LON_RHIME
ID LON_RHIME Reviewed; 806 AA.
AC O69177;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 138.
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=R01257;
GN ORFNames=SMc01905;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10762258; DOI=10.1128/jb.182.9.2551-2558.2000;
RA Summers M.L., Botero L.M., Busse S.C., McDermott T.R.;
RT "The Sinorhizobium meliloti lon protease is involved in regulating
RT exopolysaccharide synthesis and is required for nodulation of alfalfa.";
RL J. Bacteriol. 182:2551-2558(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-359.
RC STRAIN=CL375B;
RA Biondi E., Fancelli S., Bazzicalupo M.;
RT "Partial coding sequence of Sinorhizobium meliloti lon gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). In R.meliloti it is important for
CC controlling the turnover of a constitutively expressed protein(s) that,
CC when unregulated, disrupts normal nodule formation and normal growth.
CC {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; AF167159; AAF05300.1; -; Genomic_DNA.
DR EMBL; AL591688; CAC45836.1; -; Genomic_DNA.
DR EMBL; AF065445; AAC17128.1; -; Genomic_DNA.
DR RefSeq; NP_385363.1; NC_003047.1.
DR RefSeq; WP_003531808.1; NC_003047.1.
DR AlphaFoldDB; O69177; -.
DR SMR; O69177; -.
DR STRING; 266834.SMc01905; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; CAC45836; CAC45836; SMc01905.
DR GeneID; 61602715; -.
DR KEGG; sme:SMc01905; -.
DR PATRIC; fig|266834.11.peg.2671; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_5; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000001976; 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..806
FT /note="Lon protease"
FT /id="PRO_0000076144"
FT DOMAIN 14..205
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 594..775
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 786..806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 681
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 724
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 359..366
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT CONFLICT 103..126
FT /note="IERYTPRDDFYEAMAHALPEPDED -> TNAIRRVTIFTRPWPMHCPNRTRY
FT (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="L -> F (in Ref. 1; AAF05300)"
FT /evidence="ECO:0000305"
FT CONFLICT 353..359
FT /note="PILCLVG -> RSLLVVS (in Ref. 4; AAC17128)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="L -> F (in Ref. 1; AAF05300)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="I -> F (in Ref. 1; AAF05300)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="D -> E (in Ref. 1; AAF05300)"
FT /evidence="ECO:0000305"
FT CONFLICT 502
FT /note="R -> L (in Ref. 1; AAF05300)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="P -> T (in Ref. 1; AAF05300)"
FT /evidence="ECO:0000305"
FT CONFLICT 532..534
FT /note="MAV -> TAI (in Ref. 1; AAF05300)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="T -> S (in Ref. 1; AAF05300)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="H -> N (in Ref. 1; AAF05300)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="L -> I (in Ref. 1; AAF05300)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="L -> F (in Ref. 1; AAF05300)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 806 AA; 89458 MW; 4A984D1676072A00 CRC64;
MTNKTSPATE SATYPVLPLR DIVVFPHMIV PLFVGREKSI RALEEVMGTD KQIMLVTQIN
ATDDDPEPSA IYKVGTIANV LQLLKLPDGT VKVLVEGRSR AEIERYTPRD DFYEAMAHAL
PEPDEDPVEI EALSRSVVSE FESYVKLNKK ISPEVVGVAS QIEDYSKLAD TVASHLSIKI
VEKQEMLETT SVKMRLEKAL GFMEGEISVL QVEKRIRSRV KRQMEKTQRE YYLNEQMKAI
QKELGDSEDG RDEMAELEER ISKTKLSKEA REKADAELKK LRQMSPMSAE ATVVRNYLDW
LLGLPWGKKS KIKTDLNHAE KVLDTDHFGL DKVKERIVEY LAVQARSSKI KGPILCLVGP
PGVGKTSLAK SIAKATGREY IRMALGGVRD EAEIRGHRRT YIGSMPGKVV QSMKKAKKSN
PLFLLDEIDK MGQDFRGDPS SALLEVLDPE QNSTFMDHYL EVEYDLSNVM FITTANTLNI
PPPLMDRMEV IRIAGYTEDE KREIAKRHLL PKAIRDHALQ PNEFSVTDGA LMAVIQNYTR
EAGVRNFERE LMKLARKAVT EILKGKTKKV EVTAENIHDY LGVPRFRHGE AERDDQVGVV
TGLAWTEVGG ELLTIEGVMM PGKGRMTVTG NLRDVMKESI SAAASYVRSR AIDFGIEPPL
FDKRDIHVHV PEGATPKDGP SAGVAMATAI VSVMTGIPIS KDVAMTGEIT LRGRVLPIGG
LKEKLLAALR GGIKKVLIPE ENAKDLADIP DNVKNSLEII PVSRMGEVIA HALLRLPEPI
EWDPASQPAA LPSVDSQDEA GTSIAH
