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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)DescriptionActionsGraphical viewLength
    Metal bindingi193MagnesiumUniRule annotation1
    Metal bindingi213MagnesiumUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi186 – 193GTPUniRule annotation2 Publications8
    Nucleotide bindingi211 – 215GTPUniRule annotation5
    Nucleotide bindingi232 – 235GTPUniRule annotation4
    Nucleotide bindingi300 – 303GTPUniRule annotation2 Publications4
    Nucleotide bindingi334 – 336GTPUniRule annotation2 Publications3

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Ligandi

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

    Enzyme and pathway databases

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi189N → P: Loss of GTPase activity. 1 Publication1
    Mutagenesisi193T → N: Loss of GTPase activity. 1 Publication1
    Mutagenesisi213T → V: Decrease in GTPase activity. 1 Publication1
    Mutagenesisi235G → P: Loss of GTPase activity. 1 Publication1
    Mutagenesisi235G → S: Decrease in GTPase activity. 1 Publication1
    Mutagenesisi236F → P: Increase in KM for GTP and in GTPase activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004125281 – 356GTPase HflXAdd BLAST356

    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

    1356
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 7Combined sources6
    Turni10 – 12Combined sources3
    Helixi13 – 22Combined sources10
    Beta strandi25 – 31Combined sources7
    Turni39 – 41Combined sources3
    Helixi45 – 52Combined sources8
    Beta strandi59 – 64Combined sources6
    Helixi68 – 78Combined sources11
    Beta strandi82 – 84Combined sources3
    Helixi86 – 97Combined sources12
    Helixi101 – 121Combined sources21
    Helixi145 – 164Combined sources20
    Beta strandi181 – 185Combined sources5
    Turni188 – 191Combined sources4
    Helixi192 – 200Combined sources9
    Beta strandi218 – 223Combined sources6
    Beta strandi226 – 232Combined sources7
    Helixi242 – 244Combined sources3
    Helixi245 – 253Combined sources9
    Helixi254 – 257Combined sources4
    Beta strandi258 – 266Combined sources9
    Helixi271 – 288Combined sources18
    Beta strandi295 – 300Combined sources6
    Helixi302 – 304Combined sources3
    Helixi309 – 323Combined sources15
    Beta strandi327 – 332Combined sources6
    Turni335 – 338Combined sources4
    Helixi341 – 355Combined sources15

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    SMRiQ980M3.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ980M3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini180 – 356Hflx-type GUniRule annotationAdd BLAST177

    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.
    OMAiYGYEKYY.

    Family and domain databases

    CDDicd01878. HflX. 1 hit.
    Gene3Di3.40.50.300. 2 hits.
    HAMAPiMF_00900. GTPase_HflX. 1 hit.
    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
    PDB 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.
    SMRiQ980M3.
    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.
    OMAiYGYEKYY.

    Enzyme and pathway databases

    BRENDAi3.6.5.3. 6163.

    Miscellaneous databases

    EvolutionaryTraceiQ980M3.

    Family and domain databases

    CDDicd01878. HflX. 1 hit.
    Gene3Di3.40.50.300. 2 hits.
    HAMAPiMF_00900. GTPase_HflX. 1 hit.
    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...

    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: November 2, 2016
    This is version 108 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.