LON_CAUVN
ID LON_CAUVN Reviewed; 799 AA.
AC B8GX12; P52977;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=CCNA_02037;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=NA1000 / CB15N;
RX PubMed=8666236; DOI=10.1101/gad.10.12.1532;
RA Wright R.J., Stephens C., Zweiger G., Shapiro L., Alley M.K.R.;
RT "Caulobacter Lon protease has a critical role in cell-cycle control of DNA
RT methylation.";
RL Genes Dev. 10:1532-1542(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
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 (By similarity). CcrM is an important target of
CC the Lon protease pathway in C.crescentus. {ECO:0000255|HAMAP-
CC Rule:MF_01973, ECO:0000269|PubMed:8666236}.
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: Constitutively expressed at a constant level throughout the
CC cell cycle (at protein level) (PubMed:8666236). By heat shock.
CC {ECO:0000255|HAMAP-Rule:MF_01973, ECO:0000269|PubMed:8666236}.
CC -!- DISRUPTION PHENOTYPE: Cells grow more slowly, cells stall in
CC predivisional stage, about half eventually divide. Abnormal inititation
CC of extra rounds of DNA replication. CcrM methyltransferase is present
CC at all stages of the cell cycle, at least partially responsible for the
CC above phenotypes. {ECO:0000269|PubMed:8666236}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_01973}.
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DR EMBL; U56652; AAB18765.1; -; Genomic_DNA.
DR EMBL; CP001340; ACL95502.1; -; Genomic_DNA.
DR RefSeq; WP_010919826.1; NC_011916.1.
DR RefSeq; YP_002517410.1; NC_011916.1.
DR AlphaFoldDB; B8GX12; -.
DR SMR; B8GX12; -.
DR MEROPS; S16.001; -.
DR PRIDE; B8GX12; -.
DR EnsemblBacteria; ACL95502; ACL95502; CCNA_02037.
DR GeneID; 7333368; -.
DR KEGG; ccs:CCNA_02037; -.
DR PATRIC; fig|565050.3.peg.1995; -.
DR HOGENOM; CLU_004109_4_3_5; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR PhylomeDB; B8GX12; -.
DR Proteomes; UP000001364; 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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Reference proteome; Serine protease; Stress response.
FT CHAIN 1..799
FT /note="Lon protease"
FT /id="PRO_0000378303"
FT DOMAIN 7..198
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 587..768
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 772..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..799
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 674
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 717
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT CONFLICT 125
FT /note="A -> G (in Ref. 1; AAB18765)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="A -> R (in Ref. 1; AAB18765)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="D -> E (in Ref. 1; AAB18765)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 799 AA; 88244 MW; 72911212A74C48D2 CRC64;
MSELRTLPVL PLRDIVVFPH MVVPLFVGRD KSVRALEEVM RGDKQILLVT QKNSADDDPA
PGDIFEVGVL ATVLQLLKLP DGTVKVLVEG KARAAVVSFT DQESYYEAQI GEVSEDDGAG
PEAEALSRAV VEQFENYVKL NKKVPPEALA SIPQIAEPGK LADSIAAHLS VKIGDKQNLL
EIFDVVKRLE KVFALMEGEI SVLQVEKKIR SRVKRQMEKT QREYYLNEQM KAIQRELGDP
DDARDELIDL EKRIKKTKLS KEARTKAESE LKKLRNMSPM SAESTVVRNY LDWLLSIPWG
KAKTKKIDLV ESEGILDADH YGLEKVKERI LEYLAVQART NSLKGPILCL VGPPGVGKTS
LGKSIAKATG REFVRMSLGG VRDEAEIRGH RRTYIGSMPG KVVQSMKKAK TTNAFVLLDE
IDKMGSDYRG DPASALLEVL DPSQNSTFGD HYLEVDYDLS QVMFVTTANS LNMPQPLLDR
MEIIRIPGYT EDEKLEIAKR HILPKLAKDH GLKPAEFIVP DKAIRDLIRY YTREAGVRSL
ERELGALARK TVRDLAREKV ASITIDDERL AKYAGVKKYR YGETDEVDQV GIVTGLAWTE
FGGDILTIEA VKMPGKGRMQ ITGNLKDVMK ESIAAANSYV RSRALQFGIK PPVFEKTDVH
IHVPDGATPK DGPSAGIAMA LAMVSVLTGI PIRKDIAMTG EITLRGRVTA IGGLKEKLLA
ALRSGVKTVL IPQENEKDLA DVPQTVKDGL EIIPVSTVDE VLKHALTGPL TPVEWNEAEE
PITTSAKKDD GDSDAMLTH
