LONH_THEVO
ID LONH_THEVO Reviewed; 495 AA.
AC P58275;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Putative lon protease homolog;
DE EC=3.4.21.-;
DE AltName: Full=ATP-dependent protease La homolog;
GN OrderedLocusNames=TV0156; ORFNames=TVG0165728;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Ser-Lys catalytic dyad essential for
CC proteolytic activity. Its enzyme activity is therefore unsure.
CC {ECO:0000305}.
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DR EMBL; BA000011; BAB59298.1; -; Genomic_DNA.
DR RefSeq; WP_010916411.1; NC_002689.2.
DR AlphaFoldDB; P58275; -.
DR SMR; P58275; -.
DR STRING; 273116.14324370; -.
DR EnsemblBacteria; BAB59298; BAB59298; BAB59298.
DR GeneID; 1441641; -.
DR KEGG; tvo:TVG0165728; -.
DR eggNOG; arCOG02162; Archaea.
DR HOGENOM; CLU_550564_0_0_2; -.
DR OMA; HDPYGGH; -.
DR OrthoDB; 7657at2157; -.
DR PhylomeDB; P58275; -.
DR Proteomes; UP000001017; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041699; AAA_32.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002078; Sigma_54_int.
DR PANTHER; PTHR10046; PTHR10046; 2.
DR Pfam; PF13654; AAA_32; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Nucleotide-binding; Protease; Serine protease.
FT CHAIN 1..495
FT /note="Putative lon protease homolog"
FT /id="PRO_0000076158"
FT REGION 471..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52..59
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 495 AA; 55620 MW; 86F298A307DD930B CRC64;
MGSVYVNFFE EYPDTSYIKI PNNPLDRVIG QDEAVRIASV AARQRRHLLL VGPPGVGKSM
IAQALSFYIG RPNEEIRVVH NPQYPERPFV EIKTREEVML EREEESSTSG TLIDPKDAPT
SVAERLGYRC SKCGFYSSPT EMVCPNCNSP KAQIGTQGPF GDVFNVIGAA FGVQNNVDKV
TLTRRNGDHD EIVVYERYND KIRVLDEKTL ERRRRLEKKS PSKTIVPIDR NPFVLATGAS
ETELLGDVRH DPYGGHPQLG TLPYERVIAG AVHEAHEGVL FIDEITHLGN LQRYILTAMQ
EKVFPITGRN PQSAGASVRV DKVPADFILV AACNINDLPY ILSPLRSRIV GNGYEILMKT
TMKDTEENRM KYLQFIAQEI NMDGKIPHMT MDAAQLIIEE GRKRAKLIDR KNNELTLRLR
ELGGLIRAAG DIAVFKGNKL IDKEDVEEAI KLYVPVEEKI MKEYGSMAAA YSSETTGSQR
DSTYNYANMD DRSYE
