LON_MYCMS
ID LON_MYCMS Reviewed; 796 AA.
AC Q6MTF4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=MSC_0454;
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1;
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(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; BX293980; CAE77082.1; -; Genomic_DNA.
DR RefSeq; NP_975440.1; NC_005364.2.
DR AlphaFoldDB; Q6MTF4; -.
DR SMR; Q6MTF4; -.
DR STRING; 272632.MSC_0454; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; CAE77082; CAE77082; MSC_0454.
DR KEGG; mmy:MSC_0454; -.
DR PATRIC; fig|272632.4.peg.494; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_14; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000001016; 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..796
FT /note="Lon protease"
FT /id="PRO_0000396583"
FT DOMAIN 19..211
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 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 796 AA; 90443 MW; 05FDC1B9965980A9 CRC64;
MLQYLKKIKG VSFMKTIKLP VVVTRGIFIL PSTSKTIEFG RVKSKNALDA SADLYNNQIV
VVSQESPLEE EPNLEHLFYL GTVADLSVKK VWKDGTISVE LNYNQKIKID EFVEEDNIIY
AIGSVFEDKL PKTDAQKTKI KEALEELQEK HSFNTSELLL VFNENDFNKL NSLIYQIIDK
MPLVSLNTKL LLIQSTSILE KLELLKELII NRPKSTIKLN NNLNNNSTVD SEINKKLKDK
MDKQQKEYYL REKMRIIKEE LDDENSDASQ LDKYKKRLEE EPFPESVKEK ILSSIKRIET
MQPGSAEVNV ERNYVDWMMS IPWWEQSEDI DDLKYAQEIL EKHHFGLKKV KERIIEYLAV
KQKTKSLKGP IITFVGPPGV GKTSLARSIA EALGKKFVKV SLGGVKDESE IRGHRKTYVG
SMPGRIIQAL KRAKVKNPLF LLDEIDKMAS DNRGDPASAM LEVLDPEQNK EFSDHYIEEP
YDLSTVMFIA TANYIENIPE ALYDRMEIIN LSSYTEIEKM HIAKDYLTKK ILEEDQLTED
ELRFTDEAYD EIIKYYTREA GVRQLERHLA TIARKFIVKL LNGEITNLVV TREVVVQYLG
KHIFEHTSKE EESQVGVVTG LAYTQFGGDI LPIEVSTYNG KGNLTLTGKL GEVMKESATI
ALTYVKANHE KFGISKDKFD DIDIHIHVPE GAVPKDGPSA GITLTTALIS ALSKQPVSKD
FGMTGEITLR GNVLPIGGLR EKSISAARSG LKHILIPSKN VKDIEDVPQE VQDVLKITPV
SKYEDVYEII FKNNNQ
