LON_LACP7
ID LON_LACP7 Reviewed; 809 AA.
AC A9KH99;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=Cphy_0379;
OS Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
OS (Clostridium phytofermentans).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=357809;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700394 / DSM 18823 / ISDg;
RA Leschine S.B., Warnick T.A., Blanchard J.L., Schnell D.J., Petit E.L.,
RA LaTouf W.G., Copeland A., Lucas S., Lapidus A., Barry K.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T.,
RA Bruce D., Detter J.C., Han C., Kuske C., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E.A., Richardson P.;
RT "Complete genome sequence of Clostridium phytofermentans ISDg.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000885; ABX40766.1; -; Genomic_DNA.
DR RefSeq; WP_012198409.1; NC_010001.1.
DR AlphaFoldDB; A9KH99; -.
DR SMR; A9KH99; -.
DR STRING; 357809.Cphy_0379; -.
DR MEROPS; S16.001; -.
DR PRIDE; A9KH99; -.
DR EnsemblBacteria; ABX40766; ABX40766; Cphy_0379.
DR KEGG; cpy:Cphy_0379; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_9; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000000370; 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..809
FT /note="Lon protease"
FT /id="PRO_0000396549"
FT DOMAIN 8..201
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 629..809
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 716
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 759
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 809 AA; 90510 MW; 28E162BD3E1421AB CRC64;
MSEYTRQLPV VALRNMAVMP GMLIHFDVNR KVSIEAIEAA MLLNQQVLLV SQIDAETENP
TADDLYRVGT IAEIKQMIKL PGNVIRVLVT GLERATLDSL VSEQPYLKAQ LTSKEAELLN
LTEAEEEAMV RALRDLFEVY TTENNKLNKD IIRQVEASRE IEKMVEQLSI HIPMTLEDKQ
LLLAASDLME QYERLCLILA DEIEVMRIKR ELQNKVKDKV DKNQKDYIMR EQLKVIKEEL
GETSSVSDIM QYLEQLKELV ASDEVKEKIK KEIERFQNVA GSNSESAVAR GYVETLLSLP
WDKVSEDFMD LAYAKEVLET EHYGLKKVKE RVLDFLAVRQ LTEKGDSPII CLVGPPGTGK
TSIARSIAKA LNKEYVRISL GGVRDEAEIR GHRRTYVGAL PGRIITGLKQ AKVKNPLMLL
DEIDKMSSDY KGDTASAMLE VLDSEQNCNF VDHYVEIPVD LSEVMFIATA NTTQTIPKPL
LDRMEIIEVS SYTENEKFHI AKNHLLNKQI EKNGLKKSQI SISEKALRKI ISDYTREAGV
RGLERKISEV CRKIARELLE QESKENQNLI KSAKNKSNNK NQSHSEVAAA VEAEEISVTT
KPSKIKVTEK NITTYLGKPK FRNEIASQKD EVGIVCGLAW TSVGGTTLQI EVNSLPGKGA
LILTGQMGDV MKESAQLGIS YIRSLSKEYK ISEEYFQKND IHIHIPEGAT PKDGPSAGIT
MATAMLSAIT GKKVHAKVAM TGEITLRGRV LPIGGLKEKL LAAKNTGIKK VLIPEKNRPD
LEELEQEITE GMEVICVATM DEVLKHALV
