LON_CAUVC
ID LON_CAUVC Reviewed; 799 AA.
AC P0CAW0; P52977;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=CC_1960;
OS Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=190650;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19089 / CB15;
RX PubMed=11259647; DOI=10.1073/pnas.061029298;
RA Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT "Complete genome sequence of Caulobacter crescentus.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(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 (By similarity). CcrM is an important target of
CC the Lon protease pathway in C.crescentus (By similarity).
CC {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; AE005673; AAK23935.1; -; Genomic_DNA.
DR PIR; C87492; C87492.
DR RefSeq; NP_420767.1; NC_002696.2.
DR RefSeq; WP_010919826.1; NC_002696.2.
DR AlphaFoldDB; P0CAW0; -.
DR SMR; P0CAW0; -.
DR STRING; 190650.CC_1960; -.
DR MEROPS; S16.001; -.
DR PRIDE; P0CAW0; -.
DR EnsemblBacteria; AAK23935; AAK23935; CC_1960.
DR KEGG; ccr:CC_1960; -.
DR PATRIC; fig|190650.5.peg.1976; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_5; -.
DR OMA; GAWQVVD; -.
DR BioCyc; CAULO:CC1960-MON; -.
DR Proteomes; UP000001816; 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..799
FT /note="Lon protease"
FT /id="PRO_0000076129"
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"
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
