LON_BUCAP
ID LON_BUCAP Reviewed; 777 AA.
AC Q8K988;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=BUsg_461;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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; AE013218; AAM68004.1; -; Genomic_DNA.
DR RefSeq; WP_011053971.1; NC_004061.1.
DR AlphaFoldDB; Q8K988; -.
DR SMR; Q8K988; -.
DR STRING; 198804.BUsg_461; -.
DR MEROPS; S16.001; -.
DR PRIDE; Q8K988; -.
DR EnsemblBacteria; AAM68004; AAM68004; BUsg_461.
DR KEGG; bas:BUsg_461; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_6; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000000416; 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..777
FT /note="Lon protease"
FT /id="PRO_0000076126"
FT DOMAIN 11..202
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 592..773
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 679
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 722
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 777 AA; 87755 MW; 768ACD8B06713DD2 CRC64;
MNSERSERIK IPVLPLRDVV VYPHMVIPLF VGRKKSIHCI ETSMNNDKKI MLIAQKEASK
DEPSTNDLFN IGTISSILQM LKLPDGTVKV LVEGLQRACI KNIESNGEHL VAEVELIISP
TVIDKEQEVL IRTTVNQFES YIKLNKKIPS EILNTLSQTK NAEKLADTIA AHMPLKLADK
QSVLEIYNVN ERLEFLMAIM ETEIDLLKVE KRIRNRVKKQ MEKSQREYYL NEQIKAIQKE
LGDMDEIPDE NKILKRKIKS LKMPKEAKEK TESELQKLKM MSPMSAEATV VRSYIDWMIQ
VPWNIKTKIK KDIQEAKKIL DIDHFGLEKV KERILEYLAV QSRTNKVKGP ILCLIGPPGV
GKTSLGKSIA KSTGRKYVRM ALGGIRDEAE IRGHRRTYIG SMPGKLMQKM VKAKVKNPLF
LLDEIDKMSC DIRVDPASAL LEVLDPEQNI NFNDHYLEVD YDLSDVMFVA TSNSMNIPAP
LLDRMEIIRL SGYTENEKLN IAKCYLYPKQ MERNALKRNE LIITDCAIIS IIQYYTREAG
VRSLEREISK ICRKVVKLLI LNKSLKKIEI NSKNLKKFLG IKRFDYGKTN NLNQIGQVVG
LAWTEVGGEL LTIETACVSG KGKLTYTGSL GEVMQESIQA ALTVVRSQAK KLGIKKDFHE
KHDIHVHVPE GATPKDGPSA GIAMCTAIVS SLTKNPVKSN IAMTGEITLQ GRVLTIGGLK
EKLLAAHRGG VKTVLIPYEN KRNLEEIPKN IIEGLTIYPV KNIEEVLKIA LENTPYV
