LON_HELPJ
ID LON_HELPJ Reviewed; 831 AA.
AC Q9ZJL3;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 141.
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=jhp_1293;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD06875.1; -; Genomic_DNA.
DR PIR; A71825; A71825.
DR RefSeq; WP_000133766.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZJL3; -.
DR SMR; Q9ZJL3; -.
DR STRING; 85963.jhp_1293; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; AAD06875; AAD06875; jhp_1293.
DR KEGG; hpj:jhp_1293; -.
DR PATRIC; fig|85963.30.peg.1273; -.
DR eggNOG; COG0466; Bacteria.
DR OMA; KKMNPVM; -.
DR Proteomes; UP000000804; 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 Serine protease; Stress response.
FT CHAIN 1..831
FT /note="Lon protease"
FT /id="PRO_0000076138"
FT DOMAIN 9..200
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 632..831
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 574..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 737
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 780
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 367..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 831 AA; 93946 MW; 1B9249B3C49B1D5E CRC64;
MTEDFPKILP LLVEEDTFLY PFMIAPIFLQ NNASIKAVAY AKNNKSLVFI ACQKDKLNDN
EAPYYDVGVI GSVMREANMP NGRVKLLFNG IAKGRILEPA KENEQGFLEA QISPIEYLEY
DKENIQAIVE VLKEKVITLA NVSSLFPPDL IKALEDNDDP NRIADLIAAA LHLKKDQAYF
LFANNNTEQR LLDLIDIVIE ETKTQKLQKE IKSKVHQKME QTNKEYFLKE QLKQIQKELG
TDKQRDEDLN QYYQKLESIK PFLKEEAFKE IKKQIDRLSR THADSSDSAT LQNYVETMLD
VPFGQYEKKA LDIKHVKEQL DNDHYSLKRP KERIVEYFAT MQLLEMRHKK KPEKKDKTKG
TILCFYGPPG VGKTSLANSI AKAIERPLVR IALGGLEDVN ELRGHRRTYI GSMPGRIVQG
LIEAKKMNPV MVLDEIDKVD RSVRGDPASA LLEILDPEQN IAFRDHYANF SIDLSQVIFI
ATANNIDRIP APLRDRMEFI SVSSYTPSEK EEIAKNYLIP QELEKHALKP SEVDISHECL
KLIIEKYTRE AGVRDLRRQI ATIMRKAALK YLEDNPHKKG RTKKSEDKDK KGGNEENEKR
GESKDFCVSI TPDNLKEYLE RMVFEIDPID EENKIGIVNG LAWTPVGGDV LKIEAVKIRG
KGELKLTGSL GDVMKESAII AFSVVKVLLD NETLKVPKIP SETDAENKKK KKVLKVYNAY
DLHLHVPEGA TPKDGPSAGI AMASVMASIL CDRAIRSEVA MTGELTLSGE VLPIGGLKEK
LIAAFKAGIK TALIPVKNYE RDLDEIPTEV RENLNIVAVK NIAEVLEKTL L
