LON_META1
ID LON_META1 Reviewed; 835 AA.
AC B3PN08;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=MARTH_orf627;
OS Metamycoplasma arthritidis (strain 158L3-1) (Mycoplasma arthritidis).
OC Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC Metamycoplasma.
OX NCBI_TaxID=243272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=158L3-1;
RX PubMed=18573899; DOI=10.1128/iai.00516-08;
RA Dybvig K., Zuhua C., Lao P., Jordan D.S., French C.T., Tu A.H.,
RA Loraine A.E.;
RT "Genome of Mycoplasma arthritidis.";
RL Infect. Immun. 76:4000-4008(2008).
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; CP001047; ACF07410.1; -; Genomic_DNA.
DR RefSeq; WP_012498367.1; NC_011025.1.
DR AlphaFoldDB; B3PN08; -.
DR SMR; B3PN08; -.
DR STRING; 243272.MARTH_orf627; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; ACF07410; ACF07410; MARTH_orf627.
DR KEGG; mat:MARTH_orf627; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_14; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000008812; 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; 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 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.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Reference proteome; Serine protease; Stress response.
FT CHAIN 1..835
FT /note="Lon protease"
FT /id="PRO_0000396580"
FT DOMAIN 4..222
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 649..832
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 738
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 781
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 412..419
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 835 AA; 94242 MW; 6BC089430C3E02DA CRC64;
MKKLPYIAIR NQLIAPYSTA TVKIGRPNSL AAIQFAQTGF NGEIYIFYTK DNKMVDSIKK
TSDLEEYGVK AKIKEIVEQG KLQNVVFEVE ELVKVKEIYK ELGKYSFTSD IFASVTEVEY
SGNFDILSDY RSKAKMLIEK LSNLHDEIGS YIYGGRRGIK ELEKAFSANT NISPLTHDSF
NVDIWKIIDA LTIEHSWKEY FAIINETNLE KNYELAINML INAIKMGKLD EEVNSTMRGD
LENQQRDFLL RERLRQIKKL LKDDEAGAKA IENMEDAEEN ARQYPDYVIE ALKTEQNRLA
SMMPASPEAN ISKTYIDLIT TLPWKKVSGE LLDIDNVRKI LDKHHYGLEK PKERILEFIS
VLTYTKKENE KNEYVPVKGE ENRFIDKNLF VNKTGNFLKD RVNNIPILTL IGPPGTGKTT
LAKSIAEALG RQFVKISLGG VKDESEIRGH RRTYVGALPG KIISGIKKAG VSNPVILLDE
IDKMSSDFRG DPLSALLEVL DPEQNTNFQD HYLDLEYDLS KVLFIATANS FDSIPAPLYD
RVEFLELSTY TLIEKTRIAR THLLSKILSL NALTEKQYQI TDEVLAYIIK NYTRESGVRN
LQRLLDSIAR KIVVRILDKK VDKEFVIDKA IVREFLGPEL YNEKGDETQP KAGVVNALAY
TAYGGTSMTI EVTTFPTTAK GALNLTGQLK DVMRESATIS LAYVRSNAEK FGIKDFDFEN
TSIHIHVPEG AIQKDGPSAG VTFTTAIISA LSKKAVPNTI AMTGEITLRG KVLPIGGLKE
KSLAASQIGI KTIFIPKDNE KNLIDVPEEV KKDIKFVPVE YYDEIFKYIF EAKNK
