THSA_AERPE
ID THSA_AERPE Reviewed; 554 AA.
AC Q9YDK6;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Thermosome subunit alpha;
DE AltName: Full=Chaperonin subunit alpha;
DE AltName: Full=Thermosome subunit 1;
GN Name=thsA; OrderedLocusNames=APE_0907.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
CC -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in vitro,
CC and has a weak ATPase activity. {ECO:0000250}.
CC -!- SUBUNIT: Forms a Heterooligomeric complex of two stacked eight-membered
CC rings. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}.
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DR EMBL; BA000002; BAA79891.2; -; Genomic_DNA.
DR PIR; C72686; C72686.
DR AlphaFoldDB; Q9YDK6; -.
DR SMR; Q9YDK6; -.
DR STRING; 272557.APE_0907.1; -.
DR EnsemblBacteria; BAA79891; BAA79891; APE_0907.1.
DR KEGG; ape:APE_0907.1; -.
DR PATRIC; fig|272557.25.peg.657; -.
DR eggNOG; arCOG01257; Archaea.
DR OMA; QTGSNDM; -.
DR BRENDA; 3.6.4.B10; 171.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd03343; cpn60; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR InterPro; IPR017998; Chaperone_TCP-1.
DR InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR InterPro; IPR012714; Thermosome_arc.
DR PANTHER; PTHR11353; PTHR11353; 1.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00304; TCOMPLEXTCP1.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02339; thermosome_arch; 1.
DR PROSITE; PS00750; TCP1_1; 1.
DR PROSITE; PS00751; TCP1_2; 1.
DR PROSITE; PS00995; TCP1_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT CHAIN 1..554
FT /note="Thermosome subunit alpha"
FT /id="PRO_0000128379"
FT REGION 530..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 554 AA; 60374 MW; AC6796A432A256A0 CRC64;
MAATGYPVLI LKEGTQRTYG REALRANILA ARVLAEMLKS SLGPRGLDKM LVDAFGDITV
TNDGATIVKE MEIQHPAAKL LVEVAKAQDA EVGDGTTSVV VLAGALLEKA EKLLDENLHP
TIIIEGYTKA MEEALRLVDE AAVPVEVEDD SVLRRIAETT LASKFVGTGP ERDKIISMVI
DAIRTVAEKR PDGGYEVDLD YVKIEKKKGG SLLDSKLVRG IVLDKEVVHP AMPKRVENAK
ILVLDAPLEV QKPELTTKIR VTDIEKLESF LEEETRMLRD MVEKIAATGA NVVITQKGID
EVAQHFLAKK GILAVRRVKR SDIEKVAKAT GAKIVTSLRD LKPEYLGYAE LVEERKVGED
KMVFIEGAKN PKSVTILLRG ANDMLLDEAE RNIKDALHGL RNILREPKIV GGGGAVEVEL
ALKLKEFART VGGKQQLAIE AYAEALETIP TVLAESAGMD ALEALLKLRS LHSQGYKFAG
VNVLEGKIEE DMTKINVYEP VLVKKQVIKS ASEAAISILK IDDVIAAAPP KKKEKKGKTG
EEEEEEGGGS KFEF