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Protein

Bacterial dynamin-like protein

Gene

Npun_R6513

Organism
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

GTP + H2O = GDP + phosphate.

Kineticsi

kcat 0.53/min.

  1. KM=68.6 µM for GTP1 Publication

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi79 – 84GTP6
    Nucleotide bindingi235 – 241GTP7
    Nucleotide bindingi292 – 293GTP2

    GO - Molecular functioni

    • GTPase activity Source: UniProtKB
    • GTP binding Source: UniProtKB
    • lipid binding Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    GTP-binding, Lipid-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bacterial dynamin-like protein (EC:3.6.5.5)
    Short name:
    BDLP
    Gene namesi
    Ordered Locus Names:Npun_R6513
    OrganismiNostoc punctiforme (strain ATCC 29133 / PCC 73102)
    Taxonomic identifieri63737 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaNostocalesNostocaceaeNostoc
    Proteomesi
    • UP000001191 Componenti: Chromosome

    Subcellular locationi

    • Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

    • 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.Curated

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini1 – 521CytoplasmicSequence analysisAdd BLAST521
    Transmembranei522 – 542Discontinuously helicalSequence analysisAdd BLAST21
    Topological domaini543 – 553In membraneSequence analysisAdd BLAST11
    Transmembranei554 – 574Discontinuously helicalSequence analysisAdd BLAST21
    Topological domaini575 – 693CytoplasmicSequence analysisAdd BLAST119

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi82K → A: 15-fold reduction of GTP hydrolysis. 1 Publication1
    Mutagenesisi576 – 577LL → EE: No lipid-binding. 1 Publication2
    Mutagenesisi583F → E: No lipid-binding. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004255731 – 693Bacterial dynamin-like proteinAdd BLAST693

    Expressioni

    Developmental stagei

    Detected in vegetatively growing cells (at protein level).1 Publication

    Interactioni

    Subunit structurei

    Homodimer. Self-assembles in the presence of GMP-PNP and liposomes, and probably also in the presence of GTP.1 Publication

    Protein-protein interaction databases

    DIPiDIP-60443N.
    STRINGi63737.Npun_R6513.

    Structurei

    Secondary structure

    1693
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi6 – 39Combined sources34
    Turni40 – 46Combined sources7
    Helixi52 – 67Combined sources16
    Beta strandi70 – 75Combined sources6
    Helixi82 – 90Combined sources9
    Turni101 – 103Combined sources3
    Beta strandi107 – 111Combined sources5
    Beta strandi116 – 124Combined sources9
    Beta strandi129 – 131Combined sources3
    Helixi132 – 138Combined sources7
    Helixi143 – 150Combined sources8
    Turni151 – 153Combined sources3
    Beta strandi160 – 167Combined sources8
    Helixi170 – 173Combined sources4
    Beta strandi175 – 180Combined sources6
    Helixi184 – 188Combined sources5
    Helixi191 – 194Combined sources4
    Helixi196 – 199Combined sources4
    Beta strandi200 – 209Combined sources10
    Helixi216 – 225Combined sources10
    Turni226 – 228Combined sources3
    Beta strandi233 – 238Combined sources6
    Helixi240 – 246Combined sources7
    Beta strandi247 – 249Combined sources3
    Helixi253 – 271Combined sources19
    Helixi272 – 275Combined sources4
    Beta strandi276 – 279Combined sources4
    Helixi283 – 285Combined sources3
    Beta strandi287 – 289Combined sources3
    Helixi292 – 301Combined sources10
    Helixi312 – 325Combined sources14
    Helixi327 – 357Combined sources31
    Helixi362 – 370Combined sources9
    Helixi372 – 409Combined sources38
    Turni410 – 415Combined sources6
    Helixi416 – 419Combined sources4
    Turni420 – 422Combined sources3
    Helixi428 – 432Combined sources5
    Helixi436 – 497Combined sources62
    Helixi516 – 522Combined sources7
    Beta strandi527 – 534Combined sources8
    Beta strandi536 – 538Combined sources3
    Helixi544 – 553Combined sources10
    Turni559 – 561Combined sources3
    Helixi562 – 578Combined sources17
    Turni579 – 582Combined sources4
    Helixi586 – 655Combined sources70
    Helixi660 – 693Combined sources34

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2J68X-ray3.10A1-693[»]
    2J69X-ray3.00A/B/C/D1-693[»]
    2W6Delectron microscopy9.00A/B1-693[»]
    SMRiB2IZD3.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiB2IZD3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini66 – 313Dynamin-type GAdd BLAST248

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni68 – 287GTPase domainAdd BLAST220
    Regioni311 – 571Middle domainAdd BLAST261
    Regioni572 – 606Paddle domainAdd BLAST35
    Regioni607 – 693GEDAdd BLAST87

    Coiled coil

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Coiled coili347 – 378Sequence analysisAdd BLAST32
    Coiled coili661 – 688Sequence analysisAdd BLAST28

    Domaini

    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.2 Publications

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiENOG410890F. Bacteria.
    COG0699. LUCA.
    HOGENOMiHOG000035501.
    OMAiNCHAILF.
    OrthoDBiPOG091H09NR.
    PhylomeDBiB2IZD3.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR022812. Dynamin_SF.
    IPR030381. G_DYNAMIN_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00350. Dynamin_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS51718. G_DYNAMIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    B2IZD3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVNQVATDRF IQDLERVAQV RSEMSVCLNK LAETINKAEL AGDSSSGKLS
    60 70 80 90 100
    LERDIEDITI ASKNLQQGVF RLLVLGDMKR GKSTFLNALI GENLLPSDVN
    110 120 130 140 150
    PCTAVLTVLR YGPEKKVTIH FNDGKSPQQL DFQNFKYKYT IDPAEAKKLE
    160 170 180 190 200
    QEKKQAFPDV DYAVVEYPLT LLQKGIEIVD SPGLNDTEAR NELSLGYVNN
    210 220 230 240 250
    CHAILFVMRA SQPCTLGERR YLENYIKGRG LTVFFLVNAW DQVRESLIDP
    260 270 280 290 300
    DDVEELQASE NRLRQVFNAN LAEYCTVEGQ NIYDERVFEL SSIQALRRRL
    310 320 330 340 350
    KNPQADLDGT GFPKFMDSLN TFLTRERAIA ELRQVRTLAR LACNHTREAV
    360 370 380 390 400
    ARRIPLLEQD VNELKKRIDS VEPEFNKLTG IRDEFQKEII NTRDTQARTI
    410 420 430 440 450
    SESFRSYVLN LGNTFENDFL RYQPELNLFD FLSSGKREAF NAALQKAFEQ
    460 470 480 490 500
    YITDKSAAWT LTAEKDINAA FKELSRSASQ YGASYNQITD QITEKLTGKD
    510 520 530 540 550
    VKVHTTTTAE EDNSPGWAKW AMGLLSLSKG NLAGFALAGA GFDWKNILLN
    560 570 580 590 600
    YFTVIGIGGI ITAVTGILLG PIGFALLGLG VGFLQADQAR RELVKTAKKE
    610 620 630 640 650
    LVKHLPQVAH EQSQVVYNAV KECFDSYERE VSKRINDDIV SRKSELDNLV
    660 670 680 690
    KQKQTREINR ESEFNRLKNL QEDVIAQLQK IEAAYSNLLA YYS
    Length:693
    Mass (Da):78,348
    Last modified:June 10, 2008 - v1
    Checksum:iDC1483C71AF1D80D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP001037 Genomic DNA. Translation: ACC84775.1.
    RefSeqiWP_012412711.1. NC_010628.1.

    Genome annotation databases

    EnsemblBacteriaiACC84775; ACC84775; Npun_R6513.
    KEGGinpu:Npun_R6513.
    PATRICi22767045. VBINosPun48114_7640.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP001037 Genomic DNA. Translation: ACC84775.1.
    RefSeqiWP_012412711.1. NC_010628.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2J68X-ray3.10A1-693[»]
    2J69X-ray3.00A/B/C/D1-693[»]
    2W6Delectron microscopy9.00A/B1-693[»]
    SMRiB2IZD3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-60443N.
    STRINGi63737.Npun_R6513.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiACC84775; ACC84775; Npun_R6513.
    KEGGinpu:Npun_R6513.
    PATRICi22767045. VBINosPun48114_7640.

    Phylogenomic databases

    eggNOGiENOG410890F. Bacteria.
    COG0699. LUCA.
    HOGENOMiHOG000035501.
    OMAiNCHAILF.
    OrthoDBiPOG091H09NR.
    PhylomeDBiB2IZD3.

    Miscellaneous databases

    EvolutionaryTraceiB2IZD3.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR022812. Dynamin_SF.
    IPR030381. G_DYNAMIN_dom.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00350. Dynamin_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS51718. G_DYNAMIN_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiBDLP_NOSP7
    AccessioniPrimary (citable) accession number: B2IZD3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 19, 2014
    Last sequence update: June 10, 2008
    Last modified: November 2, 2016
    This is version 52 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.