LONB_THEAC
ID LONB_THEAC Reviewed; 657 AA.
AC Q9HJ89;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Archaeal Lon protease;
DE EC=3.4.21.-;
DE AltName: Full=ATP-dependent protease La homolog;
GN OrderedLocusNames=Ta1081;
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, SUBUNIT, MUTAGENESIS OF SER-525 AND LYS-568, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15560777; DOI=10.1111/j.1432-1033.2004.04421.x;
RA Besche H., Zwickl P.;
RT "The Thermoplasma acidophilum Lon protease has a Ser-Lys dyad active
RT site.";
RL Eur. J. Biochem. 271:4361-4365(2004).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-63; ASP-241;
RP ASN-293; ARG-305; ARG-375 AND ARG-382.
RX PubMed=15358558; DOI=10.1016/j.febslet.2004.08.021;
RA Besche H., Tamura N., Tamura T., Zwickl P.;
RT "Mutational analysis of conserved AAA+ residues in the archaeal Lon
RT protease from Thermoplasma acidophilum.";
RL FEBS Lett. 574:161-166(2004).
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.
CC {ECO:0000269|PubMed:15358558, ECO:0000269|PubMed:15560777}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.196 mM for ATP {ECO:0000269|PubMed:15560777};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000269|PubMed:15560777}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; 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; AL445066; CAC12209.1; -; Genomic_DNA.
DR RefSeq; WP_010901491.1; NC_002578.1.
DR AlphaFoldDB; Q9HJ89; -.
DR SMR; Q9HJ89; -.
DR STRING; 273075.Ta1081; -.
DR MEROPS; S16.A11; -.
DR EnsemblBacteria; CAC12209; CAC12209; CAC12209.
DR GeneID; 1456593; -.
DR KEGG; tac:Ta1081; -.
DR eggNOG; arCOG02160; Archaea.
DR HOGENOM; CLU_392630_0_0_2; -.
DR OMA; GLYFWNL; -.
DR OrthoDB; 7657at2157; -.
DR BRENDA; 3.4.21.53; 6324.
DR SABIO-RK; Q9HJ89; -.
DR Proteomes; UP000001024; 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 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 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Hydrolase; Membrane; Nucleotide-binding;
KW Protease; Reference proteome; Serine protease; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..657
FT /note="Archaeal Lon protease"
FT /id="PRO_0000076154"
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..657
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"
FT MUTAGEN 63
FT /note="K->A: Completely abolishes ATPase activity and makes
FT peptidase activity independent on ATP stimulus."
FT /evidence="ECO:0000269|PubMed:15358558"
FT MUTAGEN 241
FT /note="D->A: Retains 5% ATPase activity. Proteolytic
FT activity is greatly impaired and cannot be stimulated by
FT nucleotides."
FT /evidence="ECO:0000269|PubMed:15358558"
FT MUTAGEN 293
FT /note="N->A: Severely reduces ATPase and proteolytic
FT activity."
FT /evidence="ECO:0000269|PubMed:15358558"
FT MUTAGEN 305
FT /note="R->A: Decreases ATPase activity. Completely
FT abolishes peptidase activity in the absence of ATP, but
FT ATP-stimulated peptidase activity i close to wild-type
FT levels."
FT /evidence="ECO:0000269|PubMed:15358558"
FT MUTAGEN 375
FT /note="R->A: Almost completely abolishes ATPase activity
FT and severely reduces proteolytic activity."
FT /evidence="ECO:0000269|PubMed:15358558"
FT MUTAGEN 382
FT /note="R->A: Decreases ATPase activity. Completely
FT abolishes peptidase activity in the absence of ATP, but
FT ATP-stimulated peptidase activity i close to wild-type
FT levels."
FT /evidence="ECO:0000269|PubMed:15358558"
FT MUTAGEN 525
FT /note="S->A: Abolishes peptidase activity, but retains
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:15560777"
FT MUTAGEN 568
FT /note="K->A: Abolishes peptidase activity, but retains
FT ATPase activity."
FT /evidence="ECO:0000269|PubMed:15560777"
SQ SEQUENCE 657 AA; 71601 MW; FD465CD99F5B38F7 CRC64;
MEENIESVEE WVNKLDIETT KDIHVPKLLF DQVIGQDQAG EIVKKAALQR RHVILIGEPG
TGKSMLAQSM VDFLPKSELE DILVFPNPED PNKPKIKTVP AGKGKEIVRQ YQIKAEREKR
DRSRSIMFVI FSVVLLGIIA AIVLRSITLI FFAIMAAAFL YMAMAFNPVI RNERAMVPKL
LVSHNPNDKP PFVDSTGAHS GALLGDVRHD PFQSGGLETP AHERVEAGNI HKAHKGVLFI
DEINLLRPED QQAILTALQE KKYPISGQSE RSAGAMVQTE PVPCDFVLVA AGNYDAIRNM
HPALRSRIRG YGYEVVVNDY MDDNDENRRK LVQFIAQEVE KDKKIPHFDK SAIIEVIKEA
QKRSGRRNKL TLRLRELGGL VRVAGDIAVS QKKTVVTAAD VIAAKNLAKP LEQQIADRSI
EIKKIYKTFR TEGSVVGMVN GLAVVGADTG MSEYTGVVLP IVAEVTPAEH KGAGNIIATG
KLGDIAKEAV LNVSAVFKKL TGKDISNMDI HIQFVGTYEG VEGDSASVSI ATAVISAIEN
IPVDQSVAMT GSLSVRGDVL PVGGVTAKVE AAIEAGLNKV IVPELNYSDI ILDADHVNKI
EIIPAKTIED VLRVALVNSP EKEKLFDRIS NLINAAKIIK PQRPATPATT RAGNNAA
