GenomeNet

Database: UniProt
Entry: R7IIM7_9BURK
LinkDB: R7IIM7_9BURK
Original site: R7IIM7_9BURK 
ID   R7IIM7_9BURK            Unreviewed;       811 AA.
AC   R7IIM7;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
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=BN620_01568 {ECO:0000313|EMBL:CDE50447.1};
OS   Sutterella sp. CAG:351.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sutterellaceae; Sutterella.
OX   NCBI_TaxID=1262975 {ECO:0000313|EMBL:CDE50447.1, ECO:0000313|Proteomes:UP000018107};
RN   [1] {ECO:0000313|EMBL:CDE50447.1, ECO:0000313|Proteomes:UP000018107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:351 {ECO:0000313|Proteomes:UP000018107};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDE50447.1}.
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; CBJA010000237; CDE50447.1; -; Genomic_DNA.
DR   AlphaFoldDB; R7IIM7; -.
DR   STRING; 1262975.BN620_01568; -.
DR   Proteomes; UP000018107; Unassembled WGS sequence.
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; 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.
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   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW   Rule:MF_01973}; Stress response {ECO:0000256|HAMAP-Rule:MF_01973}.
FT   DOMAIN          13..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   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   811 AA;  89338 MW;  F0A34F817B086ECF CRC64;
     MTEKTQNTAL EVFPLLPLRD IVVFPRMVIT LFMGRAKSIR AAEIAMNQGK KILLVAQRDG
     QIDEPTGQDL FKVGCVGTIL QMLRLPDQTV KILVEGKERV DVSAVREVDG YLTASVSPRP
     MKESDPAETE ALRRATIESF TAYAKLNPKI PEDLARSVNQ TTDATRLADI VVQQLPVAVA
     AKQKLLESDD LNSTLTELLS LLGGETEIQK MEKRIHGRVK QQMEKNQRDY YLNEQMKAIQ
     KELGQGDDGN DVTDDYEKKI EAARMSPEAK DKALEELNKL RQMSPMSAEA TVVRAYLDTL
     ISLPWSKKTR VSSNIPKAKK ILDEDHYGLE KVKERILEYL AVQGRVTKVK APILCFVGAP
     GVGKTSLGES IARATGRKFT RLALGGVHDE AEIRGHRRTY VGSMPGKILQ NLIKVGVRNP
     LFLLDEVDKM GMDYRGDPAS ALLEVLDPEQ NSTFEDHYAE VPFDLSDVLF VATSNSYNIP
     PALLDRMEVI SLSGYTEEEK VHIAEEHLVP KQMRLNGVKK GELVIDRSAI VAIIRYYTRE
     AGVRGLEREI SKICRKVVMA NMMKEGTKKN AKTETVTVNE ENIGSYLGVR KFTFGVAAKK
     PQIGQVNGLA WTEVGGDLLS IEAAVFPGKG MVQRTGSLGD VMKESVEAAR SVVRERAESL
     GIKQDVFSKT DLHLHFPEGA TPKDGPSAGG AITTAIVSAL TRIPVRADVA MTGEITLRGE
     ILEIGGLKEK LLAALRGGIK KVMIPEDNVK DLAEIPQNVK DGLEIVPVRW IEQVLEQALV
     RMPEPLPKED MAESLAAVPA EQPGLPEIVA H
//
DBGET integrated database retrieval system