LON_FRAP2
ID LON_FRAP2 Reviewed; 774 AA.
AC B0TZA7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Fphi_1534;
OS Francisella philomiragia subsp. philomiragia (strain ATCC 25017 / FSC 153 /
OS O#319-036).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=484022;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25017 / FSC 153 / O#319-036;
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., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Richardson P.;
RT "Complete sequence of chromosome of Francisella philomiragia subsp.
RT philomiragia ATCC 25017.";
RL Submitted (DEC-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; CP000937; ABZ87760.1; -; Genomic_DNA.
DR RefSeq; WP_012280861.1; NC_010336.1.
DR AlphaFoldDB; B0TZA7; -.
DR SMR; B0TZA7; -.
DR STRING; 484022.Fphi_1534; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; ABZ87760; ABZ87760; Fphi_1534.
DR KEGG; fph:Fphi_1534; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_6; -.
DR OMA; GAWQVVD; -.
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..774
FT /note="Lon protease"
FT /id="PRO_0000396566"
FT DOMAIN 8..205
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 595..774
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 682
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 725
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 359..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 774 AA; 85998 MW; A2191A2CDD48BA3A CRC64;
MSEVLNVVPV IPLRDVVIYP SMTLPLNVGR KKSIEAVKQA SNSYNNYILL ATQKNGSSSG
DVVDNIYDIG TLAKVVQIMK LPDGSLKIIV EGIAKRLVAK YESIDGCIYA NLDSLHIDDN
YDPSQIDKEL KAILLSITDS LKKFVDISGK VSKESLATLI NTEEPHKFIY EISTILNTEI
AKKQKILEAT DIKNKALLLL SCLYEELEIL ELEAKIKDRV KSQVDKNQRE YYLNEQVKAI
YKELGEADEE SEVTALKSRI EATKMSKEAK EKCLKELKKL KAMPPSSSES AVSRNYIETI
LSLPWGKKAK VKKDINLAEK VLEKDHYGIK KVKERILEHL AVQIKRDTNA KAPILCLVGP
PGVGKTSIGQ SIARATGREY VRMALGGVRD ESEIRGHRRT YIGSMPGQII QKIIKSKTEN
PLFLLDEIDK ISSDFRGDPS AALLEVLDPE QNSTFNDHYL EIDYDLSKVM FVATANSLDI
DPALRDRLEI IHLSGYTEIE KQAIAKQYLV PKALENNGLT KNEINFTPKA TLDIIRYYTR
EAGVRNLQQK IDGVCRKAVK NLLKDPEHGK VSITQNNLED YLGVHQFDYG IKNAKPKVGQ
VTGLAWTSVG GELLTIEALA MPGKGKVKYT GSLGDVMKES IDAAFSVVRS ISKDYKLEDD
FYEKKDIHIH VPEGATPKDG PSAGIAMTTA LVSVYTNKPV RNDIAMTGEV TLRGDVLAIG
GLKEKLLAAL RGGIKEVLIP KQNVKNLADV DKEILEKLEI TPVNSIKEVL ERVF
