ID K1KGP6_9BURK Unreviewed; 827 AA.
AC K1KGP6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=HMPREF9465_01574 {ECO:0000313|EMBL:EKB30884.1};
OS Sutterella wadsworthensis 2_1_59BFAA.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=742823 {ECO:0000313|EMBL:EKB30884.1, ECO:0000313|Proteomes:UP000005835};
RN [1] {ECO:0000313|EMBL:EKB30884.1, ECO:0000313|Proteomes:UP000005835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2_1_59BFAA {ECO:0000313|EMBL:EKB30884.1,
RC ECO:0000313|Proteomes:UP000005835};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M.,
RA Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Sutterella wadsworthensis 2_1_59BFAA.";
RL Submitted (MAY-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:EKB30884.1}.
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DR EMBL; ADMG01000035; EKB30884.1; -; Genomic_DNA.
DR RefSeq; WP_005435821.1; NZ_JH815517.1.
DR AlphaFoldDB; K1KGP6; -.
DR STRING; 742823.HMPREF9465_01574; -.
DR PATRIC; fig|742823.3.peg.1566; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_4; -.
DR OrthoDB; 9803599at2; -.
DR Proteomes; UP000005835; 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 Reference proteome {ECO:0000313|Proteomes:UP000005835};
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 14..205
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 598..779
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 797..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 685
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 728
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 360..367
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 827 AA; 90675 MW; 3A5949A5B582B8E7 CRC64;
MTDGEVIYPE QIEVPAVAVR DMVIFPSTLV PVFMAREASV NAARKAFQSD NKYVFVVTQK
EPDTDAPKQD DCYGVGTLAS VMQFFGLADG TSKMLVEGLA RYRVDSLFER DGSLVARCTR
LHTVYAPERT LEPLRRQLMS EWKKYGSFGT GKSEPAGRFD AETDPERLLD LVCGQMSGLA
AAKMEMLAEV DLAARFRHGI DFLLTQIDLQ KLNVRIDGRV KRQMDKNQRD YYLHEQLKAI
RKELGDTDEG ADEEYADLEA RIASAKMPKY AEETVRNELR RLRQMPAMSS ESVVVRSYIE
TLTDYPWTKK SRVSRDLEAA ARILDEDHSG LEKVKERILE YLAVQKRVGK VKSPILCFVG
APGVGKTSLG ESIARATGRK YVRVALGGVH DESEIRGHRR TYVGSMPGQI IKSMIRAGVR
NPLFLLDEID KMGTDHRGDP ASAMLEVLDP EQNNAFADHY MEIPVDLSDV MFVATSNSYD
IPPALLDRME VISLSGYTEE EKIHISEHHL IPKQLRATGL KAEEVDLPRE AIVDIIRYWT
REAGVRGLER LIGKIFRKVV FAADKKGGSM PEKVVIKPES LSTYLGPAKY TIGLASKEPR
VGVVNGLAWT SVGGEMLVIE AQIFPGKGGV QRTGSLGDVM KESVETARSV VRARAANLGI
DTKRFYETDL HVHYPEGATP KDGPSAGIAT TTAIISAMTG IPVRSDVAMT GEITLHGEVL
EIGGLKEKLL AAVRAGCTKI LIPDVNRRDL EDVPETAKTQ IEVIPVKTID EVIAQALVRL
PEPLAVEAET AGAAAGAATG EAAASAAEER SSKASSAGKT PTLEVHA
//
