LON_UREP2
ID LON_UREP2 Reviewed; 791 AA.
AC B1AIY7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=UPA3_0364;
OS Ureaplasma parvum serovar 3 (strain ATCC 27815 / 27 / NCTC 11736).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Ureaplasma.
OX NCBI_TaxID=505682;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27815 / 27 / NCTC 11736;
RA Methe B.A., Glass J., Waites K., Shrivastava S.;
RT "Genome sequence of Ureaplasma parvum serovar 3.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000942; ACA33243.1; -; Genomic_DNA.
DR RefSeq; WP_010891739.1; NC_010503.1.
DR AlphaFoldDB; B1AIY7; -.
DR SMR; B1AIY7; -.
DR MEROPS; S16.004; -.
DR EnsemblBacteria; ACA33243; ACA33243; UPA3_0364.
DR GeneID; 29672351; -.
DR KEGG; upa:UPA3_0364; -.
DR HOGENOM; CLU_004109_4_3_14; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000002162; 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 Serine protease; Stress response.
FT CHAIN 1..791
FT /note="Lon protease"
FT /id="PRO_0000396615"
FT DOMAIN 3..198
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 605..790
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 696
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 739
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 791 AA; 89527 MW; 1980DA438D593E00 CRC64;
MKKPILISRA IVVLPYETTT IEVGRPKSIQ AIDLAKQSSS KEIIIISQKD IDTDEVVNFD
ELYKVGTLVK IKSIIDNFDE GYSIEVEGLK AVYINNENDV IDAIEYEYED VITNPILSNK
DEIAINGINS EIFNIINKRS RHKNINFDNM HALISLEKEK FAYLAAATYI NDYDNEISEK
TIEDRINILL QPNLLLVHET ILHLLFDQLV DKRVIEDEVE KTITDKINNN FQKQQREFYL
REKLKVVKEQ LGELSSREED ADKIRAKIED LELPPNVKER ALAELNRFEN AMSSNESSVI
KSYLDWLLDL PWTQQGVDNT DLMSVRTHLD DNHYGIEKVK ERILEYLALR MRNPNLKGPI
ICLVGPPGVG KTSLVTSIAQ ALNKKFVKVS LGGVRDESEI RGHRKTYVGA MPGRIIKGMK
KAGVINPLFL LDEIDKMTSD QRGDPAAAML EVLDPEQNKN FSDNYIEEEY DLSKVMFMAT
ANYYQQIPYA LIDRLEVIEL SSYTAIEKRE IAKSHLLKRI FMDAKLNENE LIFTDDALDF
IINHYTKEAG VRELDRQLGH IVRKYIVETY KNKNNQSPLN LKVDEAMIIK YLGKIKFDFN
KKEETTIPGI VNGMAYTAAG GDLLPIEVNH STNGKGGNVT ITGNLEKTMN ESVSVALGFV
KANADKYGID TKKVSFKEID IHVHVPSGGI PKDGPSAGIA ITTAIISSLS QRPVRTTLSM
TGEIMLRGNV GIIGGVKEKV ISAYRAGVRE IILPIDDERY LEDVPKYILD DIKIHLVKHY
DEVYNIVFGE K
