ID B1YJV9_EXIS2 Unreviewed; 769 AA.
AC B1YJV9;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 124.
DE RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973};
DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973};
DE AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973};
GN Name=lon {ECO:0000256|HAMAP-Rule:MF_01973};
GN OrderedLocusNames=Exig_2145 {ECO:0000313|EMBL:ACB61597.1};
OS Exiguobacterium sibiricum (strain DSM 17290 / CIP 109462 / JCM 13490 /
OS 255-15).
OC Bacteria; Bacillota; Bacilli; Bacillales;
OC Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX NCBI_TaxID=262543 {ECO:0000313|EMBL:ACB61597.1, ECO:0000313|Proteomes:UP000001681};
RN [1] {ECO:0000313|EMBL:ACB61597.1, ECO:0000313|Proteomes:UP000001681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC {ECO:0000313|Proteomes:UP000001681};
RX PubMed=16489412; DOI=10.1007/s00792-005-0497-5;
RA Rodrigues D.F., Goris J., Vishnivetskaya T., Gilichinsky D.,
RA Thomashow M.F., Tiedje J.M.;
RT "Characterization of Exiguobacterium isolates from the Siberian permafrost.
RT Description of Exiguobacterium sibiricum sp. nov.";
RL Extremophiles 10:285-294(2006).
RN [2] {ECO:0000313|EMBL:ACB61597.1, ECO:0000313|Proteomes:UP000001681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC {ECO:0000313|Proteomes:UP000001681};
RX PubMed=19019206; DOI=10.1186/1471-2164-9-547;
RA Rodrigues D.F., Ivanova N., He Z., Huebner M., Zhou J., Tiedje J.M.;
RT "Architecture of thermal adaptation in an Exiguobacterium sibiricum strain
RT isolated from 3 million year old permafrost: a genome and transcriptome
RT approach.";
RL BMC Genomics 9:547-547(2008).
RN [3] {ECO:0000313|Proteomes:UP000001681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17290 / CIP 109462 / JCM 13490 / 255-15
RC {ECO:0000313|Proteomes:UP000001681};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Chertkov O., Monk C.,
RA Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Vishnivetskaya T.,
RA Rodrigues D.F., Gilichinsky D., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Exiguobacterium sibiricum 255-15.";
RL Submitted (APR-2008) 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, ECO:0000256|PROSITE-
CC ProRule:PRU01122};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000256|HAMAP-Rule:MF_01973}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01973}.
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|PROSITE-ProRule:PRU01122,
CC ECO:0000256|RuleBase:RU000591}.
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DR EMBL; CP001022; ACB61597.1; -; Genomic_DNA.
DR RefSeq; WP_012371014.1; NC_010556.1.
DR AlphaFoldDB; B1YJV9; -.
DR STRING; 262543.Exig_2145; -.
DR MEROPS; S16.001; -.
DR KEGG; esi:Exig_2145; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_9; -.
DR OrthoDB; 9803599at2; -.
DR Proteomes; UP000001681; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973,
KW ECO:0000256|PIRSR:PIRSR001174-2};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01973};
KW Reference proteome {ECO:0000313|Proteomes:UP000001681};
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 6..196
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 587..768
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT COILED 193..221
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 674
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 717
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 351..358
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 769 AA; 85697 MW; 6610C927E01DAD6D CRC64;
MKTKQYPLLP LRGVVAYPLI GLTIDVGRPV SLKALLASKE HEIDLVVVTQ RDPEAEPSVD
GLHTIGTLVQ IAKMSELGND TVRVRVIGKE RVRIDQVTET DEGYQASIEP IEKADIKGAK
QEALVRLIKE QFGQLVSRIK GIGTDERRRF ETYERLDSLT DYIASKLPID IAKKQEFLEE
NDPVERGVML LDVMKHEYEV VELEREMRER TKKTIEQSQR EYYLREQLKT IQQELGGEAV
SAESDAVKYK EKLALLDLSE TAVINIEKEI NRLSVVPATS PEHGVIRNYL EWFFSLPWNE
ATDDFLNVEA ASEQLDEDHY GLEKVKERIL EYLAVRQLTD SLRGPILCLA GPPGVGKTSL
ARSIATALER KFVRVSLGGV RDEAEIRGHR RTYIGAMPGR IIRGLKQAGT NNPVFLLDEI
DKMANDFRGD PSSAMLEVLD PEQNNSFSDH YIEEPFDLSN VLFIATANDV SNIPGPLLDR
MELIQIGGYT EQEKTEIAIR HLLSKQLKEH GLKKSQLTVK PDALQEVVRR YTREAGVRSL
ERVIGALCRK AAKQIAMGEK KRVTVTKRNL PDFLGKPIYR YGQSELEDTI GAVTGLAYTA
FGGDTLTIEV SLAPGKGKLQ LTGKLGDVMQ ESAQTAHSFV RANAEAFKID PNFYETQDIH
IHVPEGAVPK DGPSAGITIA TALISALTKR PVRRDVGMTG EITLRGRVLP IGGLKEKSLA
AHRAGLTTIL MPQDNTRDID DIPETVRDGI RFIPVATMDQ VLEHALKGE
//
