LON_HELPY
ID LON_HELPY Reviewed; 835 AA.
AC P55995;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
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=HP_1379;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
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; AE000511; AAD08421.1; -; Genomic_DNA.
DR PIR; C64692; C64692.
DR RefSeq; NP_208170.1; NC_000915.1.
DR RefSeq; WP_000133787.1; NC_018939.1.
DR AlphaFoldDB; P55995; -.
DR SMR; P55995; -.
DR DIP; DIP-3184N; -.
DR IntAct; P55995; 7.
DR MINT; P55995; -.
DR STRING; 85962.C694_07120; -.
DR MEROPS; S16.001; -.
DR PaxDb; P55995; -.
DR EnsemblBacteria; AAD08421; AAD08421; HP_1379.
DR KEGG; hpy:HP_1379; -.
DR PATRIC; fig|85962.47.peg.1477; -.
DR eggNOG; COG0466; Bacteria.
DR OMA; KKMNPVM; -.
DR PhylomeDB; P55995; -.
DR Proteomes; UP000000429; 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; IBA:GO_Central.
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; IBA:GO_Central.
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..835
FT /note="Lon protease"
FT /id="PRO_0000076137"
FT DOMAIN 9..200
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 636..835
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 574..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 741
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 784
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 835 AA; 94419 MW; 4BDA52814191C727 CRC64;
MTEDFPKILP LLVEEDTFLY PFMIAPIFLQ NNASIKAVAY AKNNKSLVFI ACQKDKLNDN
EAPYYDVGVI GSVMREANMP NGRVKLLFNG IAKGRILEPA KENEQGFLEA QISPIEYLEY
DKENIQAIVE VLKEKVITLA NVSSLFPPDL IKALEDNDDP NRIADLIAAA LHLKKDQAYS
LFANNNTEQR LLDLIDIVIE ETKTQKLQKE IKSKVHQKME QTNKEYFLKE QLKQIQKELG
TDKQRDEDLN QYYQKLESIK PFLKEEAFKE IKKQIDRLSR THADSSDSAT LQNYIETMLD
VPFGQYGKKA LDIKHVREQL DKDHYSLKRP KERIVEYFAT MQLLEMRRKK KPEKKDKTKG
TILCFYGPPG VGKTSLANSI AKAIERPLVR IALGGLEDVN ELRGHRRTYI GSMPGRIVQG
LIEAKKMNPV MVLDEIDKVD RSVRGDPASA LLEILDPEQN TAFRDHYANF SIDLSQVIFI
ATANNIDRIP APLRDRMEFI SVSSYTPNEK EEIAKNYLIP QELEKHALKP SEVEISHECL
KLIIEKYTRE AGVRDLRRQI ATIMRKVALK YLEDNPHQKG RTKKGKNEKS EDQKSEDQKS
ENQKSENKDF CVSITPNNLK EYLERMVFEI DPIDEENKIG IVNGLAWTPV GGDVLKIEVL
KIRGKGELKL TGSLGDVMKE SAIIAFSVVK VLLDNETLKV PKIPSETDAE GKKKKKVLKV
YNAYDLHLHV PEGATPKDGP SAGIAMASVM ASILCDRATR SEVAMTGELT LSGEVLPIGG
LKEKLIAAFK AGIKTALIPV KNYERDLDEI PAEVRENLNI VAVKNIAEVL EKTLL
