ID   LON_DESVH               Reviewed;         821 AA.
AC   Q72CE6;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 133.
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=DVU_1337;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
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; AE017285; AAS95815.1; -; Genomic_DNA.
DR   RefSeq; WP_010938632.1; NC_002937.3.
DR   RefSeq; YP_010556.1; NC_002937.3.
DR   AlphaFoldDB; Q72CE6; -.
DR   SMR; Q72CE6; -.
DR   IntAct; Q72CE6; 4.
DR   STRING; 882.DVU_1337; -.
DR   MEROPS; S16.001; -.
DR   PaxDb; Q72CE6; -.
DR   PRIDE; Q72CE6; -.
DR   EnsemblBacteria; AAS95815; AAS95815; DVU_1337.
DR   KEGG; dvu:DVU_1337; -.
DR   PATRIC; fig|882.5.peg.1248; -.
DR   eggNOG; COG0466; Bacteria.
DR   HOGENOM; CLU_004109_4_3_7; -.
DR   OMA; GAWQVVD; -.
DR   PhylomeDB; Q72CE6; -.
DR   Proteomes; UP000002194; 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..821
FT                   /note="Lon protease"
FT                   /id="PRO_0000396559"
FT   DOMAIN          18..214
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT   DOMAIN          606..787
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         368..375
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ   SEQUENCE   821 AA;  91617 MW;  32FD4CB70B0ABF1E CRC64;
     MTDTGREGLQ NREEGFELPL MSLREVVMFP RSIVPLFVGR EASIKAIESA ISDYGKKIFL
     VAQREPELEK PGPEDLFEVG TVSKILQLLR LPDGTIKVLF EGLYRARWDG TADAIIGADD
     AYPRVRVTRI EQESSEDDDE ALVRATHEAL DEYGKINKKL AQETLVAISA LSDAARLADA
     IMPHLKVDYR RKQELLEVES GAERLEKVYE LLQGEIAVAS LEKRIKSRVK NQMERNQREY
     YLNEQIKAIH KEMGREDDPQ AEVNELEARL AEKSMPEEAR EKALREMKKL RQMPPSSAEY
     TVVRNYVDWI LDLPWNTLKE TEIDIDNARS ILDADHYGLE KPKERILEYL AVQKLVNRLK
     GPILCLVGPP GVGKTSLAKS VAKATGREFV RLSLGGVRDE AEIRGHRRTY VGALPGKIIQ
     SLKRVKHNNP LFCLDEIDKM STDFRGDPSS ALLEVLDPEQ NSTFNDHYLD MDYDLSQVFF
     ITTANSLHSI PLPLQDRMEI IRLPGYLETE KRRIAHDFLL PKQVEAHGLA ASNLRISDNA
     VLEIIRSYTR EAGVRNLERE IASVCRKAAM QVVEAGDKEK TLTVSRQNLG NFLGVKKYRH
     GEREDTSQVG VCTGLAWTEM GGELLVVETA LMPGSGRVEI TGKLGDVMTE SAKAALSYLR
     SRSDLFGLRP DFHKEIDIHV HVPEGATPKD GPSAGITLAT SMVSALLGIP VRNDVAMTGE
     ITLRGRVLPI GGLREKLLAA HRGQIGKVLV PRENEKDLKE VPGEILKGLE IVFVDHVDEV
     LPQALMAQAE SIFGGRTQST PLYAKLRKDA QDGGATMPTA Q