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LON_AZOC5
ID   LON_AZOC5               Reviewed;         856 AA.
AC   A8HYF7;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, 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=AZC_1610;
OS   Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS   6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC   13405 / ORS 571;
RA   Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT   "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT   caulinodans ORS571.";
RL   Submitted (APR-2007) 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; AP009384; BAF87608.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8HYF7; -.
DR   SMR; A8HYF7; -.
DR   STRING; 438753.AZC_1610; -.
DR   MEROPS; S16.001; -.
DR   PRIDE; A8HYF7; -.
DR   EnsemblBacteria; BAF87608; BAF87608; AZC_1610.
DR   KEGG; azc:AZC_1610; -.
DR   eggNOG; COG0466; Bacteria.
DR   HOGENOM; CLU_004109_4_3_5; -.
DR   OMA; GAWQVVD; -.
DR   BRENDA; 3.4.21.53; 609.
DR   Proteomes; UP000000270; 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..856
FT                   /note="Lon protease"
FT                   /id="PRO_0000396535"
FT   DOMAIN          68..259
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          647..828
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT   ACT_SITE        734
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   ACT_SITE        777
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT   BINDING         412..419
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ   SEQUENCE   856 AA;  94404 MW;  8AF4119A7EAFCDE3 CRC64;
     MVNTPVPGLG SCASRGLIAA PASIIRSRPG CDHAGECIVV CVGVFRKDWV MTSPKQRPPL
     VPGVAQTFPV LPLRDIVVFP HMIVPLFVGR EKSIRALEEV MRGDTYILLA TQENASDDDP
     ATDAIYRVGT LATVLQLLKL PDGTVKVLVE GVTRAQVVQY TDRADLYEAE AISLPDEVGD
     VVEAEALARS VVNEFENYVK LNKKVSPEVV GVVGQIEDHA KLADTIASHL AVKIPEKQAV
     LETVKVADRL EKVLGLMESE ISVLQVEKRI RTRVKRQMEK TQREYYLNEQ MKAIQKELGD
     EDGRDDLQEL EDRIKRTKLT KEAREKATHE LKKLRQMSPM SAEATVVRNY LDWLLSIPWG
     IKSKVKKDLP FAQSVLDSDH YGLDKVKERI VEYLAVQSRA NKLAGPILCL VGPPGVGKTS
     LGRSIAKATG REFVRVSLGG VRDEAEIRGH RRTYIGSMPG KIIQSMRKAK KSNPLFLLDE
     IDKMGADFRG DPSAALLEVL DPEQNPTFND HYLEVDYDLS NVMFVTTANT LNIPPALLDR
     MEVIRIAGYT EDEKAEISRK HLIPNALQKH GLSAKEWSID DAALLQVIRR YTREAGVRNL
     EREISTLARK AVKELVISKK KSVKVTAKNL ETFLGVPRFR YGEIEREDQV GVVTGLAWTE
     VGGELLTIEG VMMPGKGRMT VTGNLKEVMK ESISAAASYV RSRSVDFGIE PPLFERRDIH
     VHVPEGATPK DGPSAGVAMA TTIVSVLTGI PVRRDVAMTG EITLRGRVLP IGGLKEKLLA
     ALRGGIKKVL IPEENAKDLA DIPDNVKNAL EIIPVSRMDE VLHHALLRHP EPISWTEQPV
     SGAVVPDEDA AGVVAH
 
 
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