LON_TREPA
ID LON_TREPA Reviewed; 881 AA.
AC O83536;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Lon protease {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 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=TP_0524;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; AE000520; AAC65510.1; -; Genomic_DNA.
DR PIR; B71316; B71316.
DR RefSeq; WP_010881972.1; NC_021490.2.
DR AlphaFoldDB; O83536; -.
DR SMR; O83536; -.
DR STRING; 243276.TPANIC_0524; -.
DR EnsemblBacteria; AAC65510; AAC65510; TP_0524.
DR GeneID; 57879047; -.
DR KEGG; tpa:TP_0524; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_12; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000000811; 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; IPR008268; Peptidase_S16_AS.
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.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Reference proteome; Serine protease; Stress response.
FT CHAIN 1..881
FT /note="Lon protease"
FT /id="PRO_0000076146"
FT DOMAIN 94..285
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 679..861
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 767
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 810
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 440..447
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 881 AA; 97728 MW; 7D1905CD4920B504 CRC64;
MAKNTDIEHD AHEPAGHGDV RESAVENPSA SAVSDGEERA TFAPEVAPQT DTESAQGAAQ
ESEPEVQRAG EAEKGVPEKA KAVVPLDELL PQKVHLIPLT GRPIYPGIFT PLLISDEDDV
RSVESAYSDS GFIGLCLVKT DTQNPTISDL YEVGSVARIV KKINLPDGGL NVFISTQKRF
RIRKHVHHSK PIVAAVQYLS DLIEGDPLEI KALVRGLIGE MKELSENNPL FSEEMRLNMI
NIDHPGKIAD FIASILNISK EEQQRTLEIL DVRKRMEEVF VYIKKEKDLL EIQRKIQNDL
NSRVEKNQRE YFLREELRSI KEELGLTTDP KERDQRKFRA LIDSFHFEGE VKEAVESELE
KLSLTDPNSP EYSVGRTYLE TVLSLPWHAP EKEEYDLKKA QKLLDEDHYG LENVKERIVE
YLAVRKLRAD TKGSIILLVG PPGVGKTSVG KSIARAIHKP FFRFSVGGIS DEAEIKGHRR
TYIGALPGKV LQGLKIVKTK APVFMIDEVD KIGSGARGDP AGALLEVLDP EQNTTFRDHY
LDLPFDLSHI VFVLTANSTD PIPRPLLDRA EIIRLSGYID TEKVEIAKRH LVPKTLEKNG
LKRACVSYRK EVLLHLVHSY ARESGVRGLE KSLDKLHRKL ATEIVLGKRS FDDKCLMDEA
LIGTFLGKPV FRDDMLKDAN KVGTAVGLAW TGMGGDTLLV EAITIPGKAS FKLTGQMGAV
MKESASIALS WLRRYSAQQR IASPNWFEKR AIHLHIPEGA TPKDGPSAGI TMTTTLFSLL
TQQKVKPRLA MTGELSLTGQ VLPIGGLKEK TIAARRGGIK EIIMPKANVR DLDEIPEHVK
KGMVFHLVES MEEVLSLAFP KGKRVRAGTA AQSASPETLT G
