ACTH_THEAC
ID ACTH_THEAC Reviewed; 326 AA.
AC Q9HKL4;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Archaeal actin homolog;
GN OrderedLocusNames=Ta0583;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=17189356; DOI=10.1128/jb.01454-06;
RA Hara F., Yamashiro K., Nemoto N., Ohta Y., Yokobori S., Yasunaga T.,
RA Hisanaga S., Yamagishi A.;
RT "An actin homolog of the archaeon Thermoplasma acidophilum that retains the
RT ancient characteristics of eukaryotic actin.";
RL J. Bacteriol. 189:2039-2045(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADP, FUNCTION, ATPASE
RP ACTIVITY, AND KINETIC PARAMETERS.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=16500678; DOI=10.1016/j.jmb.2006.01.096;
RA Roeben A., Kofler C., Nagy I., Nickell S., Hartl F.U., Bracher A.;
RT "Crystal structure of an archaeal actin homolog.";
RL J. Mol. Biol. 358:145-156(2006).
CC -!- FUNCTION: Polymerizes into bundles of filaments, forming a helix with a
CC filament width of 5.5 nm and an axial repeating unit of 5.5 nm.
CC Polymerization of Ta0583 requires NTP and is optimal with ATP, but GTP,
CC UTP, CTP, and even the deoxy form of NTP can also support the
CC polymerization reaction. Nucleoside diphosphate or AMP-PNP does not
CC support polymerization. {ECO:0000269|PubMed:16500678,
CC ECO:0000269|PubMed:17189356}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=289 uM for ATP (when assaying the ATPase activity)
CC {ECO:0000269|PubMed:16500678, ECO:0000269|PubMed:17189356};
CC pH dependence:
CC Optimum pH is 4.5-5.5 for the polymerization reaction.
CC {ECO:0000269|PubMed:17189356};
CC Temperature dependence:
CC Optimum temperature is 50-56 degrees Celsius for the polymerization
CC reaction. {ECO:0000269|PubMed:17189356};
CC -!- MISCELLANEOUS: Mg(2+) is required for polymerization. 4 mM MgCl(2) is
CC sufficient to enhance the polymerization; however, higher
CC concentrations of MgCl(2) suppresses polymerization. Polymerization is
CC also suppressed by addition of NaCl, KCl or CaCl(2), with half
CC suppression by about 100 mM, 10 mM and 18 mM, respectively.
CC -!- SIMILARITY: Belongs to the thermophilic archaeal actin family.
CC {ECO:0000305}.
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DR EMBL; AL445064; CAC11723.1; -; Genomic_DNA.
DR RefSeq; WP_010901008.1; NC_002578.1.
DR PDB; 2FSJ; X-ray; 1.90 A; A=1-326.
DR PDB; 2FSK; X-ray; 2.10 A; A/B=1-326.
DR PDB; 2FSN; X-ray; 2.90 A; A/B=1-326.
DR PDBsum; 2FSJ; -.
DR PDBsum; 2FSK; -.
DR PDBsum; 2FSN; -.
DR AlphaFoldDB; Q9HKL4; -.
DR SMR; Q9HKL4; -.
DR STRING; 273075.Ta0583; -.
DR EnsemblBacteria; CAC11723; CAC11723; CAC11723.
DR GeneID; 1456173; -.
DR KEGG; tac:Ta0583; -.
DR eggNOG; arCOG03062; Archaea.
DR HOGENOM; CLU_851534_0_0_2; -.
DR OMA; TESWGIG; -.
DR OrthoDB; 68684at2157; -.
DR EvolutionaryTrace; Q9HKL4; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd10227; ParM_like; 1.
DR InterPro; IPR040607; ALP_N.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR042051; ParM-like.
DR Pfam; PF17989; ALP_N; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..326
FT /note="Archaeal actin homolog"
FT /id="PRO_0000285695"
FT BINDING 10..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 231
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 285..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2FSJ"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:2FSK"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2FSK"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:2FSN"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 127..132
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 138..150
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 153..161
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 169..177
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:2FSJ"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 206..221
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 248..270
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 271..276
FT /evidence="ECO:0007829|PDB:2FSJ"
FT STRAND 277..284
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:2FSJ"
FT TURN 307..312
FT /evidence="ECO:0007829|PDB:2FSJ"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:2FSJ"
SQ SEQUENCE 326 AA; 34880 MW; 6F1DB85F2D6E68AC CRC64;
MVVVGLDVGY GDTKVIGVDG KRIIFPSRWA VTETESWGIG GKIPVLSTDG GQTKFIYGKY
ASGNNIRVPQ GDGRLASKEA FPLIAAALWE SGIHNDGSPV DLVIGSGTPL GTFDLEVKAA
KEALENKVLT VTGPEGEVRQ FNITRLIMRP QGVGAALYLL NQGIIEQQPG YGVVIDVGSR
TTDVLTINLM DMEPVVELSF SLQIGVGDAI SALSRKIAKE TGFVVPFDLA QEALSHPVMF
RQKQVGGPEV SGPILEDLAN RIIENIRLNL RGEVDRVTSL IPVGGGSNLI GDRFEEIAPG
TLVKIKPEDL QFANALGYRD AAERSM
