LON_HAEIN
ID LON_HAEIN Reviewed; 803 AA.
AC P43864;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 143.
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}; Synonyms=lon-A;
GN OrderedLocusNames=HI_0462;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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.
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; L42023; AAC22121.1; -; Genomic_DNA.
DR PIR; A64070; A64070.
DR RefSeq; NP_438623.1; NC_000907.1.
DR RefSeq; WP_005693703.1; NC_000907.1.
DR AlphaFoldDB; P43864; -.
DR SMR; P43864; -.
DR STRING; 71421.HI_0462; -.
DR MEROPS; S16.001; -.
DR PRIDE; P43864; -.
DR EnsemblBacteria; AAC22121; AAC22121; HI_0462.
DR KEGG; hin:HI_0462; -.
DR PATRIC; fig|71421.8.peg.482; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_6; -.
DR OMA; GAWQVVD; -.
DR PhylomeDB; P43864; -.
DR BioCyc; HINF71421:G1GJ1-478-MON; -.
DR Proteomes; UP000000579; 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..803
FT /note="Lon protease"
FT /id="PRO_0000076136"
FT DOMAIN 9..200
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 592..773
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 679
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 722
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 803 AA; 89347 MW; 9E590852611EEA5B CRC64;
MAKNTQRTMP VLPLRDVVVF PYMVMPLFVG RAKSINALEE AMNDDKQILL VSQREADLEE
PTPEDLFDVG TIANIIQLLK LPDDTVKVLV EGQNRAKINS LEDGEKCFSA QITPIETTYG
DEKELVVAKS AVLSEFENYL TLNKKVPTDI LNALQRIDDV DRLADTMAAH LPVSIRHKQN
ALELANVQER LEYLLGMMES EADILQVEKR IRGRVKKQME KSQRNYYLNE QIKAIRKEMD
GGENEDTIDE VEQLHQKVEA AGMPADVRDK VENELQKLKM MSAMSSEATV IRSYIEWMIQ
VPWHQRSKVK KDIVKAQQVL DTDHYGLDRV KERILEYLAV QARLNKVKGP ILCLVGPPGV
GKTSLGQSIA NATGRKYVRM ALGGVRDEAE IRGHRKTYIG ALPGKLIQKM AKVGVKNPLF
LLDEIDKMAS DMRGDPASAL LEVLDPEQNT TFNDHYLEVD YDLSDVMFVA TSNSMNIPGP
LLDRMEVIRL SGYTEDEKLN IAMRHLLAKQ IERNGLKKGE LTVEESAILD IIRYYTREAG
VRGLEREISK ICRKAVKNLL VNPKLKSITV NSDNLHDYLG VKRFEFGKAD TQNRIGEVTG
LAWTEVGGDL LTIETASVVG KGKLSFTGSL GDVMKESIQA AMTVVRARAD KLGINAEFHE
KRDIHIHVPD GATPKDGPSA GIAMCTALIS CLTGNPVRAD VAMTGEISLR GKVLPIGGLK
EKLLAAHRGG IKTVLIPKEN VKDLEEIPEN VKQNLAIHAV ETIDEVLGFA LENPPEGIEF
VKVEAKPKAP RRKVTSKSER AVN
