LONB_THEVO
ID LONB_THEVO Reviewed; 655 AA.
AC P58274;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Archaeal Lon protease;
DE EC=3.4.21.-;
DE AltName: Full=ATP-dependent protease La homolog type 1;
GN OrderedLocusNames=TV0493; ORFNames=TVG0479569;
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 -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of mutant and abnormal proteins as well as certain short-
CC lived regulatory proteins. Degrades polypeptides processively (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. Archaeal LonB
CC subfamily. {ECO:0000305}.
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DR EMBL; BA000011; BAB59635.1; -; Genomic_DNA.
DR RefSeq; WP_010916752.1; NC_002689.2.
DR AlphaFoldDB; P58274; -.
DR SMR; P58274; -.
DR STRING; 273116.14324708; -.
DR MEROPS; S16.A11; -.
DR EnsemblBacteria; BAB59635; BAB59635; BAB59635.
DR GeneID; 1441010; -.
DR KEGG; tvo:TVG0479569; -.
DR eggNOG; arCOG02160; Archaea.
DR HOGENOM; CLU_392630_0_0_2; -.
DR OMA; GLYFWNL; -.
DR PhylomeDB; P58274; -.
DR Proteomes; UP000001017; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041699; AAA_32.
DR InterPro; IPR004663; Lon_arc.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR InterPro; IPR002078; Sigma_54_int.
DR PANTHER; PTHR10046; PTHR10046; 1.
DR Pfam; PF13654; AAA_32; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00764; lon_rel; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Hydrolase; Membrane; Nucleotide-binding;
KW Protease; Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..655
FT /note="Archaeal Lon protease"
FT /id="PRO_0000076155"
FT TOPO_DOM 1..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 433..618
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 525
FT /evidence="ECO:0000250"
FT ACT_SITE 568
FT /evidence="ECO:0000250"
FT BINDING 57..64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 655 AA; 71341 MW; 9DA7A252DA261C1D CRC64;
MEENIESVEE WVSKLDIETT KDIHVPKLLF DQVIGQDQAG EIVKKAALQR RHVILIGEPG
TGKSMLAQSM VDFLPKSELE DILVFPNPED PNKPKIKTVP AGKGKEIVRQ YQIKAEREKR
DRSRSIMFVI FSVVLLGIIA AIVLRSITLI FFAIMAAAFL YMAMAFNPVI RNEKAMVPKL
LVSHSSTDKP PFVDSTGAHS GALLGDVRHD PFQSGGLETP AHERVEAGNI HKAHKGVLFI
DEINLLRPED QQAILTALQE KKYPISGQSE RSAGAMVQTE PVPCDFVLVA AGNYDAIRNM
HPALRSRIRG YGYEVVVNDY MDDNDENRKK LVQFIAQEVE KDKKIPHFDK SAIVEIIKEA
QKRSGRRNKL TLRLRELGGL VRVAGDIAVS QKRNIVTASD VIAAKALSKP LEQQIADKSI
EIKKIYKTFR TEGSVVGMVN GLAVVGADTG MAEYTGVVLP IVAEVTPAEH KGAGNIIATG
KLGDIAKEAV LNVSAVFKKI TGKDISNMDI HIQFVGTYEG VEGDSASVSI ATAVISAIEN
IPVDQSVAMT GSLSVRGDVL PVGGVTAKVE AAIEAGMAKV IVPELNYNDI ILDAEHINRI
QIIPARTIED VLKVALVNSP EKDKLFDRIA SIINNAKIIK PQKPVASTRA GQNVA
