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
