BDLP_NOSP7
ID BDLP_NOSP7 Reviewed; 693 AA.
AC B2IZD3;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Bacterial dynamin-like protein {ECO:0000303|PubMed:17122778};
DE Short=BDLP;
DE EC=3.6.5.5 {ECO:0000269|PubMed:17122778};
GN OrderedLocusNames=Npun_R6513;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J.,
RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.;
RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:2J68, ECO:0007744|PDB:2J69}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH
RP GTP ANALOG, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DOMAIN, GTP-BINDING,
RP LIPID-BINDING, AND MUTAGENESIS OF LYS-82.
RC STRAIN=ATCC 29133 / PCC 73102;
RX PubMed=17122778; DOI=10.1038/nature05312;
RA Low H.H., Lowe J.;
RT "A bacterial dynamin-like protein.";
RL Nature 444:766-769(2006).
RN [3] {ECO:0007744|PDB:2W6D}
RP STRUCTURE BY ELECTRON MICROSCOPY (9.00 ANGSTROMS) BOUND TO LIPID TUBES,
RP DOMAIN, LIPID-BINDING, AND MUTAGENESIS OF 576-LEU-LEU-577 AND PHE-583.
RX PubMed=20064379; DOI=10.1016/j.cell.2009.11.003;
RA Low H.H., Sachse C., Amos L.A., Lowe J.;
RT "Structure of a bacterial dynamin-like protein lipid tube provides a
RT mechanism for assembly and membrane curving.";
RL Cell 139:1342-1352(2009).
CC -!- FUNCTION: Dynamin-related GTPase probably involved in membrane
CC remodeling. Lipid and nucleotide-binding are thought to induce a large
CC intramolecular rearrangement, leading to assembly on lipid bilayers and
CC possible membrane curving. In the presence of the non-hydrolyzable GTP
CC analog GMP-PNP self-assembles on a lipid bilayer; this does not
CC stimulate subsequent GTPase activity. Does not bind lipids in the
CC presence of GDP; perhaps GTP hydrolysis disrupts membrane-binding.
CC {ECO:0000269|PubMed:17122778}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.5;
CC Evidence={ECO:0000269|PubMed:17122778};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=68.6 uM for GTP {ECO:0000269|PubMed:17122778};
CC Note=kcat is 0.53 min(-1). {ECO:0000269|PubMed:17122778};
CC -!- SUBUNIT: Homodimer. Self-assembles in the presence of GMP-PNP and
CC liposomes, and probably also in the presence of GTP.
CC {ECO:0000269|PubMed:17122778}.
CC -!- INTERACTION:
CC B2IZD3; B2IZD3: Npun_R6513; NbExp=2; IntAct=EBI-15613218, EBI-15613218;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:17122778}; Peripheral membrane protein
CC {ECO:0000305|PubMed:17122778}. Note=Probably inserts into the outer
CC leaflet of the membrane only (Probable). Forms foci localized in the
CC cell periphery, and occasionally in the cell interior.
CC {ECO:0000305|PubMed:20064379}.
CC -!- DEVELOPMENTAL STAGE: Detected in vegetatively growing cells (at protein
CC level). {ECO:0000269|PubMed:17122778}.
CC -!- DOMAIN: The GTPase domain dimerizes and forms the BDLP tube surface,
CC the middle and GED domains are elongated and involved in self-assembly,
CC while the paddle region inserts into the outer leaflet of the membrane,
CC possibly promoting membrane curvature. {ECO:0000269|PubMed:17122778,
CC ECO:0000269|PubMed:20064379}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. Mitofusin subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01055}.
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DR EMBL; CP001037; ACC84775.1; -; Genomic_DNA.
DR RefSeq; WP_012412711.1; NC_010628.1.
DR PDB; 2J68; X-ray; 3.10 A; A=1-693.
DR PDB; 2J69; X-ray; 3.00 A; A/B/C/D=1-693.
DR PDB; 2W6D; EM; 9.00 A; A/B=1-693.
DR PDBsum; 2J68; -.
DR PDBsum; 2J69; -.
DR PDBsum; 2W6D; -.
DR AlphaFoldDB; B2IZD3; -.
DR SMR; B2IZD3; -.
DR DIP; DIP-60443N; -.
DR STRING; 63737.Npun_R6513; -.
DR EnsemblBacteria; ACC84775; ACC84775; Npun_R6513.
DR KEGG; npu:Npun_R6513; -.
DR eggNOG; COG0699; Bacteria.
DR HOGENOM; CLU_025039_0_0_3; -.
DR OMA; WAKWAMG; -.
DR OrthoDB; 152800at2; -.
DR PhylomeDB; B2IZD3; -.
DR EvolutionaryTrace; B2IZD3; -.
DR Proteomes; UP000001191; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR027094; Mitofusin_fam.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10465; PTHR10465; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Coiled coil; GTP-binding;
KW Hydrolase; Lipid-binding; Membrane; Nucleotide-binding; Reference proteome.
FT CHAIN 1..693
FT /note="Bacterial dynamin-like protein"
FT /id="PRO_0000425573"
FT TOPO_DOM 1..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 522..574
FT /evidence="ECO:0000305|PubMed:17122778,
FT ECO:0000305|PubMed:20064379"
FT TOPO_DOM 575..693
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 66..313
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 76..83
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 102..103
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 180..183
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 238..241
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 268
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 311..571
FT /note="Middle domain"
FT /evidence="ECO:0000305|PubMed:17122778,
FT ECO:0000305|PubMed:20064379"
FT REGION 572..606
FT /note="Paddle domain"
FT /evidence="ECO:0000305|PubMed:17122778,
FT ECO:0000305|PubMed:20064379"
FT REGION 607..693
FT /note="GED"
FT /evidence="ECO:0000305|PubMed:17122778,
FT ECO:0000305|PubMed:20064379"
FT COILED 347..378
FT /evidence="ECO:0000255"
FT COILED 661..688
FT /evidence="ECO:0000255"
FT BINDING 79..84
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:17122778,
FT ECO:0007744|PDB:2J68"
FT BINDING 235..241
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:17122778,
FT ECO:0007744|PDB:2J68"
FT BINDING 292..293
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:17122778,
FT ECO:0007744|PDB:2J68"
FT MUTAGEN 82
FT /note="K->A: 15-fold reduction of GTP hydrolysis."
FT /evidence="ECO:0000269|PubMed:17122778"
FT MUTAGEN 576..577
FT /note="LL->EE: No lipid-binding."
FT /evidence="ECO:0000269|PubMed:20064379"
FT MUTAGEN 583
FT /note="F->E: No lipid-binding."
FT /evidence="ECO:0000269|PubMed:20064379"
FT HELIX 6..39
FT /evidence="ECO:0007829|PDB:2J69"
FT TURN 40..46
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:2J69"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 82..90
FT /evidence="ECO:0007829|PDB:2J69"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:2J69"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:2J69"
FT STRAND 116..124
FT /evidence="ECO:0007829|PDB:2J69"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 143..150
FT /evidence="ECO:0007829|PDB:2J69"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:2J68"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:2J69"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 184..188
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:2J69"
FT STRAND 200..209
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:2J69"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:2J69"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 240..246
FT /evidence="ECO:0007829|PDB:2J69"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:2J68"
FT HELIX 253..271
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:2J69"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:2J69"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 292..301
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 312..325
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 327..357
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 362..370
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 372..409
FT /evidence="ECO:0007829|PDB:2J69"
FT TURN 410..415
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 416..419
FT /evidence="ECO:0007829|PDB:2J69"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 436..497
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 516..522
FT /evidence="ECO:0007829|PDB:2J69"
FT STRAND 527..534
FT /evidence="ECO:0007829|PDB:2J68"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:2J68"
FT HELIX 544..553
FT /evidence="ECO:0007829|PDB:2J69"
FT TURN 559..561
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 562..578
FT /evidence="ECO:0007829|PDB:2J69"
FT TURN 579..582
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 586..655
FT /evidence="ECO:0007829|PDB:2J69"
FT HELIX 660..693
FT /evidence="ECO:0007829|PDB:2J69"
SQ SEQUENCE 693 AA; 78348 MW; DC1483C71AF1D80D CRC64;
MVNQVATDRF IQDLERVAQV RSEMSVCLNK LAETINKAEL AGDSSSGKLS LERDIEDITI
ASKNLQQGVF RLLVLGDMKR GKSTFLNALI GENLLPSDVN PCTAVLTVLR YGPEKKVTIH
FNDGKSPQQL DFQNFKYKYT IDPAEAKKLE QEKKQAFPDV DYAVVEYPLT LLQKGIEIVD
SPGLNDTEAR NELSLGYVNN CHAILFVMRA SQPCTLGERR YLENYIKGRG LTVFFLVNAW
DQVRESLIDP DDVEELQASE NRLRQVFNAN LAEYCTVEGQ NIYDERVFEL SSIQALRRRL
KNPQADLDGT GFPKFMDSLN TFLTRERAIA ELRQVRTLAR LACNHTREAV ARRIPLLEQD
VNELKKRIDS VEPEFNKLTG IRDEFQKEII NTRDTQARTI SESFRSYVLN LGNTFENDFL
RYQPELNLFD FLSSGKREAF NAALQKAFEQ YITDKSAAWT LTAEKDINAA FKELSRSASQ
YGASYNQITD QITEKLTGKD VKVHTTTTAE EDNSPGWAKW AMGLLSLSKG NLAGFALAGA
GFDWKNILLN YFTVIGIGGI ITAVTGILLG PIGFALLGLG VGFLQADQAR RELVKTAKKE
LVKHLPQVAH EQSQVVYNAV KECFDSYERE VSKRINDDIV SRKSELDNLV KQKQTREINR
ESEFNRLKNL QEDVIAQLQK IEAAYSNLLA YYS
