LONB_THEKO
ID LONB_THEKO Reviewed; 635 AA.
AC Q8NKS6; Q5JGL4;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Archaeal Lon protease;
DE EC=3.4.21.-;
DE AltName: Full=LonTk;
GN Name=lon; OrderedLocusNames=TK1264;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=12057965; DOI=10.1128/jb.184.13.3689-3698.2002;
RA Fukui T., Eguchi T., Atomi H., Imanaka T.;
RT "A membrane-bound archaeal Lon protease displays ATP-independent
RT proteolytic activity towards unfolded proteins and ATP-dependent activity
RT for folded proteins.";
RL J. Bacteriol. 184:3689-3698(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Serine protease that displays ATP-independent proteolytic
CC activity towards peptides and unfolded proteins and ATP-dependent
CC activity for the cleavage of folded proteins.
CC {ECO:0000269|PubMed:12057965}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:12057965};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:12057965};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12057965};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:12057965};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:12057965};
CC Note=Mg(2+). Exhibits no peptide cleavage activity without Mg(2+),
CC regardless of the presence or the absence of ATP. Can also use other
CC divalent cations such as Ni(2+), Ca(2+), Mn(2+) and Co(2+).
CC {ECO:0000269|PubMed:12057965};
CC -!- ACTIVITY REGULATION: ADP inhibits the peptide cleavage activity of
CC LonTk, but the enzyme retains 57% activity in comparison to the
CC condition with the addition of ATP. {ECO:0000269|PubMed:12057965}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9 for the ATP-independent peptide cleavage activity and
CC for ATPase activity. {ECO:0000269|PubMed:12057965};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius for the ATP-independent
CC peptide cleavage activity, and 95 degrees Celsius for ATPase
CC activity. {ECO:0000269|PubMed:12057965};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12057965};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12057965}.
CC -!- DOMAIN: Possesses a two-domain structure consisting of an N-terminal
CC ATPase domain belonging to the AAA(+) superfamily and a C-terminal
CC protease domain. The ATPase domain likely acts as a molecular chaperone
CC functioning in the unfolding of protein structures, along with ATP
CC hydrolysis. {ECO:0000269|PubMed:12057965}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. Archaeal LonB
CC subfamily. {ECO:0000305}.
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DR EMBL; AB066562; BAC00917.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD85453.1; -; Genomic_DNA.
DR RefSeq; WP_011250215.1; NC_006624.1.
DR AlphaFoldDB; Q8NKS6; -.
DR SMR; Q8NKS6; -.
DR STRING; 69014.TK1264; -.
DR MEROPS; S16.A11; -.
DR EnsemblBacteria; BAD85453; BAD85453; TK1264.
DR GeneID; 3234902; -.
DR KEGG; tko:TK1264; -.
DR PATRIC; fig|69014.16.peg.1237; -.
DR eggNOG; arCOG02160; Archaea.
DR HOGENOM; CLU_392630_0_0_2; -.
DR InParanoid; Q8NKS6; -.
DR OMA; GLYFWNL; -.
DR OrthoDB; 7657at2157; -.
DR PhylomeDB; Q8NKS6; -.
DR BRENDA; 3.4.21.53; 5246.
DR Proteomes; UP000000536; 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 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Direct protein sequencing; Hydrolase;
KW Magnesium; Membrane; Nucleotide-binding; Protease; Reference proteome;
KW Serine protease; Transmembrane; Transmembrane helix.
FT CHAIN 1..635
FT /note="Archaeal Lon protease"
FT /id="PRO_0000429042"
FT TOPO_DOM 1..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 435..614
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 521
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 564
FT /evidence="ECO:0000250"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 635 AA; 70258 MW; CCEB5FD3C1A902EC CRC64;
MDEESTKERL IPREYGESLD LGIDFKTTEE IPVPEKLIDQ VIGQEHAVEV IKTAANQRRH
VLLIGEPGTG KSMLGQAMAE LLPTENLEDI LVFPNPEDEN MPKIKTVPAC QGRRIVENYR
RKAKEQEGIK NYLLMFVIFT VILAIIMEPT ATTLLMGMFV VLLSMMVLSN MRFRNTVLVP
KLLVDNCGRK KAPFVDATGA HAGALLGDVR HDPFQSGGLG TPAHERVEPG MIHRAHKGVL
FIDEIATLSL KMQQSLLTAM QEKKFPITGQ SEMSSGAMVR TEPVPCDFIL VAAGNLDTID
KMHPALRSRI RGYGYEVYMR TTMPDTIENR RKLVQFVAQE VKRDGKIPHF TREAVEEIVR
EAQKRAGRKG HLTLRLRDLG GIVRAAGDIA IKKGKKYVER EDVLEAMRMA KPLEKQLADW
YIENKKEYQV IKTEGGEIGR VNGLAVIGEQ SGIVLPIEAV VAPAASKEEG KIIVTGKLGE
IAKEAVQNVS AIIKRYKGED ISRYDIHVQF LQTYEGVEGD SASISVATAV ISALENIPIR
QDVAMTGSLS VRGEVLPIGG ATPKIEAAIE AGIKKVIIPK ANEKDVFLSP DKAEKIEIYP
VETIDQVLEI ALQDGPEKDE LLRRIREALP LYGSS
