LON_MYCPN
ID LON_MYCPN Reviewed; 795 AA.
AC P78025;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=MPN_332;
GN ORFNames=MP504;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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; U00089; AAB96152.1; -; Genomic_DNA.
DR PIR; S73830; S73830.
DR RefSeq; NP_110020.1; NC_000912.1.
DR RefSeq; WP_010874688.1; NC_000912.1.
DR AlphaFoldDB; P78025; -.
DR SMR; P78025; -.
DR STRING; 272634.MPN_332; -.
DR MEROPS; S16.004; -.
DR EnsemblBacteria; AAB96152; AAB96152; MPN_332.
DR KEGG; mpn:MPN_332; -.
DR PATRIC; fig|272634.6.peg.356; -.
DR HOGENOM; CLU_004109_4_3_14; -.
DR OMA; GAWQVVD; -.
DR BioCyc; MPNE272634:G1GJ3-525-MON; -.
DR Proteomes; UP000000808; 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..795
FT /note="Lon protease"
FT /id="PRO_0000076140"
FT DOMAIN 7..211
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"
SQ SEQUENCE 795 AA; 90204 MW; 7E7855082060C891 CRC64;
MPAVKKPQIL VVRNQVIFPY NGFELDVGRE RSKKLIKALK NLKTKRLVLV TQKNSDQLNP
EFDDIYHCGT LCDIDEIIEV PSEDGKTADY KIKGKGLQRV AITSFSDADL TKYDHHFLNS
TLTENKALDK LLERIFPDKE DFAEILDSLN SFLELQELKK LSKVPKDIKR YDIITFKLAS
LIFKDITLQQ AILEENDIEK RLQKIIGSGI EDLGHISEEA RAKQRESEFD KIDNRITRKV
NEQLSRQQRD FYLREKLRVI REEIGMTSKK EDEVSNIRKK LEENPYPEHI KKRILSELDH
FENSSSSSQE STLTKTYIDT LMNLPWWQES KDNADVKNLI KILNKNHSGL DKVKERVVEY
LAVQLRTKKL KGPIMCLVGP PGVGKSSLAK SIAEALNKCF VKVSLGGVHD ESEIRGHRKT
YLGSMPGRIL KGMVRAKVIN PLFLLDEIDK MTSSNQGYPS GALLEVLDPE LNNKFSDNYV
EEDYDLSKVM FVATANYIED IPEALLDRME VIELTSYTEQ EKLQITKSHL VKRCLDDAEI
KTDDLKFTDE GISYIIKFYT REAGVRQLER LIQQIVRKYI VNLQKTGEQQ VVVDVDLVKK
YLKKEIFDYT VRDEDALPGI VNGMAYTPTG GDLLPIEVTH VAGKGDLILT GNLKQTMRES
ASVALGYVKA NAQSFNINPN LFKKVDINIH VPGGGIPKDG PSAGAALVTA IISSLTGKKV
DPKIAMTGEI TLRGKVMTIG GVKEKTISAY RGGVRTIFMP EKNERYLDEV PKDIVKDLEI
ILVKEYKDIY NKIFN
