LON_MESH2
ID LON_MESH2 Reviewed; 870 AA.
AC Q600B5;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
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=mhp541;
OS Mesomycoplasma hyopneumoniae (strain 232) (Mycoplasma hyopneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=295358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=232;
RX PubMed=15489423; DOI=10.1128/jb.186.21.7123-7133.2004;
RA Minion F.C., Lefkowitz E.J., Madsen M.L., Cleary B.J., Swartzell S.M.,
RA Mahairas G.G.;
RT "The genome sequence of Mycoplasma hyopneumoniae strain 232, the agent of
RT swine mycoplasmosis.";
RL J. Bacteriol. 186:7123-7133(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; AE017332; AAV27942.1; -; Genomic_DNA.
DR RefSeq; WP_011206374.1; NC_006360.1.
DR AlphaFoldDB; Q600B5; -.
DR SMR; Q600B5; -.
DR STRING; 295358.mhp541; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; AAV27942; AAV27942; mhp541.
DR KEGG; mhy:mhp541; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_5_1_14; -.
DR OMA; KKMNPVM; -.
DR PhylomeDB; Q600B5; -.
DR Proteomes; UP000006822; 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; 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; IPR027417; P-loop_NTPase.
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 SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Serine protease; Stress response.
FT CHAIN 1..870
FT /note="Lon protease"
FT /id="PRO_0000396581"
FT DOMAIN 7..268
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 691..870
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 777
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 820
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 454..461
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 870 AA; 98728 MW; 85189528090E312F CRC64;
MPTNSYRFLV ASEDIYFQNT LQQSITFSDP ESIKVLKDFY HSNSRPTLTN KDFLIVYRKE
KEKDTKKKNS SVIKFPRNDF NSFEDSKNDI QNQAKILNGK VGDFENSLLP RIYDLDELSK
YASLARIQSY RAKTSPDKSE WQTVILDFIV TEKVQLVELI NDPQNPKVGQ IIIKPVRETI
KSPEIHINLI NDLLEMARKA KNFRIPTELL LIVDKFGANS EYSTNEYIKG VTNTLSCSPS
LTYPQKYQLF SYNSYPAKIK KLYEHIHTFA EQIKLEDEIN VILKTNLDKQ QTEFILKEKI
KAIRKKLGED SRYEDEIEEL LHSELGKKVF PKEVAKTIMR ETNKLKSMIV TSPESNITKS
YLDLLVALPW KKVKKDILDI KNVREKLEEA HYGLDEIKKR IIEYLAALIH RRSQSEGKPE
LEKVGSDYID SNLFLSHKIR KVRSNSIPIL TLVGPPGTGK TSIAMAVAEA IGKEFVKISL
GGIRDEAEIR GHRRTYVGAL PGKIIQALKK VGVSNPLILL DEIDKMGADF KGDPSAAMLE
VLDPEQNRFF QDHYLELEYD LSQVLFVATA NEIYDIPEPL LDRVEIIELS SYTFIEKIQI
AKSHLIPAVL KENALDPKYF PIQDQTIDFL IRHYTREAGV RGLKRVIDKI VRKIIVKLLE
KTLDQNFVID IEFVRELLGI EKYDPDNVDS SPQIGTVTGL GYSPLGGSTL QIEVSTIPGR
GDIKLTGSLK DVMQESARIA LSYVQSKAKD FGINFDFENT LIHIHVPEGA IPKDGPSAGI
TFATAIISAL SQKPVSHNIA MTGEITLRGK VLAIGGLKEK TMGAYKNGIK IIFIPKANEK
NLVDIPQEVK DVIQFIPVDT YQQIYDFIFK
