ID LON_MYCGE Reviewed; 795 AA.
AC P47481; Q49276;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 27-MAR-2024, entry version 146.
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=MG239;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Mycoplasmoides.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 484-606.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
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.
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; L43967; AAC71460.1; -; Genomic_DNA.
DR EMBL; U02148; AAD12428.1; -; Genomic_DNA.
DR PIR; D64226; D64226.
DR RefSeq; WP_009885776.1; NZ_AAGX01000005.1.
DR AlphaFoldDB; P47481; -.
DR SMR; P47481; -.
DR STRING; 243273.MG_239; -.
DR MEROPS; S16.004; -.
DR KEGG; mge:MG_239; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_14; -.
DR InParanoid; P47481; -.
DR OrthoDB; 9803599at2; -.
DR BioCyc; MGEN243273:G1GJ2-286-MONOMER; -.
DR Proteomes; UP000000807; 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 CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF56; LON PROTEASE; 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 PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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..795
FT /note="Lon protease"
FT /id="PRO_0000076139"
FT DOMAIN 7..213
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 615..795
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 702
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 745
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 379..386
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT CONFLICT 494
FT /note="T -> S (in Ref. 2; AAD12428)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 795 AA; 89988 MW; 31C8188EA40F5E39 CRC64;
MPVTKKSQIL VVRGQVIFPF VPFSLDVGRP RSRKIIKALK TLKTKRLVLV TQKFTGEQNP
EFNDIYHVGT LCEIDEIVDV PGVDSKTVDY RIKGRGLQRV LIEKFSDADI NEVSYQLLNS
TVKDEANVDR FLQRIFPEKE EIEQLMEGAE KFLELENISK TVNVPKGLKQ LDIITFKLAN
LVPNTESIKQ AILEENEIAN RLEKIIQAGI EDLQKIQDYG RSKNKETEFD KLDSKITRKI
NEQLSRQQRD FYLREKLRII REEIGISSKK EDEVASIRKK LDENPYPEAI KKRILSELEH
YENSSSSSQE STLTKTYIDT LLNLPWWQKS KDNSDVKNLI KTLDKNHTGL DKVKERIVEY
LAVQLRTQKN KGPIMCLVGP PGVGKSSLAK SIAEALDKKF VKISLGGVHD ESEIRGHRKT
YLGSMPGRIL KGMTRAKVIN PLFLLDEIDK MTSSNQGYPS GALLEVLDPE LNNKFSDNYV
EEDYDLSKVM FIATANYIED IPEALLDRME IIELTSYTEQ EKIEIAKNHL IKRCLEDADL
NSEELKFTDE AISYIIKFYT REAGVRQLER LIQQVVRKYI VAMQKDGIKQ ETIDVNAVKK
YLKKEIFDHT MRDEVSLPGI VNGMAYTPTG GDLLPIEVTH VAGKGELILT GNLKQTMRES
ANVALGYVKA NAERFNINPS LFKKIDINIH VPGGGIPKDG PSAGAALVTA IISSLTGKKV
DPTVAMTGEI TLRGKVLVIG GVKEKTISAY RGGVTTIFMP EKNERYLDEV PKEIVDKLNI
IFVKEYSDIY NKLFS
//
