LON_MALP2
ID LON_MALP2 Reviewed; 781 AA.
AC Q8EV77;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=MYPE6910;
OS Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX NCBI_TaxID=272633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF-2;
RX PubMed=12466555; DOI=10.1093/nar/gkf667;
RA Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT bacterial pathogen in humans.";
RL Nucleic Acids Res. 30:5293-5300(2002).
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; BA000026; BAC44483.1; -; Genomic_DNA.
DR RefSeq; WP_011077513.1; NC_004432.1.
DR AlphaFoldDB; Q8EV77; -.
DR SMR; Q8EV77; -.
DR STRING; 272633.26454153; -.
DR MEROPS; S16.004; -.
DR EnsemblBacteria; BAC44483; BAC44483; BAC44483.
DR KEGG; mpe:MYPE6910; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_14; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000002522; 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..781
FT /note="Lon protease"
FT /id="PRO_0000396584"
FT DOMAIN 16..212
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 601..781
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 688
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 731
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 365..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 781 AA; 88389 MW; E126A8DA49498B41 CRC64;
MNNKKNEKTT NNKEIANVLV TRGIVFYPNT KIRIEIGREK SIAAINDSKE KKQNMIVVSQ
ENPSIDSPSK NEIFTVGTLC SFEIDNKHPD GSYSIIFTGI KRVKINKLSE KASDGEIKTK
FFYADYSEIE EDTKLSKSNE EAIKDLHAKF ENELNNLTFF PKKDLALSKE NRHTIVDWLP
IALKFSLEEK QQLLEEPSLS KRIEKILSFT IDERVSQKID SEISKKINTN LSKQQKEFYL
RERVRAIKEE LGDISSKEDD AESIRDRVRN NPYPEHIKKR ILSEVNKLES SSNSNEYSMS
KTYIDWLIDL PYWQKTDDVD SLADVENVLN NNHYGLEKVK ERIIEYLAVR MKSKSAKGSI
ICLVGPPGVG KTSLAQSIAE ALKKKFVKVS LGGMRDEAEL KGHRKTYIGA MPGRIIKAMS
KAGVVNPVFL LDEIDKLGSD HKGDPASAML DILDPEQNNR FSDNYIEEDY DLSNVLFIAT
ANYEENIPEP LHDRLEIIRL SSYTENEKLS IAKNYLVKKI LVESALKKDE LKFTDDGLSY
IIKRYTREAG VREVERAIRQ IARKFVVRQQ KEKLTSQTIG VEEVKYYLKK EIYDYTKKDK
EYMPGVVNGM AYTTAGGDLL PIEATFAPGK GKIEITGNLK ETMKESVNVA LGYVKTNAVK
FGIDPKIFGE IDLHVHVPSG GIPKDGPSAG IALTTAILSA LKNVKIPSNV AMTGEITLRG
RVLIIGGVKE KTISAYRGGA NDIFMPKEDE RYLDDVPEEV RSKIKITLVD TYDDVYNRLF
K
