LON2_HERA2
ID LON2_HERA2 Reviewed; 815 AA.
AC A9B3R2;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Lon protease 2 {ECO:0000255|HAMAP-Rule:MF_01973};
DE EC=3.4.21.53 {ECO:0000255|HAMAP-Rule:MF_01973};
DE AltName: Full=ATP-dependent protease La 2 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon2 {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=Haur_2996;
OS Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95).
OC Bacteria; Chloroflexi; Chloroflexia; Herpetosiphonales; Herpetosiphonaceae;
OC Herpetosiphon.
OX NCBI_TaxID=316274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23779 / DSM 785 / 114-95;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779.";
RL Submitted (OCT-2007) 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:0000255|HAMAP-Rule:MF_01973}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01973};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- INDUCTION: By heat shock. {ECO:0000255|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000255|HAMAP-
CC Rule:MF_01973}.
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DR EMBL; CP000875; ABX05634.1; -; Genomic_DNA.
DR AlphaFoldDB; A9B3R2; -.
DR SMR; A9B3R2; -.
DR STRING; 316274.Haur_2996; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; ABX05634; ABX05634; Haur_2996.
DR KEGG; hau:Haur_2996; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_0; -.
DR OMA; VLDCVPM; -.
DR Proteomes; UP000000787; 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 Gene3D; 2.30.130.40; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; PTHR10046; 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 SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00763; lon; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
DR PROSITE; PS01046; LON_SER; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Hydrolase; Nucleotide-binding; Protease;
KW Reference proteome; Serine protease; Stress response.
FT CHAIN 1..815
FT /note="Lon protease 2"
FT /id="PRO_0000396574"
FT DOMAIN 19..210
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 601..782
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 688
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 731
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 365..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 815 AA; 90406 MW; 979C3FE5B4B20427 CRC64;
MADDRQLVDE ISAATTLELP VLPLINTVLF PTMVTPLFVA RELSMAAIEA AMSADRQIVA
VAQRAIEIEE HDTSQLYQVG VIAHIERVLK LPDGTTSVLV QGQQRVQIVD WLATEPYINA
QVQIIEPDHE SSLAIEAMMR GVLASYEKVV KLSRTMPDDA YVAALNLEDA SALADLIAST
LPLDIVRRQQ LLELFEVEER LRRLSVVLSQ EIDVLELEHH IQNQVQKEVD KSQRDFFLRE
QLKAIQTELG QEDPLTRELN ELHDRIVAAN LPAKAQAKAL EELGRLEMMP PAAPEYSVIR
TYLDWLLELP WSKTSADVAD LEVAAKVLEN NHYGLKKVKE RILEFIAVRM LAGDSTKSPI
LCFVGPPGVG KTSLGRSVAE ALGREFVRLS LGGVHDEAEI RGHRRTYIGA MPGRIIQTMK
DAGTINPVFM LDEIDKLGND FRGDPAAALL EVLDPEQNNT FADHYLDLPY DLSKIMFITT
ANMLDPIDEP LLDRMEIVEL PGYIEEEKVQ IARKFLIPKQ IEANGLKQHP ITISDEALRQ
IIRTYTWEAG VRNLEREIGG ICRKIARRVA EKKRYPRRIT PTMLTDFLGQ PPFDYSRAND
RDEIGVATGM VWSSNGGDVV AIETAIVDGK GTTTLTGQLG DVMQESAQAA LSYARASSRR
LGIDGKRFEK IDIHIHVPEG GVPKDGPSAG ITLACSVISA LTHRPLRRDV AMTGEITLRG
RVLPIGGLRD KILGAYRAGI TTMLIPKKNL RDLEEVPNNV RRQITVVAVE HMDEVLPIAF
VSNPLERGSQ HTSDGDQTSV VLPTITQPQL GSVEL
