LON_RICCN
ID LON_RICCN Reviewed; 778 AA.
AC Q92HZ1;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
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=RC0629;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL03167.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE006914; AAL03167.1; ALT_INIT; Genomic_DNA.
DR PIR; E97778; E97778.
DR RefSeq; WP_016830768.1; NC_003103.1.
DR AlphaFoldDB; Q92HZ1; -.
DR SMR; Q92HZ1; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; AAL03167; AAL03167; RC0629.
DR KEGG; rco:RC0629; -.
DR PATRIC; fig|272944.4.peg.715; -.
DR HOGENOM; CLU_004109_4_3_5; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000000816; 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..778
FT /note="Lon protease"
FT /id="PRO_0000280892"
FT DOMAIN 6..205
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 592..773
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 679
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 722
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 778 AA; 87000 MW; 2039A138A9C8F956 CRC64;
MHKKSLPLMA LRDMVVFPGV IAPIFVGRPK SLQALSHTTI SEEDNSKYIL VTLQKKFDQE
NPSTHELYNT AILAKIIQIV KLPNNTAKIL IEAVARVKLS NIKGEEAFEA NYEIIPDEEI
FDVNNMRSLV DNAVQLFSKY AINDKKVNAE IIETINKEIS NSTNFIDIIN ILASHLITSL
EAKQHLLEET SPFKRITTVI SMLNSNIVNS ETEQALQKRV RKQIEKTQRD YYLHEQMKAI
QKELDEDKSE LADIENKIKS LKLSKEAKEK AEAELKKLRT MNQMSAESGV TRNYLETLLS
LPWGKYDNSK IDINQAEKIL NRDHFGLEKV KERIIEYLAV LQRSSKIRGP ILCLIGPPGV
GKTSLVKSIA EGMGRKYTKL ALGGVRDEAE IRGHRKTYLG SMPGKILGQL KKVKTSNPVM
LLDEIDKMSS DFRGDPASAL LEVLDPEQNS HFVDHYLEVE YDLSNVIFIA TANSHDLPRA
LSDRMEKIYI SGYVEETKLQ IARNYLVPKQ FKMHKIKKDE ITISETAILD LIRYYTKESG
VRALEREIGA LTRKALKQIL ADKSVKHIAI DSNHLEEFLG AKKYNFGLAE KEDQIGSTTG
LAYTEVGGEL LTIEALAFPG KGEIKTTGKL GDVMKESAMA AYSCFRSRAT NFGLKYDNYK
DFDIHIHVPA GAIPKDGPSA GCALFTTIVS LMTKIPVHRT VAMTGEITLR GNVLPIGGLK
EKLLAASRGG IKTVLIPEEN VKDLKDIPPN IKESLEIISV SNIDQVLKHA LVGTPINK
