LON1_SYNFM
ID LON1_SYNFM Reviewed; 815 AA.
AC A0LEE9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Lon protease 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon1 {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=Sfum_0098;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) 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; CP000478; ABK15801.1; -; Genomic_DNA.
DR RefSeq; WP_011696974.1; NC_008554.1.
DR AlphaFoldDB; A0LEE9; -.
DR SMR; A0LEE9; -.
DR STRING; 335543.Sfum_0098; -.
DR MEROPS; S16.001; -.
DR PRIDE; A0LEE9; -.
DR EnsemblBacteria; ABK15801; ABK15801; Sfum_0098.
DR KEGG; sfu:Sfum_0098; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_7; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000001784; 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..815
FT /note="Lon protease 1"
FT /id="PRO_0000396605"
FT DOMAIN 19..210
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 601..782
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 793..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 688
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 731
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 364..371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 815 AA; 91777 MW; D0C246D66E7A5B60 CRC64;
MFKLTRNKDE QSGSATFAMP LLPLRDIVVF PSMVVPLFVG RDKSVNALDK AMATDKKIFL
AAQTKAKTDT PGESDIYRVG TVANILQILR LPDGTVKVLV EGDFRARISS FIPHPDHFFV
SLEGLEESED ESVEIEALRR GVRAAFDAYS KHNKKINQEI LDAVAAIDNA SRLADTIAAY
MPFKLDVKQK LLETLGVAKR LEKLFGQIRS EIEILQTEER IKGRVKKQME KTQREYYLNE
QMRAIQKEMG EKDDFKSELE ELEKRIKRKK LSQEAAAKVR AEFKKLKLMS PMSAEATVVR
NYIDWILSLP WYEKTRDKLD IDESIRILDE DHYGLEKPKE RIIEYLAVQA LVKRIKGPIL
CFVGPPGVGK TSLAKSIARA MNRNFIRLSL GGVRDEAEIR GHRRTYIGAM PGKIIQSLKK
VKSNNPVFCL DEVDKMSMDF RGDPSAALLE VLDPEQNFSF NDHYLDLDYD LSEVFFITTA
NNLHSIPPPL RDRMEIIQIA GYTEFDKLNI GRNFLVAKQC KANGLSLDNI AFSDDMLLYI
IRHYTKEAGV RNLEREIASI CRKVAKEVVR RGPETRIELT EDLVQEYLGI PKFRYGVAEE
KDEIGLAVGL AWTEFGGDIL GIETVVMPGK GKVQITGKLG DVMQESAQAA LSYVRSRAKR
LGIDPDFYQN FDIHVHVPEG AIPKDGPSAG ITMATSIVSA LARIPVRSDL AMTGEITLRG
RVLPIGGLKE KILAAHRALL KTVLIPKDNA KDLKDIPAKI LEEIQVELVE HMDDVLRKAM
VVPEDRELFH EEEAGAQQAV MFEQKPPAAD EIRAH
