DLP1_CAMJJ
ID DLP1_CAMJJ Reviewed; 728 AA.
AC A0A0H3PJL7;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Dynamin-like protein 1 {ECO:0000303|PubMed:30131557};
DE Short=DLP1 {ECO:0000303|PubMed:30131557};
GN Name=dlp1 {ECO:0000303|PubMed:30131557};
GN Synonyms=cj0411 {ECO:0000303|PubMed:30131557};
GN OrderedLocusNames=CJJ81176_0435;
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-175.
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 weakly binds to liposomes; GTP, GDP,
CC GMPPCP and GMPPNP do not change heterotetramer binding. Tetramerization
CC is required for GTPase activity, suggesting the GTPase domains
CC (dynamin-type G) from DLP1 and DLP2 must dimerize to reconstitute the
CC 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: Protein is very flexible, is probably able to bind membranes in
CC many conformations. The N-terminus of DLP2 inserts into the assembly
CC domain of DLP1; this is followed by a 9 residue DLP2 linker which
CC allows DLP1 significant movement. The linker is long enough to allow
CC the GTPase domains (dynamin-type G) of DLP1 and DLP2 to heterodimerize.
CC {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}.
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DR EMBL; CP000538; EAQ73461.1; -; Genomic_DNA.
DR RefSeq; WP_002857319.1; NC_008787.1.
DR PDB; 5OWV; X-ray; 3.72 A; A/B=1-728.
DR PDB; 5OXF; X-ray; 3.94 A; A/B=1-728.
DR PDBsum; 5OWV; -.
DR PDBsum; 5OXF; -.
DR SMR; A0A0H3PJL7; -.
DR STRING; 354242.CJJ81176_0435; -.
DR EnsemblBacteria; EAQ73461; EAQ73461; CJJ81176_0435.
DR KEGG; cjj:CJJ81176_0435; -.
DR eggNOG; COG0699; Bacteria.
DR HOGENOM; CLU_019605_0_0_7; -.
DR OMA; DLMIHLM; -.
DR Proteomes; UP000000646; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
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; Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding.
FT CHAIN 1..728
FT /note="Dynamin-like protein 1"
FT /id="PRO_0000453205"
FT DOMAIN 159..442
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 1..119
FT /note="Assembly domain, required for tetramerization"
FT /evidence="ECO:0000269|PubMed:30131557"
FT REGION 169..176
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 195..196
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 298..301
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 358..361
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 388
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 470..695
FT /note="Required for liposome binding but not for
FT tetramerization"
FT /evidence="ECO:0000269|PubMed:30131557"
FT BINDING 171..177
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:30131557,
FT ECO:0007744|PDB:5OXF"
FT BINDING 359
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:30131557,
FT ECO:0007744|PDB:5OXF"
FT BINDING 400..402
FT /ligand="GDP"
FT /ligand_id="ChEBI:CHEBI:58189"
FT /evidence="ECO:0000269|PubMed:30131557,
FT ECO:0007744|PDB:5OXF"
FT MUTAGEN 175
FT /note="K->A: No GTPase activity."
FT /evidence="ECO:0000269|PubMed:30131557"
SQ SEQUENCE 728 AA; 84585 MW; 364E2217E6BAC2F2 CRC64;
MKELFQKIWQ NELQFLNFDA KFQDKSKLDT AECAIILSVN KDNYERYFLL KEFQELCKKI
DLRVDIFSMQ NAQICILNLF KSGFISKQDL LKALKILEKI SKNTEIFDFI LQEKVQSIDQ
KALFQNDFKE LNTINLELQK LSFDENLKSR LQKTLEKFQN LEFNIAITGV MNAGKSSLLN
ALLKEDFLGV SNIPETANLT VLSYGKSEEA KIYFWDKKEW QNILESSHFN ADLKEFIDKL
DKSVNIEDFI KDKPLIQNIA LCELKNFSSA KNKISALIKK IEIKSHLEFL KNNISIVDTP
GLDDVVVQRE IVTNEYLRES DFLIHLMNAS QSLTQKDADF LVHCLLNSRL SKFLIVLTKA
DLLSKKDLEE VIVYTKESLK SRLVDLDENL VEKIDFLCVS AKMASDFYKG LASKESLQKS
GMQEFENYLF NELYAGEKSK IALRAYKKEL HLELKNILSE YEMQNRLIKE NKQGVSEENQ
KLLLELQKQN TLLKEAQDEI SNSIAKLKNI DSGIDNLVLL LAKKLKERLI DEFKYLKNNA
QKLNLSRILN IVDITTKDGI NDILREIKFE NIKKIEELKT NLSLKYDFLK DDFDNGFEGF
KDGISKNIDS IFQSEKFALL RLKIEKLSNL KSDLYELETN LDTVIFDTFK EFKMSEILNS
LNINGAFFEF LNDKLKHYEK NQKSKLESLE KVLQSLKNQD ANILNSFEEN LEKIEKLKQL
EMGLLNAD
