LON_PARPJ
ID LON_PARPJ Reviewed; 804 AA.
AC B2TFQ5;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Bphyt_5717;
OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS (Burkholderia phytofirmans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=398527;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX PubMed=21551308; DOI=10.1128/jb.05055-11;
RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT "Complete genome sequence of the plant growth-promoting endophyte
RT Burkholderia phytofirmans strain PsJN.";
RL J. Bacteriol. 193:3383-3384(2011).
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; CP001053; ACD20063.1; -; Genomic_DNA.
DR RefSeq; WP_012427571.1; NC_010676.1.
DR AlphaFoldDB; B2TFQ5; -.
DR SMR; B2TFQ5; -.
DR STRING; 398527.Bphyt_5717; -.
DR EnsemblBacteria; ACD20063; ACD20063; Bphyt_5717.
DR KEGG; bpy:Bphyt_5717; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_4; -.
DR OMA; MVNIEDK; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000001739; Chromosome 2.
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..804
FT /note="Lon protease"
FT /id="PRO_0000396540"
FT DOMAIN 30..222
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 612..793
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 699
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 742
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 376..383
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 804 AA; 87789 MW; 9515256CC906AF1D CRC64;
MSADSENETS ESSPAGEATA STSALPDEPL ILLPVRNAVL FPGMVLPFTA GRGQVKEDVQ
AAVKRQQPLG VVLQRDPRVQ DPTFDDLNTI GTVANVVRYV TSPEDGAHHL ICQGVERFRL
IAPVEGLGFR AARVEFLPET TARNPAVDAR ALVLRQRAGE MIGLLPNAGG ELVRALDAIE
LPGLLADTIA GLLDIPPERK QEILETLDVC KRLDKVLDAV AGRIEVLRLS QEIGEQTRGR
IDQRQREMML REQLRTIQNE LGENIESREE VRKLTEAIEA AHMPPEVESH ARKELGRLER
MPEASSEYSI SVSYLEWLTE LPWPLPAEAP IDIARARQIL DEAHFGLDKV KRRILEYLGV
RKLNPHGKAP ILCFLGPPGV GKTSLGQSIA RALERPFVRV SLGGVHDEAE IRGHRRTYIG
AMPGNIIQAI RKAGARNCVM LLDELDKLGQ GVHGDPAAAM LEVLDPEQNA SFRDNYLGVP
FDLSAIVFVA TANQIEGIAG PLRDRMEILD LPGYTEAEKF QIAQRFLVPR QLEACGLTAA
QCELPDETLR AIIRDYTREA GVRSLERQIG AVFRYVALRV AEDPSTHERI EPDRLSSILG
HRRFESEVAM RTSLPGVVTG LAWTPVGGDL LFIEASSTPG GGRLVLTGQL GDVMKESVQA
ALTLVKSRCE SLHIDCSNFD KRDIHVHVPA GAVPKDGPSA GVAMFIAIAS LLMGRAVRSD
CAVTGEISLR GIVLPVGGIK EKVLAALRGG IKTVLLPARN APDLEDIPVD ARNQMRFVLL
ETVDDAVREI IEDESVTSSR NVDI
