LON_FRAAA
ID LON_FRAAA Reviewed; 874 AA.
AC Q0RPW3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=FRAAL1764;
OS Frankia alni (strain ACN14a).
OC Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=326424;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACN14a;
RX PubMed=17151343; DOI=10.1101/gr.5798407;
RA Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA Benson D.R.;
RT "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT reflect host range and host plant biogeography.";
RL Genome Res. 17:7-15(2007).
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; CT573213; CAJ60416.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0RPW3; -.
DR SMR; Q0RPW3; -.
DR STRING; 326424.FRAAL1764; -.
DR KEGG; fal:FRAAL1764; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_11; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000000657; 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..874
FT /note="Lon protease"
FT /id="PRO_0000396567"
FT DOMAIN 18..259
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 667..851
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 47..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 757
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 800
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 430..437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 874 AA; 91415 MW; A1800E1F177722EB CRC64;
MTQLPHVRVD HMPQIRVLPV LPLDDAVVLP GMVVSLDMSD EQTRAAVDAA RTGGSAGSSD
ARAPGISSRA AGRPAEVLLV PRVGGELAEV ATVGVIEQVG RLPRGGSAAV VRGTARAQVG
GVRPAPAGTD TTGTGTADAT SGAGSGAGVQ WVDAVVLDDS AATPFGALDD PAGTRAGSPA
DEAARVDKLA KEYRALVTDL LRQRGAWQVV DSVSAITDPG TLADTAGYSS YLTTAQKIEL
LGTPAVGTRL ERLLTWTKEH LAEQDVAETI RRDVQEGMDR QQREFLLRRQ LEAVRKELSE
LDGSGGGADG ASGSEPADYR ARVEAADLPE KVRAAALKEV DKLERTSDSS PEGGWIRTWL
DTVLDLPWNV RAEDSYDIIA ARAVLDADHA GLDDVKDRII EHLAVRRRRA DAGLGVVGGR
RGGAVLALAG PPGVGKTSLG ESIARAMGRS FVRVALGGVR DEAEIRGHRR TYVGALPGRI
VRAIREAGSM NPVVLLDEVD KLGADYRGDP TAALLEVLDP EQNHTFRDHY LEVELDLSDV
LFLATANVLE AIPAPLLDRM ELIRLDGYTE DEKVVIARDH LLHRQLDRAG LAEGDVSVGD
DALHALAGEY TREAGVRDLE RSIARLLRKV VAQVALGAAA LPVTIDAGDL TGYLGRPRHT
PESAERTALP GVATGLAVTG AGGDVLFVEA SLADAETGGG GITLTGQLGD VMKESAQIAL
SYLRSHGVEL ELPVGDLADR GVHVHVPAGA VPKDGPSAGV TMTTALASLL SGRPVRADVA
MTGEVSLTGR VLPIGGVKQK LLAAHRAGLT TVLLPQRNGP DLDDVPAPVR DALTVHLVTD
VREVLDLALE PAFDADHGGR SPGRAGHSPT ALAA
