LON_XANOR
ID LON_XANOR Reviewed; 850 AA.
AC Q5H432;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=XOO1035;
OS Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=291331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC10331 / KXO85;
RX PubMed=15673718; DOI=10.1093/nar/gki206;
RA Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S.,
RA Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H.,
RA Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S.,
RA Go S.-J.;
RT "The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the
RT bacterial blight pathogen of rice.";
RL Nucleic Acids Res. 33:577-586(2005).
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; AE013598; AAW74289.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5H432; -.
DR SMR; Q5H432; -.
DR STRING; 291331.XOO1035; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; AAW74289; AAW74289; XOO1035.
DR KEGG; xoo:XOO1035; -.
DR HOGENOM; CLU_004109_4_3_6; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000006735; 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..850
FT /note="Lon protease"
FT /id="PRO_0000396617"
FT DOMAIN 38..230
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 634..815
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 819..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 721
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 764
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 384..391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 850 AA; 93449 MW; 549816F9926F86B9 CRC64;
MQHLADGPIT GPSAFLFPQI PIPAERPMAQ SQPEVLDLPV LPLRDVVVFP HMVIPLFVGR
DKSMRALEKA MEADKRILLV AQKSAETDDP AAVDLHTVGT LAQVLQLLKL PDGTIKVLVE
GLSRVTVDKV VEQDGALQGQ GTEVEASDAR EPREVEAIAR SLMSLFEQYV KTNRKLPPEL
LQTLAGIDEP GRLADTIAPH IGVRLADKQR LLEITDIGER LELLVGLVDG EIDVQQLEKR
IRGRVKSQME KSQREYYLNE QMKAIQKELG DLDDVPGELE ELARKIAEAG MPKPVETKAK
AELNKLKQMS PMSAEAAVVR NYLDWLLGVP WKKRTKVRKD LKVAEDTLDA DHYGLDKVKE
RILEYLAVQS RVKQMKGPIL CLVGPPGVGK TSLGQSIAKA TNRKFVRMSL GGIRDEAEIR
GHRRTYVGSM PGRLVQNLNK VGSKNPLFLL DEIDKMSMDF RGDPSSALLE VLDPEQNNSF
NDHYLEVDLD LSEVMFVATS NSLNIPGPLL DRMEVIRIPG YTEDEKLNIA MRYLVPKQIK
ANGLKPEEIE IGGDAIQDIV RYYTRESGVR NLEREVAKIC RKVVKEIALA GPQPAAKKAV
AKKGKPKALV TVNAKNLDKY LGVRRFDFGR AEEENEIGLV TGLAWTEVGG ELLQVESTLV
PGKGNLILTG QLGNVMKESA SAALSVVRSR AERLGIDVDF LQKQDVHVHV PDGATPKDGP
SAGIAMVTSL VSVLTKVPIR ADVAMTGEIT LRGRVSAIGG LKEKLLAALR GGIRTVLIPG
ENRKDLADIP ANVTRDLKIV PVKWIDEVLD LALERPLTPK KAGKEKARKT APRVAVRGKS
RSTPGTRVKH
