hydrolysis disrupts membrane-binding.
Catalytic activity
- GTP + H2O = GDP + H+ + phosphate
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
68.6 μM | GTP |
kcat is 0.53 min-1.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | identical protein binding | |
Molecular Function | lipid binding | |
Biological Process | mitochondrial fusion |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBacterial dynamin-like protein
- EC number
- Short namesBDLP
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Cyanobacteriota > Cyanophyceae > Nostocales > Nostocaceae > Nostoc
Accessions
- Primary accessionB2IZD3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Peripheral membrane protein
Note: Probably inserts into the outer leaflet of the membrane only (Probable). Forms foci localized in the cell periphery, and occasionally in the cell interior.
Features
Showing features for topological domain, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-521 | Cytoplasmic | ||||
Sequence: MVNQVATDRFIQDLERVAQVRSEMSVCLNKLAETINKAELAGDSSSGKLSLERDIEDITIASKNLQQGVFRLLVLGDMKRGKSTFLNALIGENLLPSDVNPCTAVLTVLRYGPEKKVTIHFNDGKSPQQLDFQNFKYKYTIDPAEAKKLEQEKKQAFPDVDYAVVEYPLTLLQKGIEIVDSPGLNDTEARNELSLGYVNNCHAILFVMRASQPCTLGERRYLENYIKGRGLTVFFLVNAWDQVRESLIDPDDVEELQASENRLRQVFNANLAEYCTVEGQNIYDERVFELSSIQALRRRLKNPQADLDGTGFPKFMDSLNTFLTRERAIAELRQVRTLARLACNHTREAVARRIPLLEQDVNELKKRIDSVEPEFNKLTGIRDEFQKEIINTRDTQARTISESFRSYVLNLGNTFENDFLRYQPELNLFDFLSSGKREAFNAALQKAFEQYITDKSAAWTLTAEKDINAAFKELSRSASQYGASYNQITDQITEKLTGKDVKVHTTTTAEEDNSPGWAKWA | ||||||
Intramembrane | 522-574 | |||||
Sequence: MGLLSLSKGNLAGFALAGAGFDWKNILLNYFTVIGIGGIITAVTGILLGPIGF | ||||||
Topological domain | 575-693 | Cytoplasmic | ||||
Sequence: ALLGLGVGFLQADQARRELVKTAKKELVKHLPQVAHEQSQVVYNAVKECFDSYEREVSKRINDDIVSRKSELDNLVKQKQTREINRESEFNRLKNLQEDVIAQLQKIEAAYSNLLAYYS |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 82 | 15-fold reduction of GTP hydrolysis. | ||||
Sequence: K → A | ||||||
Mutagenesis | 576-577 | No lipid-binding. | ||||
Sequence: LL → EE | ||||||
Mutagenesis | 583 | No lipid-binding. | ||||
Sequence: F → E |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000425573 | 1-693 | Bacterial dynamin-like protein | |||
Sequence: MVNQVATDRFIQDLERVAQVRSEMSVCLNKLAETINKAELAGDSSSGKLSLERDIEDITIASKNLQQGVFRLLVLGDMKRGKSTFLNALIGENLLPSDVNPCTAVLTVLRYGPEKKVTIHFNDGKSPQQLDFQNFKYKYTIDPAEAKKLEQEKKQAFPDVDYAVVEYPLTLLQKGIEIVDSPGLNDTEARNELSLGYVNNCHAILFVMRASQPCTLGERRYLENYIKGRGLTVFFLVNAWDQVRESLIDPDDVEELQASENRLRQVFNANLAEYCTVEGQNIYDERVFELSSIQALRRRLKNPQADLDGTGFPKFMDSLNTFLTRERAIAELRQVRTLARLACNHTREAVARRIPLLEQDVNELKKRIDSVEPEFNKLTGIRDEFQKEIINTRDTQARTISESFRSYVLNLGNTFENDFLRYQPELNLFDFLSSGKREAFNAALQKAFEQYITDKSAAWTLTAEKDINAAFKELSRSASQYGASYNQITDQITEKLTGKDVKVHTTTTAEEDNSPGWAKWAMGLLSLSKGNLAGFALAGAGFDWKNILLNYFTVIGIGGIITAVTGILLGPIGFALLGLGVGFLQADQARRELVKTAKKELVKHLPQVAHEQSQVVYNAVKECFDSYEREVSKRINDDIVSRKSELDNLVKQKQTREINRESEFNRLKNLQEDVIAQLQKIEAAYSNLLAYYS |
Expression
Developmental stage
Detected in vegetatively growing cells (at protein level).
Interaction
Subunit
Homodimer. Self-assembles in the presence of GMP-PNP and liposomes, and probably also in the presence of GTP.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | B2IZD3 | Npun_R6513 B2IZD3 | 2 | EBI-15613218, EBI-15613218 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 66-313 | Dynamin-type G | ||||
Sequence: QQGVFRLLVLGDMKRGKSTFLNALIGENLLPSDVNPCTAVLTVLRYGPEKKVTIHFNDGKSPQQLDFQNFKYKYTIDPAEAKKLEQEKKQAFPDVDYAVVEYPLTLLQKGIEIVDSPGLNDTEARNELSLGYVNNCHAILFVMRASQPCTLGERRYLENYIKGRGLTVFFLVNAWDQVRESLIDPDDVEELQASENRLRQVFNANLAEYCTVEGQNIYDERVFELSSIQALRRRLKNPQADLDGTGFP | ||||||
Region | 76-83 | G1 motif | ||||
Sequence: GDMKRGKS | ||||||
Region | 102-103 | G2 motif | ||||
Sequence: CT | ||||||
Region | 180-183 | G3 motif | ||||
Sequence: DSPG | ||||||
Region | 238-241 | G4 motif | ||||
Sequence: NAWD | ||||||
Region | 268 | G5 motif | ||||
Sequence: N | ||||||
Region | 311-571 | Middle domain | ||||
Sequence: GFPKFMDSLNTFLTRERAIAELRQVRTLARLACNHTREAVARRIPLLEQDVNELKKRIDSVEPEFNKLTGIRDEFQKEIINTRDTQARTISESFRSYVLNLGNTFENDFLRYQPELNLFDFLSSGKREAFNAALQKAFEQYITDKSAAWTLTAEKDINAAFKELSRSASQYGASYNQITDQITEKLTGKDVKVHTTTTAEEDNSPGWAKWAMGLLSLSKGNLAGFALAGAGFDWKNILLNYFTVIGIGGIITAVTGILLGP | ||||||
Coiled coil | 347-378 | |||||
Sequence: REAVARRIPLLEQDVNELKKRIDSVEPEFNKL | ||||||
Region | 572-606 | Paddle domain | ||||
Sequence: IGFALLGLGVGFLQADQARRELVKTAKKELVKHLP | ||||||
Region | 607-693 | GED | ||||
Sequence: QVAHEQSQVVYNAVKECFDSYEREVSKRINDDIVSRKSELDNLVKQKQTREINRESEFNRLKNLQEDVIAQLQKIEAAYSNLLAYYS | ||||||
Coiled coil | 661-688 | |||||
Sequence: ESEFNRLKNLQEDVIAQLQKIEAAYSNL |
Domain
The GTPase domain dimerizes and forms the BDLP tube surface, the middle and GED domains are elongated and involved in self-assembly, while the paddle region inserts into the outer leaflet of the membrane, possibly promoting membrane curvature.
Sequence similarities
Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length693
- Mass (Da)78,348
- Last updated2008-06-10 v1
- ChecksumDC1483C71AF1D80D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP001037 EMBL· GenBank· DDBJ | ACC84775.1 EMBL· GenBank· DDBJ | Genomic DNA |