LON_SULSY
ID LON_SULSY Reviewed; 800 AA.
AC B2V6N0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
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};
GN OrderedLocusNames=SYO3AOP1_0116;
OS Sulfurihydrogenibium sp. (strain YO3AOP1).
OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC Sulfurihydrogenibium; unclassified Sulfurihydrogenibium.
OX NCBI_TaxID=436114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YO3AOP1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(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; CP001080; ACD65762.1; -; Genomic_DNA.
DR RefSeq; WP_012458854.1; NC_010730.1.
DR AlphaFoldDB; B2V6N0; -.
DR SMR; B2V6N0; -.
DR STRING; 436114.SYO3AOP1_0116; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; ACD65762; ACD65762; SYO3AOP1_0116.
DR KEGG; sul:SYO3AOP1_0116; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_0; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
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..800
FT /note="Lon protease"
FT /id="PRO_0000396604"
FT DOMAIN 17..210
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 606..788
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 693
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 736
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 370..377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 800 AA; 90763 MW; A11DC2979F1F4FA9 CRC64;
MGPFEDKLDL LELPSTYPLI PTRDVIVFPY MVFPLFIGRP FSIKAVEEAL DNNQRYIFLS
LQKDKEKEIP TKKDIHEIGV VATIIRMMKL EDNRIKILVQ GVSRGRIKEL KKVDDYYQVG
VEIIEDPEVE ETLEVQALKH SLKDLLDKAI SLGKQIVPDL VEIIKSVEEP GRLADLVASI
LDIKAEEAQQ ILEILDPVER LRVVHDKFLK EVGILELQQK IRISAREAIE KDQREYFLRQ
QIKAIQEELG ERDEKQEEIE NYKKKIEESG MPDEIKEEAL KQLKRLEKMH PDSAEAGVIR
TYLDWLVELP WNKRTKDRLD LKIAKKILDE DHYDLEKIKE RILEYLAVLK LKKESSKDKS
IKGPILCFVG PPGVGKTSLG RSIAKALNRK FVRISLGGVR DEAEIRGHRR TYVGAMPGKI
IQAIKQARTK NPVIMLDEVD KIGLDFRGDP TAALLEVLDP EQNKEFIDHY LGVPFDLSEV
MFICTANRLD TIPRPLLDRM EVIRLSGYSE EEKLHIAKKY LIPKQLKENG LDEKTVEFSD
KAITFLIRGY TREAGVRNLE RQIGSIIRKI AKKIIETGKK RKYKITPSLI KKFLGAPIYS
TEKEEKDEVG VVTGLAWTEV GGEILKIEVT KMDGKGNLVL TGSLGDVMKE SARIAFSYVK
SKAKELGIDP EEFGKYDLHI HVPAGAIPKD GPSAGIAITT GIASVFTNRP VRSDVAMTGE
ITLRGKVLPV GGLKEKILAA KRAGIKTVIL PKDNKEEVMS DLPPYVRKSM NLIFVDHIDE
VFKIALREEK KEVENQESES
