GPN_PYRAB
ID GPN_PYRAB Reviewed; 248 AA.
AC Q9UYR9; G8ZIK1;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-NOV-2014, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=GPN-loop GTPase PAB0955 {ECO:0000303|PubMed:17468740};
DE EC=3.6.5.- {ECO:0000269|PubMed:17468740};
GN OrderedLocusNames=PYRAB14380 {ECO:0000312|EMBL:CAB50343.1};
GN ORFNames=PAB0955 {ECO:0000312|EMBL:CAB50343.1,
GN ECO:0000312|EMBL:CCE70884.1};
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
RN [3]
RP SUBUNIT.
RX PubMed=16510996; DOI=10.1107/s1744309105000035;
RA Gras S., Fernandez B., Chaumont V., Carpentier P., Armengaud J.,
RA Housset D.;
RT "Expression, purification, crystallization and preliminary crystallographic
RT analysis of the PAB0955 gene product.";
RL Acta Crystallogr. F 61:208-211(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-248 IN COMPLEX WITH GTP,
RP CATALYTIC ACTIVITY, AND INTERACTION WITH TOP6B; DNAG AND RF-C.
RX PubMed=17468740; DOI=10.1038/sj.embor.7400958;
RA Gras S., Chaumont V., Fernandez B., Carpentier P., Charrier-Savournin F.,
RA Schmitt S., Pineau C., Flament D., Hecker A., Forterre P., Armengaud J.,
RA Housset D.;
RT "Structural insights into a new homodimeric self-activated GTPase family.";
RL EMBO Rep. 8:569-575(2007).
CC -!- FUNCTION: Small GTPase that may be involved in genome maintenance. Has
CC weak intrinsic GTPase activity but displays no ATPase activity.
CC {ECO:0000269|PubMed:17468740}.
CC -!- SUBUNIT: Homodimer (PubMed:16510996). Interacts with DNA topoisomerase
CC VI subunit B (top6B), DNA primase DnaG and RF-C (PubMed:17468740).
CC {ECO:0000269|PubMed:16510996, ECO:0000269|PubMed:17468740}.
CC -!- SIMILARITY: Belongs to the GPN-loop GTPase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB50343.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ248287; CAB50343.1; ALT_INIT; Genomic_DNA.
DR EMBL; HE613800; CCE70884.1; -; Genomic_DNA.
DR PIR; B75056; B75056.
DR RefSeq; WP_048147021.1; NC_000868.1.
DR PDB; 1YR6; X-ray; 2.15 A; A=1-248.
DR PDB; 1YR7; X-ray; 2.08 A; A=1-248.
DR PDB; 1YR8; X-ray; 2.40 A; A=1-248.
DR PDB; 1YR9; X-ray; 2.80 A; A=1-248.
DR PDB; 1YRA; X-ray; 2.30 A; A/B=1-248.
DR PDB; 1YRB; X-ray; 1.75 A; A/B=1-248.
DR PDB; 2OXR; X-ray; 2.40 A; A=1-248.
DR PDBsum; 1YR6; -.
DR PDBsum; 1YR7; -.
DR PDBsum; 1YR8; -.
DR PDBsum; 1YR9; -.
DR PDBsum; 1YRA; -.
DR PDBsum; 1YRB; -.
DR PDBsum; 2OXR; -.
DR AlphaFoldDB; Q9UYR9; -.
DR SMR; Q9UYR9; -.
DR MINT; Q9UYR9; -.
DR STRING; 272844.PAB0955; -.
DR EnsemblBacteria; CAB50343; CAB50343; PAB0955.
DR GeneID; 1495713; -.
DR KEGG; pab:PAB0955; -.
DR PATRIC; fig|272844.11.peg.1529; -.
DR eggNOG; arCOG01225; Archaea.
DR HOGENOM; CLU_037460_3_0_2; -.
DR OrthoDB; 86220at2157; -.
DR EvolutionaryTrace; Q9UYR9; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; Chromosome.
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; IPR004130; Gpn.
DR InterPro; IPR030230; Gpn1/Npa3/XAB1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR21231; PTHR21231; 1.
DR PANTHER; PTHR21231:SF8; PTHR21231:SF8; 1.
DR Pfam; PF03029; ATP_bind_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Hydrolase; Nucleotide-binding.
FT CHAIN 1..248
FT /note="GPN-loop GTPase PAB0955"
FT /id="PRO_0000431297"
FT MOTIF 65..67
FT /note="Gly-Pro-Asn (GPN)-loop; involved in dimer interface"
FT /evidence="ECO:0000269|PubMed:17468740"
FT BINDING 10..15
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:17468740"
FT BINDING 165..168
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:17468740"
FT BINDING 224
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:17468740"
FT SITE 67
FT /note="Stabilizes the phosphate intermediate; shared with
FT dimeric partner"
FT /evidence="ECO:0000305|PubMed:17468740"
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:1YRB"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:1YRB"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1YRB"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 56..60
FT /evidence="ECO:0007829|PDB:1YRB"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:1YRB"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:1YRB"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1YRB"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 139..156
FT /evidence="ECO:0007829|PDB:1YRB"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 185..194
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 198..213
FT /evidence="ECO:0007829|PDB:1YRB"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:1YRB"
FT HELIX 230..244
FT /evidence="ECO:0007829|PDB:1YRB"
SQ SEQUENCE 248 AA; 28697 MW; F88FB5473E40B0D3 CRC64;
MIVVFVGTAG SGKTTLTGEF GRYLEDNYKV AYVNLDTGVK ELPYEPSIDV REFVTVEEIM
REGYGPNGAI VESYDRLMEK FNEYLNKILR LEKENDYVLI DTPGQMETFL FHEFGVRLME
NLPYPLVVYI SDPEILKKPN DYCFVRFFAL LIDLRLGATT IPALNKVDLL SEEEKERHRK
YFEDIDYLTA RLKLDPSMQG LMAYKMCSMM TEVLPPVRVL YLSAKTREGF EDLETLAYEH
YCTCGDLT
