LON2_THET2
ID LON2_THET2 Reviewed; 804 AA.
AC Q72JM6;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Lon protease 2 {ECO:0000255|HAMAP-Rule:MF_01973};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973};
DE AltName: Full=ATP-dependent protease La 2 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon2 {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=TT_C0746;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(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. Required for cellular homeostasis and for
CC survival from DNA damage and developmental changes induced by stress.
CC Degrades polypeptides processively to yield small peptide fragments
CC that are 5 to 10 amino acids long. Binds to DNA in a double-stranded,
CC site-specific manner. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01973};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_01973}.
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DR EMBL; AE017221; AAS81092.1; -; Genomic_DNA.
DR RefSeq; WP_011173183.1; NC_005835.1.
DR AlphaFoldDB; Q72JM6; -.
DR SMR; Q72JM6; -.
DR STRING; 262724.TT_C0746; -.
DR MEROPS; S16.001; -.
DR PRIDE; Q72JM6; -.
DR EnsemblBacteria; AAS81092; AAS81092; TT_C0746.
DR KEGG; tth:TT_C0746; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_0; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0034605; P:cellular response to heat; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01973; lon_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027543; Lon_bac.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; PTHR10046; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR PIRSF; PIRSF001174; Lon_proteas; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Serine protease; Stress response.
FT CHAIN 1..804
FT /note="Lon protease 2"
FT /id="PRO_0000396610"
FT DOMAIN 6..197
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 598..779
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 685
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 728
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 362..369
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 804 AA; 90513 MW; A7DB7782AC90FF33 CRC64;
MLPETMPVCP VRGSVIYPTM VMPIDAGRPI SIRAIDEALA RDRVLLIVSQ RDKEVETPRP
SDLFEVGTAC NILKMRKNPD GSVQVLVQAF ARVRVREWLD LGDHLEARGE VLADEPGEPI
LVKALVREVK DKFQALLKEG KYLAPEVAQF ILNLEDPSQL ADYVAFHMDF RLEDKQKVLE
TANVAERLRA VLVLLEAELA LIETQRRIQQ QVKEEIDRNQ REYFLREQMK AIQRELHGEE
GEQEVEEFRR KLEALDLPPV VRQEVERELN RFARMHPDSA EASVIRTYLD WIVNLPWNTR
TEDNLDLERA KEILERDHYG LEKVKDRVLE YLAVRKLKAE RAKRGEIPPD EVNKGPILLF
VGPPGVGKTS IAKSIAEALG RKYVRVSLGG VRDESDIRGH RRTYIGAMPG RIIQGLRQAG
TKNPVFLLDE VDKLGISYQG DPAAALLEVL DPAQNKEFVD HYLGVPFDLS EVMFICTANF
PQNIPAPLYD RMEPIEFTSY TEQEKLEIAK RYLLPRQLKE NGLEPEQVVV TEAALTRLIT
HYTREAGVRQ LEREIGALLR KAARRILEEG KKRVRITEKD LEAYLGPPRF LPETEAREPQ
VGVATGMYYT PVGGDIMFVE VSVMPGKGNL ILTGQLGDVM KESARAALSY AKKNALRFGI
PLEKFDKSDI HIHVPAGAIP KEGPSAGVAL VSALVSALTE VPVRHDIAMT GEITLTGRVL
PIGGVKEKVL GARRAGIREV ILPKLNEPDL ADIPKPLRQN MTFHFVEHLD QVLDLALVGG
LKALEERGRR SRSARRKKEL VAHA
