ID V5NN19_HELPX Unreviewed; 834 AA.
AC V5NN19;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
DE AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973};
GN Name=lon {ECO:0000256|HAMAP-Rule:MF_01973};
GN ORFNames=U064_0084 {ECO:0000313|EMBL:AHA89032.1};
OS Helicobacter pylori BM012S.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1407463 {ECO:0000313|EMBL:AHA89032.1, ECO:0000313|Proteomes:UP000018543};
RN [1] {ECO:0000313|EMBL:AHA89032.1, ECO:0000313|Proteomes:UP000018543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BM012S {ECO:0000313|EMBL:AHA89032.1,
RC ECO:0000313|Proteomes:UP000018543};
RX DOI=10.1371/journal.pone.0082187;
RA Linz B., Windsor H.M., Gajewski J.P., Hake C.M., Drautz D.I.,
RA Schuster S.C., Marshall B.J.;
RT "Helicobacter pylori genomic microevolution during naturally occurring
RT transmission between adults.";
RL PLoS ONE 8:E82187-E82187(2013).
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:0000256|HAMAP-Rule:MF_01973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01973,
CC ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}.
CC -!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
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DR EMBL; CP006889; AHA89032.1; -; Genomic_DNA.
DR RefSeq; WP_023591528.1; NC_022911.1.
DR AlphaFoldDB; V5NN19; -.
DR KEGG; hez:U064_0084; -.
DR PATRIC; fig|1407463.3.peg.84; -.
DR HOGENOM; CLU_004109_4_3_7; -.
DR Proteomes; UP000018543; 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 CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR43718; LON PROTEASE; 1.
DR PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 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 PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01973};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973,
KW ECO:0000256|PIRNR:PIRNR001174};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01973};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_01973};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01973}.
FT DOMAIN 9..200
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 635..834
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 574..608
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 740
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 783
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 367..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 834 AA; 94083 MW; BEA8C7822431D8A0 CRC64;
MTEDFPKILP LLVEEDTFLY PFMIAPIFLQ NNASIKAVAY AKNNKSLVFI ACQKDKLNDN
EAPYYDVGVI GSVMREANMP NGRVKLLFNG IAKGRILEPA KENEQGFLEA QISPIEYLEY
DKENIQAIVE VLKEKVITLA NVSSLFPPDL IKALEDNDDP NRIADLIAAA LHLKRDQAYS
LFANNNTEQR LLDLIDIVIE ETKTQKLQKE IKSKVHQKME QTNKEYFLKE QLKQIQKELG
TDKQRDEDLN QYYQKLESIK PFLKEEAFKE IKKQIDRLSR THADSSDSAT LQNYIETMLD
VPFGQYGKKA LDIKHVREQL DKDHYSLKRP KERIVEYFAT MQLLEMRRKK KPEKKDKAKG
TILCFYGPPG VGKTSLANSI AKAIERPLVR IALGGLEDVN ELRGHRRTYI GSMPGRIVQG
LIEAKKMNPV MVLDEIDKVD RSVRGDPASA LLEILDPEQN TAFRDHYANF SIDLSQVIFI
ATANNIDRIP APLRDRMEFI SVSSYTPNEK EEIAKNYLIP QELEKHALKP SEVDISHECL
KLIIEKYTRE AGVRDLRRQI ATIMRKVALK YLEDNPHQKG RTKKSENEKS EDKKSENKEN
EKRGGNKDFC VSITPNNLKE YLERMVFEID PIDGENKIGI VNGLAWTPVG GDVLKIEALK
IRGKGELKLT GSLGDVMKES ALIAFSVVKA LLDNETLKAP KIPNETDAEG KKKKKALKVY
NAYDLHLHVP EGATPKDGPS AGIAMASVIA SILCDRATRS EVAMTGELTL SGEVLPIGGL
KEKLIAAFKA GIKTALVPVK NYERDLDEIP AEVRENLNIV AVKNIAEVLE KTLL
//
