LON_CLOAB
ID LON_CLOAB Reviewed; 778 AA.
AC Q97FT9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=CA_C2637;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80584.1; -; Genomic_DNA.
DR PIR; E97224; E97224.
DR RefSeq; NP_349244.1; NC_003030.1.
DR RefSeq; WP_010965925.1; NC_003030.1.
DR AlphaFoldDB; Q97FT9; -.
DR SMR; Q97FT9; -.
DR STRING; 272562.CA_C2637; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; AAK80584; AAK80584; CA_C2637.
DR GeneID; 44999105; -.
DR KEGG; cac:CA_C2637; -.
DR PATRIC; fig|272562.8.peg.2826; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_9; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000000814; 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..778
FT /note="Lon protease"
FT /id="PRO_0000396546"
FT DOMAIN 8..200
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 591..772
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 678
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 721
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 354..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 778 AA; 87599 MW; 5C5052C37B661BB9 CRC64;
MNQENKVLPL IPLRGLIVFP YMVVHFDVGR DKSIEALEKA MMNDQQIFLS TQKDAKIEEP
NEDDINSVGT ICSIKQILRL PGDAVRVLVE GISRGKIDKY LKQEPFIEAE ITEFKDEDNY
EEYEIKALMR IITKEFGKYV KLSGAVTKDA VDFLKDIKEP GKFADIVSSY LIIKQEQKQS
VLNSIDEKER LENVLTVIKD ELQILELERN IGVKVKEKID KSQREYYLRE QIKVMQDQLG
DDDEEKAEIK EYTQKIKKGK LTKEAKEKAL HELKKLENAG AYSPEGAGIK TYLDWILSLP
WKDKTKDNLD IKRAREILNK EHYGLSDVKD RIIEYLAVKK MSKSLKGPIL CLVGPPGVGK
TSIAKSIANA VNRNFVRISL GGVNDEAEIR GHRRTYVGAI PGRIIYGMKQ AKSNNPLMLL
DEIDKMSSSY KGESADALLE VLDTSENNKF RDNYLELDFD LSDVMFVTTA NTLETIPRPL
MDRMEIIEVS GYTYEEKFHI AKEHLIPKQL EEHNMPEDKK ITFMDSSIYY IIENYTRESG
VRSLERKIAA IIRKIITEIV EKDKSSISVN SRTVKKYLGE DVFSADKIDK EDKIGVVTGM
AWTAYGGDTL PVEAVIMPGN GKLQLTGQLG DVMKESAQAG YSYVRANSVK YGIDKEFYKN
KDIHVHVPEG AVPKDGPSAG VTMITAMVSA LSDKKVKHNV AMTGEITLTG RVLAIGGLKE
KTLAAYRAGV DTIIIPKQNE KDINKVPKAI RGKIKFILAE EVDTVLENAL IGGINNDN
