LON1_BDEBA
ID LON1_BDEBA Reviewed; 793 AA.
AC Q6ML73;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=Bd2144;
OS Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 /
OS HD100).
OC Bacteria; Proteobacteria; Oligoflexia; Bdellovibrionales;
OC Bdellovibrionaceae; Bdellovibrio.
OX NCBI_TaxID=264462;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100;
RX PubMed=14752164; DOI=10.1126/science.1093027;
RA Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C.,
RA Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E.,
RA Schuster S.C.;
RT "A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a
RT genomic perspective.";
RL Science 303:689-692(2004).
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; BX842651; CAE79984.1; -; Genomic_DNA.
DR RefSeq; WP_011164586.1; NC_005363.1.
DR AlphaFoldDB; Q6ML73; -.
DR SMR; Q6ML73; -.
DR STRING; 264462.Bd2144; -.
DR EnsemblBacteria; CAE79984; CAE79984; Bd2144.
DR KEGG; bba:Bd2144; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_7; -.
DR OMA; EWAVSRN; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000008080; 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..793
FT /note="Lon protease 1"
FT /id="PRO_0000396538"
FT DOMAIN 8..200
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 590..770
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 676
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 719
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 793 AA; 88636 MW; A90E589F4502CC54 CRC64;
MSYVSGYVPV IPLKNSVLFP DISMPLRIGR EKSIAALQKA LRDNHWVILL TQKNPNASVD
KIEDLYQVGT LAKVESFRME EDGSYNIFVK AHQRVRLIHS RDSEGHIEAQ TEALEDSGRL
DKKTEEALLS SLRQLSDDLL DLLPGNTRQI REMIAEIEDL QTLVNMCAAY ADINISDKQE
ILEIPLLKDR ALKLLDRLQE LKERLKIQRG IRDKLQESFQ QNQKESILRE QMRVIREELG
DHEGEDLFAK FKDKIDKAGM PPEALELAKN QLRRLETSNS ASPEYQMIRT HLELMTSLPW
NQSSAQQDID LEAAERVLNE DHYGLEKIKK RILQHLAVMK LRKSQQGSIL MFIGPPGVGK
TSLGKSIARA LGKKYVRVAL GGVRDDAEIR GHRRTYIGAL PGRIIAGIKK AGENDPVFIL
DEIDKLTRGF GGDPASAMLE VLDPEQNNTF QDHYLDTPFD LSKVFFIATA NSLEGIPLPL
LDRMEVIDLS GYTVDEKRQI ARSHLWPKQL KEHGLEENQL QITDQALTKL LTHYTREAGV
RDLQRKIASI CKHMSLKIIK SEGLPLLVEE QDLEDIFGAE RFSADMIGSL LPPGVVTGLA
WTPVGGDILF IESAQMPGKG NLLLTGQLGE VMQESAKIAL TLLKSRLPLL DPLLDFAKKD
IHVHVPAGAI PKDGPSAGIT MLTSMASMLL NKPVDPKVAM TGEISLRGSV MPVGGIKEKV
IAAHRAGVQE ILLCKRNEKD LREIPEDIRK DLRFHFVEDV NEVLKITLGV NVPKWDQVQL
PPPSPLSSTD AGT
