LON_FUSNN
ID LON_FUSNN Reviewed; 768 AA.
AC Q8RHK0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Lon protease {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 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=FN2014;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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}.
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; AE009951; AAL94104.1; -; Genomic_DNA.
DR RefSeq; NP_602805.1; NC_003454.1.
DR AlphaFoldDB; Q8RHK0; -.
DR SMR; Q8RHK0; -.
DR STRING; 190304.FN2014; -.
DR MEROPS; S16.009; -.
DR EnsemblBacteria; AAL94104; AAL94104; FN2014.
DR KEGG; fnu:FN2014; -.
DR PATRIC; fig|190304.8.peg.482; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_0; -.
DR InParanoid; Q8RHK0; -.
DR OMA; KKMNPVM; -.
DR BioCyc; FNUC190304:G1FZS-501-MON; -.
DR Proteomes; UP000002521; 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..768
FT /note="Lon protease"
FT /id="PRO_0000396568"
FT DOMAIN 4..196
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 586..768
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 674
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 717
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 349..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 768 AA; 86349 MW; BCAE37797F58CEA4 CRC64;
MLKAPFLPIR DLVIFPNVVT PIYVGRANSI ATLEKAIANK TKLVLGLQKD ASQENPTFDG
DIYEVGVIAN IVQIIRMPNN NIKVLVEAED RVKIKNIEKE ENEYVTTYTV IKETLKDSKE
TEAIYRKVFT RFEKYVSMIG KFSSELILNL KKIEDYSNGL DIMASNLNIS SEKKQEILEI
SNVRDRGYRI LDEIVAEMEI ASLEKTIDDK VKNKMNEAQR AYYLKEKISV MKEELGDFSQ
DDDVIEIVDR LKNTELPKEV REKLEAEVKK LTKMQPFSAE SSVIRNYIEA VLELPWNSET
NDVLDLKKAS QILERDHYGL KDAKEKVLDY LAVKKLNPSM NGVILCLSGP PGIGKTSLVK
SIAESMGRKF VRVSLGGVRD EAEIRGHRRT YVGSMPGKIM KAMKEAGTNN PVMLLDEIDK
MSNDFKGDPA SAMLEVLDPE QNKNFEDHYI DMPFDLSKVF FVATANDLRN VSAPLRDRMD
ILQLSSYTEF EKLHIAQKFL LKQAQKENGL ANIDIKIPDK VMFKLIDEYT REAGVRNLKR
EIITICRKLA REVVEKDTKK FNLKPTDLEK YLGKAKFRPE KSRKATGKIG VVNGLAWTAV
GGVTLDVQGV DTPGKGEVTL TGTLGNVMKE SASVAMTYVK ANLKKYPPKD KDFFKDRTIH
LHFPEGATPK DGPSAGITIT TAIVSVLTNK KVRQDIAMTG EITITGDVLA IGGVREKVIG
AHRAGIKEVI LPEDNRVDTD EIPDELKSTM KIHFAKTYDD VSKLVFVK
