ID W0U8E0_9FIRM Unreviewed; 803 AA.
AC W0U8E0;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
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:CCO06054.1};
GN ORFNames=RBI_II00280 {ECO:0000313|EMBL:CCO06054.1};
OS Ruminococcus bicirculans (ex Wegman et al. 2014).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminococcus.
OX NCBI_TaxID=1160721 {ECO:0000313|EMBL:CCO06054.1, ECO:0000313|Proteomes:UP000027600};
RN [1] {ECO:0000313|EMBL:CCO06054.1, ECO:0000313|Proteomes:UP000027600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=80/3 {ECO:0000313|EMBL:CCO06054.1};
RX PubMed=23919528; DOI=10.1111/1462-2920.12217;
RA Wegmann U., Louis P., Goesmann A., Henrissat B., Duncan S.H., Flint H.J.;
RT "Complete genome of a new Firmicutes species belonging to the dominant
RT human colonic microbiota ('Ruminococcus bicirculans') reveals two
RT chromosomes and a selective capacity to utilize plant glucans.";
RL Environ. Microbiol. 16:2879-2890(2014).
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; HF545617; CCO06054.1; -; Genomic_DNA.
DR RefSeq; WP_041337342.1; NZ_HF545617.1.
DR AlphaFoldDB; W0U8E0; -.
DR STRING; 1160721.RBI_II00280; -.
DR GeneID; 41520343; -.
DR KEGG; rus:RBI_II00280; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_9; -.
DR OrthoDB; 9803599at2; -.
DR Proteomes; UP000027600; Chromosome II.
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 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 13..207
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 599..780
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 686
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT ACT_SITE 729
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PIRSR:PIRSR001174-1"
FT BINDING 363..370
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 803 AA; 89697 MW; F4FD79960EFA9594 CRC64;
MKDKTDVKIN NIMPCVPTRD LVVFPGMSMH FDVGRPRTIK SMKNAMDGDQ LVFLCAQKDV
YLEMPEKKDM FKVGTVAKVR QIVKAPDGIY RCYVEGLRKA RLAEFYQYDD CYEADVRLVP
NYSKDRLDDD EQLAVFRSVL DEFEEYVQVV PKMPEELYAQ ILGSKTPVQL FESLAFNIPL
AFTDRQSLLE APSVSDKLIL MVTILSRETN VLSLERRIHS QVHSQIEESQ REYYIREQIK
ALQNELGENE DGSDVNEIDE YTHRIDSLVL SEEVRDKLMG EVRKLSKMGM MSQEGVVLRN
YLDTVLALPW NAVTKDRTDV KKAKQILDKD HYGMAKVKDR ILENLAVRAL TPDVKGQILC
LVGPPGVGKT SVAKSVARAL NRNFVRVSLG GVKDESDIRG HRKTYVGAMP GRIMNAMKLA
GSKNPVVLLD EIDKMSNDFR GDPSSAMLEV LDSEQNNAFR DHYIEVPFDL SDVLFITTAN
TLDTVQAPLL DRMEVIELSS YTREEKFHIA KEHLIKKQEG KNGLKASQIR ICNDAIYKLI
DSYTREAGVR NLERQLGSLC RKAAKEIVED GVKKVTFKAD NLEKYLGHEK YLPDVVSDKD
AVGSVNGLAW TSVGGVVMPL EVLVLDGKGR IELTGSLGDV MKESAKIAVS YCRSVADKYG
IDKDFYEKKD LHIHAPEGAV PKDGPSAGVT MITGIISALG NIKVRSDVAM TGEITLSGKV
LPIGGLREKT MAAYKAGVKT IIVPFANKGD LDDVDDTVKL CCEFVFAKTI QDVLDVALVP
NSKNNVPLEL LSKNEPERKK LTV
//
