UniProt: Q1PXW3

Database: UniProt
Entry: Q1PXW3_KUEST

LinkDB:  Q1PXW3_KUEST 
Original site:  Q1PXW3_KUEST

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (3)   
   EMBL (3)   
Protein domain (21)   
   InterPro (13)   
   Pfam (3)   
   PROSITE (3)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (35)   

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ID   Q1PXW3_KUEST            Unreviewed;       805 AA.
AC   Q1PXW3;
DT   16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
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   ECO:0000313|EMBL:CAJ72871.1};
GN   Synonyms=lon_1 {ECO:0000313|EMBL:SOH04352.1};
GN   ORFNames=KsCSTR_03630 {ECO:0000313|EMBL:QII09742.1}, KSMBR1_1853
GN   {ECO:0000313|EMBL:SOH04352.1}, kustd2126
GN   {ECO:0000313|EMBL:CAJ72871.1};
OS   Kuenenia stuttgartiensis.
OC   Bacteria; Planctomycetota; Candidatus Brocadiia; Candidatus Brocadiales;
OC   Candidatus Brocadiaceae; Kuenenia.
OX   NCBI_TaxID=174633 {ECO:0000313|EMBL:CAJ72871.1};
RN   [1] {ECO:0000313|EMBL:CAJ72871.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16598256; DOI=10.1038/nature04647;
RA   Strous M., Pelletier E., Mangenot S., Rattei T., Lehner A., Taylor M.W.,
RA   Horn M., Daims H., Bartol-Mavel D., Wincker P., Barbe V., Fonknechten N.,
RA   Vallenet D., Segurens B., Schenowitz-Truong C., Medigue C., Collingro A.,
RA   Snel B., Dutilh B.E., OpDenCamp H.J.M., vanDerDrift C., Cirpus I.,
RA   vanDePas-Schoonen K.T., Harhangi H.R., vanNiftrik L., Schmid M.,
RA   Keltjens J., vanDeVossenberg J., Kartal B., Meier H., Frishman D.,
RA   Huynen M.A., Mewes H., Weissenbach J., Jetten M.S.M., Wagner M.,
RA   LePaslier D.;
RT   "Deciphering the evolution and metabolism of an anammox bacterium from a
RT   community genome.";
RL   Nature 440:790-794(2006).
RN   [2] {ECO:0000313|EMBL:CAJ72871.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Genoscope;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000221734}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Frank J.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:SOH04352.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kuenenia_mbr1_ru-nijmegen {ECO:0000313|EMBL:SOH04352.1};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:QII09742.1, ECO:0000313|Proteomes:UP000501926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CSTR1 {ECO:0000313|EMBL:QII09742.1,
RC   ECO:0000313|Proteomes:UP000501926};
RA   Ding C., Adrian L.;
RT   "Newly sequenced genome of strain CSTR1 showed variability in Candidatus
RT   Kuenenia stuttgartiensis genomes.";
RL   Submitted (FEB-2020) 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}.
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DR   EMBL; CT573072; CAJ72871.1; -; Genomic_DNA.
DR   EMBL; CP049055; QII09742.1; -; Genomic_DNA.
DR   EMBL; LT934425; SOH04352.1; -; Genomic_DNA.
DR   KEGG; kst:KSMBR1_1853; -.
DR   OrthoDB; 9803599at2; -.
DR   Proteomes; UP000221734; Chromosome Kuenenia_stuttgartiensis_MBR1.
DR   Proteomes; UP000501926; 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:SF64; 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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01973};
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:UP000221734};
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          37..228
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51787"
FT   DOMAIN          618..799
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   ACT_SITE        705
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   ACT_SITE        748
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   BINDING         382..389
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   805 AA;  89435 MW;  12C8F3C1854359C7 CRC64;
     MTNSENNNHG EDQEHPVLTV EEEVQDKIER IKIPHETPVL PVKDTVVFPG MVAALSVYTD
     RDIKLLNDVL AGNRFLTLTA QKDKDIKVLK QSDIYECATA AVVLQMLRMP DNSAKMLVQG
     LRRVKIGEYV QSDPYFKAKI SAIEDIIEDD RETEALARNA ADQFAHMISM MPSLPEELKI
     AVVNIENPSR LADLITSHLN VSVAEKQKVL ELANVKLRLQ KVTTLIASEL EVLEMATKIQ
     SQVRNEMEKG QKEYYLRQQL KAIQDELGEG DERSMEIKEL KEKIENAKMP AEAKKEAERE
     LERLAKMHSA SAEYTVSRTY LDLLIALPWS VSTKDQLDIK TASTILDEDH YDLEKLKERI
     LEYLAVRKLK DDMKGPILCF VGPPGTGKTS VGMSIARSMG RKFVRMSLGG VRDEAEIRGH
     RRTYIGALPG RIIQGLKKAE SNNPVFMLDE IDKLGADFRG DPSAALLEVL DPEQNHAFSD
     HYLDVAFDLS NVMFITTANI LDTVPPALKD RMEVLELSGY TAEEKISIVK KFILPKQLKA
     HGLKEEQLTI TDDAIKMVIT DYTREAGLRN LEREIAHLCR KTAKKIASGE ETSVTINAEQ
     LNTLLGPIKF FSEAAERTTD AGVATGLAWT QAGGDILFIE ATFMPGTGKL TLTGCLGDIM
     KESAQAAMSY IRSKLESLKI SFKDFDKYDF HIHVPAGAIP KDGPSAGVTM AMALISLLKG
     TPILSNVAMT GEITLRGRVL PVGGIKEKVL AAKRAGITTV VLPKRNEKDL TEVPENAKKR
     LNFAFVERVD EMLPIVFGAE EPKKG
//

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