LON_FLAJ1
ID LON_FLAJ1 Reviewed; 817 AA.
AC A5FG89;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Fjoh_2754;
OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS 14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=376686;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 / UW101;
RX PubMed=19717629; DOI=10.1128/aem.01495-09;
RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA Cheng Y.Q., Stein J.L.;
RT "Novel features of the polysaccharide-digesting gliding bacterium
RT Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL Appl. Environ. Microbiol. 75:6864-6875(2009).
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; CP000685; ABQ05776.1; -; Genomic_DNA.
DR RefSeq; WP_012024815.1; NZ_MUGZ01000005.1.
DR AlphaFoldDB; A5FG89; -.
DR SMR; A5FG89; -.
DR STRING; 376686.Fjoh_2754; -.
DR EnsemblBacteria; ABQ05776; ABQ05776; Fjoh_2754.
DR KEGG; fjo:Fjoh_2754; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_10; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000006694; 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 Serine protease; Stress response.
FT CHAIN 1..817
FT /note="Lon protease"
FT /id="PRO_0000396565"
FT DOMAIN 44..237
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 626..807
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 713
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 756
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 390..397
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 817 AA; 91375 MW; F1056EB18ABA1172 CRC64;
MSNHKILTID NLSLQEFDSE AELIPLLTPE DEEEMNNEEL PVSLPILPLR NTVLFPGVVI
PISAGRDKSI KLINDANAGG KIIGVVSQIN EEDEDPSKDD IHKIGTVARI LRVLKMPDGN
VTVILQGKKR FEIDEVVSEE PYMTASIKEV SEERPDENDS EFTAILDSVK ELAIQIIKES
PNIPSEATFA IKNIESQSFL INFVSSNMNL SVKEKQGLLS INGLKERALE TLRYMNVELQ
KLELKNDIQS KVRFDLDQQQ REYFLHQQMK TIQEELGGVS QEEEMDEMGQ KAKTKKWDEK
TQKHFEKELS KMRRMNPQSP DFGIQRNYLE LFLELPWGEY SKDKFDLKHA QKVLDKDHFG
LDEVKKRMIE HLAVLKLRND MKSPIICLTG PPGVGKTSIG RSVAEALGRE YVRISLGGLR
DEAEIRGHRK TYIGAMPGRI IQSLKKAGTS NPVFILDEID KLSSGNSGDP SSALLEVLDP
EQNNAFYDNF LEMGYDLSKV MFIATSNNMA AIQPALRDRM EVIKMSGYTI EEKVEIAKRH
LFPKQLEAHG LTSKDLTIGK KQLEKIVEGY TRESGVRNLE TKIAQVIRNA AKAVAMEEEY
NKKVTDEDIV KVLGVPRLER DKYENNDVAG VVTGLAWTSV GGDILFIESL ISEGKGALTI
TGNLGNVMKE SATIALEYIK ANAKKLGLAI ELFQKYNIHL HVPEGATPKD GPSAGIAMLT
SLVSLLTQKK VKKSLAMTGE ITLRGKVLPV GGIKEKILAA KRAGIKEIIL CHENKSDIDE
IKEEYLEGLT FHYVKEMSEV LAIALTDQNV KNAKTLK
