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Protein

Archaeal actin homolog

Gene

Ta0583

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Polymerizes into bundles of filaments, forming a helix with a filament width of 5.5 nm and an axial repeating unit of 5.5 nm. Polymerization of Ta0583 requires NTP and is optimal with ATP, but GTP, UTP, CTP, and even the deoxy form of NTP can also support the polymerization reaction. Nucleoside diphosphate or AMP-PNP does not support polymerization.2 Publications

Kineticsi

  1. KM=289 µM for ATP (when assaying the ATPase activity)2 Publications

    pH dependencei

    Optimum pH is 4.5-5.5 for the polymerization reaction.1 Publication

    Temperature dependencei

    Optimum temperature is 50-56 degrees Celsius for the polymerization reaction.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei179 – 1791ATP; via amide nitrogen
    Binding sitei231 – 2311ATP
    Binding sitei311 – 3111ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 145ATP
    Nucleotide bindingi285 – 2884ATP

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Archaeal actin homolog
    Gene namesi
    Ordered Locus Names:Ta0583
    OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
    Taxonomic identifieri273075 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
    Proteomesi
    • UP000001024 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 326326Archaeal actin homologPRO_0000285695Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi273075.Ta0583.

    Structurei

    Secondary structure

    1
    326
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 87Combined sources
    Beta strandi10 – 167Combined sources
    Helixi18 – 203Combined sources
    Beta strandi22 – 276Combined sources
    Beta strandi29 – 324Combined sources
    Turni40 – 423Combined sources
    Beta strandi46 – 494Combined sources
    Beta strandi52 – 576Combined sources
    Helixi58 – 603Combined sources
    Beta strandi63 – 653Combined sources
    Beta strandi75 – 773Combined sources
    Turni78 – 803Combined sources
    Helixi81 – 9111Combined sources
    Beta strandi100 – 1089Combined sources
    Helixi110 – 1123Combined sources
    Helixi113 – 12412Combined sources
    Beta strandi127 – 1326Combined sources
    Helixi134 – 1363Combined sources
    Beta strandi138 – 15013Combined sources
    Helixi153 – 1619Combined sources
    Beta strandi169 – 1779Combined sources
    Beta strandi182 – 1887Combined sources
    Turni189 – 1913Combined sources
    Helixi196 – 1983Combined sources
    Beta strandi200 – 2034Combined sources
    Helixi206 – 22116Combined sources
    Helixi227 – 2337Combined sources
    Beta strandi238 – 2403Combined sources
    Beta strandi243 – 2453Combined sources
    Helixi248 – 27023Combined sources
    Helixi271 – 2766Combined sources
    Beta strandi277 – 2848Combined sources
    Helixi287 – 2904Combined sources
    Helixi291 – 2977Combined sources
    Turni307 – 3126Combined sources
    Helixi313 – 32311Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FSJX-ray1.90A1-326[»]
    2FSKX-ray2.10A/B1-326[»]
    2FSNX-ray2.90A/B1-326[»]
    ProteinModelPortaliQ9HKL4.
    SMRiQ9HKL4. Positions 1-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HKL4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thermophilic archaeal actin family.Curated

    Phylogenomic databases

    eggNOGiarCOG03061. Archaea.
    COG1077. LUCA.
    HOGENOMiHOG000033795.
    OMAiASKEAFP.

    Sequencei

    Sequence statusi: Complete.

    Q9HKL4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVVVGLDVGY GDTKVIGVDG KRIIFPSRWA VTETESWGIG GKIPVLSTDG
    60 70 80 90 100
    GQTKFIYGKY ASGNNIRVPQ GDGRLASKEA FPLIAAALWE SGIHNDGSPV
    110 120 130 140 150
    DLVIGSGTPL GTFDLEVKAA KEALENKVLT VTGPEGEVRQ FNITRLIMRP
    160 170 180 190 200
    QGVGAALYLL NQGIIEQQPG YGVVIDVGSR TTDVLTINLM DMEPVVELSF
    210 220 230 240 250
    SLQIGVGDAI SALSRKIAKE TGFVVPFDLA QEALSHPVMF RQKQVGGPEV
    260 270 280 290 300
    SGPILEDLAN RIIENIRLNL RGEVDRVTSL IPVGGGSNLI GDRFEEIAPG
    310 320
    TLVKIKPEDL QFANALGYRD AAERSM
    Length:326
    Mass (Da):34,880
    Last modified:March 1, 2001 - v1
    Checksum:i6F1DB85F2D6E68AC
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL445064 Genomic DNA. Translation: CAC11723.1.
    RefSeqiWP_010901008.1. NC_002578.1.

    Genome annotation databases

    EnsemblBacteriaiCAC11723; CAC11723; CAC11723.
    GeneIDi1456173.
    KEGGitac:Ta0583.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL445064 Genomic DNA. Translation: CAC11723.1.
    RefSeqiWP_010901008.1. NC_002578.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FSJX-ray1.90A1-326[»]
    2FSKX-ray2.10A/B1-326[»]
    2FSNX-ray2.90A/B1-326[»]
    ProteinModelPortaliQ9HKL4.
    SMRiQ9HKL4. Positions 1-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi273075.Ta0583.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAC11723; CAC11723; CAC11723.
    GeneIDi1456173.
    KEGGitac:Ta0583.

    Phylogenomic databases

    eggNOGiarCOG03061. Archaea.
    COG1077. LUCA.
    HOGENOMiHOG000033795.
    OMAiASKEAFP.

    Miscellaneous databases

    EvolutionaryTraceiQ9HKL4.

    Family and domain databases

    ProtoNetiSearch...

    Entry informationi

    Entry nameiACTH_THEAC
    AccessioniPrimary (citable) accession number: Q9HKL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 2007
    Last sequence update: March 1, 2001
    Last modified: November 11, 2015
    This is version 61 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Mg2+ is required for polymerization. 4 mM MgCl2 is sufficient to enhance the polymerization; however, higher concentrations of MgCl2 suppresses polymerization. Polymerization is also suppressed by addition of NaCl, KCl or CaCl2, with half suppression by about 100 mM, 10 mM and 18 mM, respectively.

    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.