ID A0A3D8VC62_9GAMM Unreviewed; 812 AA.
AC A0A3D8VC62;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
DE AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973};
GN Name=lon {ECO:0000256|HAMAP-Rule:MF_01973};
GN ORFNames=DX912_12845 {ECO:0000313|EMBL:RDY66621.1}, GOY17_12825
GN {ECO:0000313|EMBL:QGW65711.1};
OS Lysobacter soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=453783 {ECO:0000313|EMBL:RDY66621.1, ECO:0000313|Proteomes:UP000256829};
RN [1] {ECO:0000313|EMBL:RDY66621.1, ECO:0000313|Proteomes:UP000256829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 22011 {ECO:0000313|EMBL:RDY66621.1,
RC ECO:0000313|Proteomes:UP000256829};
RA Zhang X., Feng G., Zhu H.;
RT "Lysobacter soli KCTC 22011, whole genome shotgun sequence.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QGW65711.1, ECO:0000313|Proteomes:UP000424027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XL170 {ECO:0000313|EMBL:QGW65711.1,
RC ECO:0000313|Proteomes:UP000424027};
RA Sun X.;
RT "Microbial interaction.";
RL Submitted (DEC-2019) 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:0000256|HAMAP-Rule:MF_01973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01973,
CC ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}.
CC -!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122, ECO:0000256|RuleBase:RU000591}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP046603; QGW65711.1; -; Genomic_DNA.
DR EMBL; QTJR01000008; RDY66621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8VC62; -.
DR KEGG; lsol:GOY17_12825; -.
DR OrthoDB; 9803599at2; -.
DR Proteomes; UP000256829; Unassembled WGS sequence.
DR Proteomes; UP000424027; 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 CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF56; LON PROTEASE; 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 PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01973};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973,
KW ECO:0000256|PIRNR:PIRNR001174};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01973};
KW Reference proteome {ECO:0000313|Proteomes:UP000256829};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_01973};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_01973}.
FT DOMAIN 12..204
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 600..781
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 783..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 687
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 730
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 358..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 812 AA; 89140 MW; E66FD0748D7A2231 CRC64;
MAVSTEHETL TLPVLPLRDV VVFPHMVIPL FVGRDKSIHA LDVAMEADKR ILLVAQKSAE
TDDPGADDLY KVGTLAQVLQ LLKLPDGTIK VLVEGVSRVN VHDVTERGGA LSGQAEVVEP
ESDREEREIE AIARSLMGLF EQYVKTNRKL PPELMQTLSG IDEPGRLADT IAAHLGVRIG
DKQKLLETHG VGARLEQLVG LVDGEIDVQQ LEKRIRGRVK SQMEKSQREY YLNEQMKAIQ
KELGEIDDAP NDIDELTRKI AEAGMPKAVE AKAKAELNKL KQMSPMSAEA AVVRNYLDWL
LGVPWKKRTK VRKDLKAAQD VLDADHFGLE KVKDRILEYL AVQSRVKQMK GPILCLVGPP
GVGKTSLGQS IAKATNRKFV RMSLGGVRDE AEIRGHRRTY VGSMPGRIVQ NLNKVGSKNP
LFVLDEIDKM SMDFRGDPSS ALLEVLDPEQ NNAFNDHYLE VDLDLSEVMF VATSNSLNIP
GPLLDRMEVI RIPGYTEEEK LNIAMRYLLP KQIKGNGLKP EELKVAESAV RDIVRYYTRE
SGVRSLEREI AKICRKVVKE IALAGPSKKG AKKNVVNVTS KNLDKYLGVR RYDFGRAEEQ
NEVGLVTGLA WTEVGGDLLQ IEATLVPGKG QLLLTGQLGD VMKESASAAL SVVRARTEQL
GIDLDFLQKH DVHVHVPEGA TPKDGPSAGI AMATALVSML TRNPVKADVA MTGEITLRGR
VLPIGGLKEK LLAALRGGIR TVIIPEENRK DLADLPKTVT QGLKIIPAKW IDEVLNIALE
RAPTPAPASA SGEGETPVRD GSKTVTQTDV KH
//
