LON_METSB
ID LON_METSB Reviewed; 810 AA.
AC B8EMF2;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Msil_3172;
OS Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS 13906 / BL2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Methylocella.
OX NCBI_TaxID=395965;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2;
RX PubMed=20472789; DOI=10.1128/jb.00506-10;
RA Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT "Complete genome sequence of the aerobic facultative methanotroph
RT Methylocella silvestris BL2.";
RL J. Bacteriol. 192:3840-3841(2010).
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; CP001280; ACK52080.1; -; Genomic_DNA.
DR RefSeq; WP_012592149.1; NC_011666.1.
DR AlphaFoldDB; B8EMF2; -.
DR SMR; B8EMF2; -.
DR STRING; 395965.Msil_3172; -.
DR PRIDE; B8EMF2; -.
DR EnsemblBacteria; ACK52080; ACK52080; Msil_3172.
DR KEGG; msl:Msil_3172; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_5; -.
DR OMA; MVNIEDK; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000002257; 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..810
FT /note="Lon protease"
FT /id="PRO_5000424817"
FT DOMAIN 40..231
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 621..802
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 708
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 751
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 385..392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 810 AA; 88383 MW; 9DDB4073A153716F CRC64;
MESFAPTRKG RAVFSADAAA TAAPGSAGAG ETLDPAKDAL IIVPVRGFVL FPGIVMPVVL
NGPAAIAAAQ EAVRQQRSVG ILMQRESGAE EASPLNMHRF GVVANILRYI TAQDGGHHLI
CQGEQRFHVE EFLRERPYLA ARVKRIEEPD ERSPDIEARF VHLQGQASEA LQLLPQTPPE
LIAAVNSAPS PGALTDLVAA YMDASPAQKQ DILETIDLRA RMDMVAKLLA QRIEVLRLSQ
EIGRQTKASL DERQREMLLR EQMASIQRQL GEGDGKAQEI AELTEAIAKA KMPAEVEEAA
RKELRRLERM PDASAEYGMI RTYIDWLIEL PWSLPEEAPI DIAEARRILD ADHFGLDKIK
QRIVEYLAVR KLAPQGKAPI LCFVGPPGVG KTSLGQSIAR AMGRKFVRVS LGGVHDEAEI
RGHRRTYVGA LPGNIIQAIR KAGARNCVMM LDEIDKMGAS AHGDPGSAML EVLDPEQNST
FRDNYLAVPF DLSRVVFIAT ANMLDTVPGP LRDRMEIIAL TGYTDREKLE IARRYLVRRQ
LEANGLKPDQ VEIDDDALIE IIRGYTREAG VRNLEREIGR VLRHVAVRIA DGSASHVHVS
RAELTELLGQ QRFEDEVAMR LSVPGVATGL AWTPVGGDIL FIEATRAPGH GKLTLTGQLG
EVMRESVQAA LSLIKSRAAE LGVDPESFDK TDIHVHVPAG ATPKDGPSAG VAMFIALVSI
LTGRLVRNDT AMTGEISLRG LVLPVGGIKE KVVAAARAGL TRVLLPARNR RDYDEIPQDT
REKLEFVWLE KVDDAMAAAF EGMAATPAPN
