VAT_THEAC
ID VAT_THEAC Reviewed; 745 AA.
AC O05209;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=VCP-like ATPase;
GN Name=vat; OrderedLocusNames=Ta0840;
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 [GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=9119075; DOI=10.1016/s0014-5793(97)00138-5;
RA Pamnani V., Tamura T., Lupas A.N., Peters J., Cejka Z., Ashraf W.,
RA Baumeister W.;
RT "Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue
RT from the archaeon Thermoplasma acidophilum.";
RL FEBS Lett. 404:263-268(1997).
RN [2]
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 [3]
RP 3D-STRUCTURE BY ELECTRON TOMOGRAPHY.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=10356978; DOI=10.1016/s0014-5793(99)00431-7;
RA Rockel B., Walz J., Hegerl R., Peters J., Typke D., Baumeister W.;
RT "Structure of VAT, a CDC48/p97 ATPase homologue from the archaeon
RT Thermoplasma acidophilum as studied by electron tomography.";
RL FEBS Lett. 451:27-32(1999).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius.;
CC -!- SUBUNIT: Homohexamer. Forms a ring-shaped particle.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. CDC48 subfamily.
CC {ECO:0000305}.
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DR EMBL; U78072; AAC45089.1; -; Genomic_DNA.
DR EMBL; AL445065; CAC11969.1; -; Genomic_DNA.
DR PIR; T37458; T37458.
DR RefSeq; WP_010901251.1; NC_002578.1.
DR PDB; 1CZ4; NMR; -; A=1-183.
DR PDB; 1CZ5; NMR; -; A=1-183.
DR PDB; 5G4F; EM; 7.00 A; A/B/C/D/E/P=1-726.
DR PDB; 5G4G; EM; 7.80 A; A/B/C/D/E/F=6-726.
DR PDB; 5VC7; EM; 3.90 A; A/C/D/E/F/G=183-745.
DR PDB; 5VCA; EM; 3.90 A; M/N/O/P/Q/R=183-745.
DR PDB; 7DBO; X-ray; 1.90 A; A/B=1-91.
DR PDBsum; 1CZ4; -.
DR PDBsum; 1CZ5; -.
DR PDBsum; 5G4F; -.
DR PDBsum; 5G4G; -.
DR PDBsum; 5VC7; -.
DR PDBsum; 5VCA; -.
DR PDBsum; 7DBO; -.
DR AlphaFoldDB; O05209; -.
DR BMRB; O05209; -.
DR SMR; O05209; -.
DR STRING; 273075.Ta0840; -.
DR EnsemblBacteria; CAC11969; CAC11969; CAC11969.
DR GeneID; 1456383; -.
DR KEGG; tac:Ta0840; -.
DR eggNOG; arCOG01308; Archaea.
DR HOGENOM; CLU_000688_12_2_2; -.
DR OMA; HACHDIK; -.
DR OrthoDB; 2808at2157; -.
DR EvolutionaryTrace; O05209; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR005938; AAA_ATPase_CDC48.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR004201; Cdc48_dom2.
DR InterPro; IPR029067; CDC48_domain_2-like_sf.
DR InterPro; IPR003338; CDC4_N-term_subdom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 2.
DR Pfam; PF17862; AAA_lid_3; 2.
DR Pfam; PF02933; CDC48_2; 1.
DR Pfam; PF02359; CDC48_N; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01072; CDC48_2; 1.
DR SMART; SM01073; CDC48_N; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54585; SSF54585; 1.
DR TIGRFAMs; TIGR01243; CDC48; 1.
DR PROSITE; PS00674; AAA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..745
FT /note="VCP-like ATPase"
FT /id="PRO_0000084624"
FT BINDING 231..238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 508..515
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:7DBO"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:7DBO"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:7DBO"
FT STRAND 41..56
FT /evidence="ECO:0007829|PDB:7DBO"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:7DBO"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:7DBO"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:7DBO"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:7DBO"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:1CZ4"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:1CZ5"
FT HELIX 116..124
FT /evidence="ECO:0007829|PDB:1CZ4"
FT STRAND 149..160
FT /evidence="ECO:0007829|PDB:1CZ4"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1CZ4"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1CZ5"
SQ SEQUENCE 745 AA; 83139 MW; B195EB2044FCF1F2 CRC64;
MESNNGIILR VAEANSTDPG MSRVRLDESS RRLLDAEIGD VVEIEKVRKT VGRVYRARPE
DENKGIVRID SVMRNNCGAS IGDKVKVRKV RTEIAKKVTL APIIRKDQRL KFGEGIEEYV
QRALIRRPML EQDNISVPGL TLAGQTGLLF KVVKTLPSKV PVEIGEETKI EIREEPASEV
LEEVSRISYE DIGGLSEQLG KIREMIELPL KHPELFERLG ITPPKGVILY GPPGTGKTLI
ARAVANESGA NFLSINGPEI MSKYYGQSEQ KLREIFSKAE ETAPSIIFID EIDSIAPKRE
EVQGEVERRV VAQLLTLMDG MKERGHVIVI GATNRIDAID PALRRPGRFD REIEIGVPDR
NGRKEILMIH TRNMPLGMSE EEKNKFLEEM ADYTYGFVGA DLAALVRESA MNALRRYLPE
IDLDKPIPTE ILEKMVVTED DFKNALKSIE PSSLREVMVE VPNVHWDDIG GLEDVKREIK
ETVELPLLKP DVFKRLGIRP SKGFLLYGPP GVGKTLLAKA VATESNANFI SIKGPEVLSK
WVGESEKAIR EIFKKAKQVA PAIVFLDEID SIAPRRGTTS DSGVTERIVN QLLTSLDGIE
VMNGVVVIGA TNRPDIMDPA LLRAGRFDKL IYIPPPDKEA RLSILKVHTK NMPLAPDVDL
NDIAQRTEGY VGADLENLCR EAGMNAYREN PDATSVSQKN FLDALKTIRP SVDEEVIKFY
RTLSETMSKS VSERRKQLQD QGLYL