DLP2_CAMJJ
ID DLP2_CAMJJ Reviewed; 609 AA.
AC A0A0H3PJK4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Dynamin-like protein 2 {ECO:0000303|PubMed:30131557};
DE Short=DLP2 {ECO:0000303|PubMed:30131557};
GN Name=dlp2 {ECO:0000303|PubMed:30131557};
GN Synonyms=cj0412 {ECO:0000303|PubMed:30131557};
GN OrderedLocusNames=CJJ81176_0436;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:5OWV, ECO:0007744|PDB:5OXF}
RP X-RAY CRYSTALLOGRAPHY (3.72 ANGSTROMS) WITH AND WITHOUT GDP, CATALYTIC
RP ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF LYS-74 AND 530-PHE--PHE-533.
RC STRAIN=81-176;
RX PubMed=30131557; DOI=10.1038/s41467-018-05523-8;
RA Liu J., Noel J.K., Low H.H.;
RT "Structural basis for membrane tethering by a bacterial dynamin-like
RT pair.";
RL Nat. Commun. 9:3345-3345(2018).
CC -!- FUNCTION: The heterotetrameric DLP1(2)-DLP2(2) complex tethers
CC liposomes and may mediate their fusion. Initial binding is probably
CC mediated by DLP1, while DLP2 couples DLP1 subunits and increases the
CC effective reach of the complex up to 45 nm. The role of the nucleotide
CC is unknown. This subunit alone very weakly binds to liposomes; GTP,
CC GDP, GMPPCP and GMPPNP do not change heterotetramer binding.
CC Tetramerization is required for GTPase activity, suggesting the GTPase
CC domains (dynamin-type G) from DLP1 and DLP2 must dimerize to
CC reconstitute the GTPase active site. {ECO:0000269|PubMed:30131557}.
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;
CC Evidence={ECO:0000269|PubMed:30131557};
CC -!- SUBUNIT: Forms a 2:2 heterotetramer with DLP1. DLP2 forms a central
CC back-to-back dimer flanked on each side by a DLP1 subunit. In the
CC crystal structures the 2 DLP1 subunits are in very different
CC conformations. {ECO:0000269|PubMed:30131557}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30131557}.
CC -!- DOMAIN: The 9 residue linker permits DLP1 (tethered to DLP2)
CC considerable flexibility; it is long enough to allow the GTPase domains
CC (dynamin-type G) of DLP1 and DLP2 to heterodimerize. Two regions within
CC the tip of the trunk are required for homodimerization; deletion of
CC residues 348-401 and 509-542 prevents DLP2 dimerization, but not
CC formation of a DLP1-DLP2 dimer. {ECO:0000269|PubMed:30131557}.
CC -!- DISRUPTION PHENOTYPE: Double dlp1-dlp2 deletions have no obvious cell
CC division defects, have no flagella (possibly due to loss of expression
CC of flgP) and are non-motile. {ECO:0000269|PubMed:30131557}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAQ73444.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000538; EAQ73444.2; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002858743.1; NC_008787.1.
DR PDB; 5OWV; X-ray; 3.72 A; C/D=1-609.
DR PDB; 5OXF; X-ray; 3.94 A; C/D=1-609.
DR PDBsum; 5OWV; -.
DR PDBsum; 5OXF; -.
DR SMR; A0A0H3PJK4; -.
DR STRING; 354242.CJJ81176_0436; -.
DR EnsemblBacteria; EAQ73444; EAQ73444; CJJ81176_0436.
DR KEGG; cjj:CJJ81176_0436; -.
DR eggNOG; COG0699; Bacteria.
DR HOGENOM; CLU_447378_0_0_7; -.
DR OMA; WQEPYEL; -.
DR Proteomes; UP000000646; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00350; Dynamin_N; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase.
FT CHAIN 1..609
FT /note="Dynamin-like protein 2"
FT /id="PRO_0000453206"
FT DOMAIN 63..310
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 1..16
FT /note="Inserts into assembly domain of DLP1, required for
FT tetramerization"
FT /evidence="ECO:0000269|PubMed:30131557"
FT REGION 17..25
FT /note="Linker"
FT REGION 68..75
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055,
FT ECO:0000305"
FT REGION 93..95
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055,
FT ECO:0000305"
FT REGION 158..161
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055,
FT ECO:0000305"
FT REGION 216..219
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055,
FT ECO:0000305"
FT BINDING 72..76
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:30131557,
FT ECO:0007744|PDB:5OXF"
FT MUTAGEN 74
FT /note="K->A: No GTPase activity."
FT /evidence="ECO:0000269|PubMed:30131557"
FT MUTAGEN 530..533
FT /note="FVLF->EEEE: Loss of liposome-binding."
FT /evidence="ECO:0000269|PubMed:30131557"
SQ SEQUENCE 609 AA; 71304 MW; D784CC56FF66EF33 CRC64;
MQINLLNDFI KAYENTYSVS FDDSFKGRIQ ELCKELNEPF MHASYALENE LKELVFSLDK
NVNIAIIGQF SSGKSSLLNL ILGRDCLPTG VVPVTFKPTF LRYAKEYFLR VEFEDGSDII
TNIEKLAFYT DQRNEVKQAK SLHIFAPIPL LEKITLVDTP GLNANENDTL TTLDELKNIH
GAIWLSLIDN AGKKSEEDAI KANLELLGEN SICVLNQKDK LSAEELDNVL NYAKSVFLKY
FNELIAISCK EAKDEQSYEK SNFQSLLDFL TQLDTTVLKE KFVKRKILNL CEILEDENQL
FVGIFDRLLN QFQSYEKHLL LAYENFLKEI EILNHQILEQ LKSISERISS EIFASVKEKD
AYFYKESKGF LKKDLYTRYD YKAPYISSDD AFLAMFYNSD VMSKEFKKIK NELYKSFEEI
KMKLKDFINI LEREILLFKA EFSNIQKDHI FQSDKNFSEL RAFCNASDEY FLKDFKELLF
KSILELDLFF EKLNLKAFTN YENATKLSLA FFSRKINESR VLYELDSSEF VLFYPKKSEI
YERVLNELNV YEFETLLINK PILTKIAKNF LEQSQNLIQE KNKFLDLKKA ELQKRRAQIL
NVRESIKED
