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Protein

GTPase HflX

Gene

hflX

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GTPase that associates with the 50S ribosomal subunit and may have a role during protein synthesis or ribosome biogenesis. Specific for GTP.UniRule annotation2 Publications

Cofactori

Mg2+UniRule annotation

Enzyme regulationi

GTPase activity is stimulated by the presence of 50S ribosomal subunits. Hydrolysis is probably regulated by the HflX N-terminal domain.2 Publications

Kineticsi

  1. KM=5.3 µM for GTP1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi193 – 1931MagnesiumUniRule annotation
    Metal bindingi213 – 2131MagnesiumUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi186 – 1938GTPUniRule annotation2 Publications
    Nucleotide bindingi211 – 2155GTPUniRule annotation
    Nucleotide bindingi232 – 2354GTPUniRule annotation
    Nucleotide bindingi300 – 3034GTPUniRule annotation2 Publications
    Nucleotide bindingi334 – 3363GTPUniRule annotation2 Publications

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Ligandi

    GTP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciSSOL273057:GCH2-257-MONOMER.
    BRENDAi3.6.5.3. 6163.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTPase HflXUniRule annotation
    Alternative name(s):
    GTP-binding protein HflXUniRule annotation
    Gene namesi
    Name:hflXUniRule annotation
    Ordered Locus Names:SSO0269
    OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
    Taxonomic identifieri273057 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    Proteomesi
    • UP000001974 Componenti: Chromosome

    Subcellular locationi

    • Cytoplasm UniRule annotation

    • Note: May associate with membranes.UniRule annotation

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi189 – 1891N → P: Loss of GTPase activity. 1 Publication
    Mutagenesisi193 – 1931T → N: Loss of GTPase activity. 1 Publication
    Mutagenesisi213 – 2131T → V: Decrease in GTPase activity. 1 Publication
    Mutagenesisi235 – 2351G → P: Loss of GTPase activity. 1 Publication
    Mutagenesisi235 – 2351G → S: Decrease in GTPase activity. 1 Publication
    Mutagenesisi236 – 2361F → P: Increase in KM for GTP and in GTPase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 356356GTPase HflXPRO_0000412528Add
    BLAST

    Interactioni

    Subunit structurei

    Monomer. Associates with the 50S ribosomal subunit. Does not associate with 70S ribosomes.UniRule annotation3 Publications

    Protein-protein interaction databases

    STRINGi273057.SSO0269.

    Structurei

    Secondary structure

    1
    356
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 76Combined sources
    Turni10 – 123Combined sources
    Helixi13 – 2210Combined sources
    Beta strandi25 – 317Combined sources
    Turni39 – 413Combined sources
    Helixi45 – 528Combined sources
    Beta strandi59 – 646Combined sources
    Helixi68 – 7811Combined sources
    Beta strandi82 – 843Combined sources
    Helixi86 – 9712Combined sources
    Helixi101 – 12121Combined sources
    Helixi145 – 16420Combined sources
    Beta strandi181 – 1855Combined sources
    Turni188 – 1914Combined sources
    Helixi192 – 2009Combined sources
    Beta strandi218 – 2236Combined sources
    Beta strandi226 – 2327Combined sources
    Helixi242 – 2443Combined sources
    Helixi245 – 2539Combined sources
    Helixi254 – 2574Combined sources
    Beta strandi258 – 2669Combined sources
    Helixi271 – 28818Combined sources
    Beta strandi295 – 3006Combined sources
    Helixi302 – 3043Combined sources
    Helixi309 – 32315Combined sources
    Beta strandi327 – 3326Combined sources
    Turni335 – 3384Combined sources
    Helixi341 – 35515Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QTFX-ray2.00A1-356[»]
    2QTHX-ray2.00A1-356[»]
    3KXIX-ray2.65A1-356[»]
    3KXKX-ray2.35A/B1-356[»]
    3KXLX-ray2.50A/B1-356[»]
    ProteinModelPortaliQ980M3.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ980M3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini180 – 356177Hflx-type GUniRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. HflX GTPase family.UniRule annotation
    Contains 1 Hflx-type G (guanine nucleotide-binding) domain.UniRule annotation

    Phylogenomic databases

    eggNOGiarCOG00353. Archaea.
    COG2262. LUCA.
    HOGENOMiHOG000260368.
    InParanoidiQ980M3.
    KOiK03665.
    OMAiKWQLVLE.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    HAMAPiMF_00900. GTPase_HflX.
    InterProiIPR030394. G_HFLX_dom.
    IPR032305. GTP-bd_M.
    IPR006073. GTP_binding_domain.
    IPR016496. GTPase_HflX.
    IPR025121. GTPase_HflX_N.
    IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    [Graphical view]
    PANTHERiPTHR10229. PTHR10229. 1 hit.
    PfamiPF16360. GTP-bdg_M. 1 hit.
    PF13167. GTP-bdg_N. 1 hit.
    PF01926. MMR_HSR1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006809. GTP-binding_hflX_prd. 1 hit.
    PRINTSiPR00326. GTP1OBG.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR03156. GTP_HflX. 1 hit.
    TIGR00231. small_GTP. 1 hit.
    PROSITEiPS51705. G_HFLX. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q980M3-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKTAALFVSK EFEEEAIALV EGANYKVTSI YKLPKSPNVK FYIQYDKLQQ
    60 70 80 90 100
    IKNDEEISTL IIFEQLKPRH FINIRRELKG KEVLDKILLL LEIFALHAGS
    110 120 130 140 150
    KEAKMQIELA RLKYELPIIK ETYTKSKIGE QQGPLGAGTY GVESTIKFYK
    160 170 180 190 200
    RRINKLMKEL ESIKIFKEKS IESNKRNNIP SIGIVGYTNS GKTSLFNSLT
    210 220 230 240 250
    GLTQKVDTKL FTTMSPKRYA IPINNRKIML VDTVGFIRGI PPQIVDAFFV
    260 270 280 290 300
    TLSEAKYSDA LILVIDSTFS ENLLIETLQS SFEILREIGV SGKPILVTLN
    310 320 330 340 350
    KIDKINGDLY KKLDLVEKLS KELYSPIFDV IPISALKRTN LELLRDKIYQ

    LATQLS
    Length:356
    Mass (Da):40,538
    Last modified:October 1, 2001 - v1
    Checksum:i602D4DBBE3BEAB1C
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE006641 Genomic DNA. Translation: AAK40607.1.
    PIRiH90168.
    RefSeqiWP_009990543.1. NC_002754.1.

    Genome annotation databases

    EnsemblBacteriaiAAK40607; AAK40607; SSO0269.
    GeneIDi27426564.
    KEGGisso:SSO0269.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE006641 Genomic DNA. Translation: AAK40607.1.
    PIRiH90168.
    RefSeqiWP_009990543.1. NC_002754.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QTFX-ray2.00A1-356[»]
    2QTHX-ray2.00A1-356[»]
    3KXIX-ray2.65A1-356[»]
    3KXKX-ray2.35A/B1-356[»]
    3KXLX-ray2.50A/B1-356[»]
    ProteinModelPortaliQ980M3.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi273057.SSO0269.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAK40607; AAK40607; SSO0269.
    GeneIDi27426564.
    KEGGisso:SSO0269.

    Phylogenomic databases

    eggNOGiarCOG00353. Archaea.
    COG2262. LUCA.
    HOGENOMiHOG000260368.
    InParanoidiQ980M3.
    KOiK03665.
    OMAiKWQLVLE.

    Enzyme and pathway databases

    BioCyciSSOL273057:GCH2-257-MONOMER.
    BRENDAi3.6.5.3. 6163.

    Miscellaneous databases

    EvolutionaryTraceiQ980M3.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    HAMAPiMF_00900. GTPase_HflX.
    InterProiIPR030394. G_HFLX_dom.
    IPR032305. GTP-bd_M.
    IPR006073. GTP_binding_domain.
    IPR016496. GTPase_HflX.
    IPR025121. GTPase_HflX_N.
    IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    [Graphical view]
    PANTHERiPTHR10229. PTHR10229. 1 hit.
    PfamiPF16360. GTP-bdg_M. 1 hit.
    PF13167. GTP-bdg_N. 1 hit.
    PF01926. MMR_HSR1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006809. GTP-binding_hflX_prd. 1 hit.
    PRINTSiPR00326. GTP1OBG.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR03156. GTP_HflX. 1 hit.
    TIGR00231. small_GTP. 1 hit.
    PROSITEiPS51705. G_HFLX. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
    2. "An HflX-Type GTPase from Sulfolobus solfataricus binds to the 50S ribosomal subunit in all nucleotide-bound states."
      Blombach F., Launay H., Zorraquino V., Swarts D.C., Cabrita L.D., Benelli D., Christodoulou J., Londei P., van der Oost J.
      J. Bacteriol. 193:2861-2867(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, SUBUNIT, INTERACTION WITH 50S SUBUNIT.
      Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
    3. "Functional study on GTP hydrolysis by the GTP-binding protein from Sulfolobus solfataricus, a member of the HflX family."
      Huang B., Wu H., Hao N., Blombach F., van der Oost J., Li X., Zhang X.C., Rao Z.
      J. Biochem. 148:103-113(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF WILD-TYPE IN COMPLEX WITH GDP AND OF MUTANTS PRO-235 AND SER-235, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-189; THR-193; THR-213; GLY-235 AND PHE-236.
    4. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH GDP, FUNCTION AS A GTPASE, ENZYME REGULATION, SUBUNIT.

    Entry informationi

    Entry nameiHFLX_SULSO
    AccessioniPrimary (citable) accession number: Q980M3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: October 1, 2001
    Last modified: July 6, 2016
    This is version 105 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.