LON3_SORC5
ID LON3_SORC5 Reviewed; 830 AA.
AC A9GIS9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Lon protease 3 {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 3 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon3 {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=sce3149;
OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS ce56)).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC Polyangiaceae; Sorangium.
OX NCBI_TaxID=448385;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=So ce56;
RX PubMed=17965706; DOI=10.1038/nbt1354;
RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA Puehler A., Mueller R.;
RT "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL Nat. Biotechnol. 25:1281-1289(2007).
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; AM746676; CAN93308.1; -; Genomic_DNA.
DR RefSeq; WP_012235780.1; NC_010162.1.
DR AlphaFoldDB; A9GIS9; -.
DR SMR; A9GIS9; -.
DR STRING; 448385.sce3149; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; CAN93308; CAN93308; sce3149.
DR KEGG; scl:sce3149; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_7; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR BioCyc; SCEL448385:SCE_RS16135-MON; -.
DR Proteomes; UP000002139; 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..830
FT /note="Lon protease 3"
FT /id="PRO_0000396602"
FT DOMAIN 19..211
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 604..784
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 811..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 690
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 733
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 367..374
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 830 AA; 92887 MW; 3C29658402B334A8 CRC64;
MFFKNDSDRG KNAPERGIVP LLPLRDIIVF PHMVSQLFVG RERSIAALDE AMNRGKEIFL
AAQRNAKTND PTPDDIFGVG SVGAIMQLLR LPDGTVKVLI EGKRRARIRR YVQSDAYFLI
EYDEIVESSV ASVEVEALMR SVQSTFEMYV KLNKKIQPEV LMAVQAIDEA SRLADTIIAN
LPTIKLTDRQ ALLEMEEPQK RLERLIELMQ AEIEILQVEK KIRSRVKKQM EKTQKEYYLN
EQMQAIQKEL GGGERDEFKN EIQEIEEALK TKRMSKEAAA KVKKELKKLK MMHPTSAEAT
VVRNYIDWIL ELPWYDKSEE RYDLVEAERI LDEDHYGLKK IKERILEYLA VQALTKKLKG
PVLCFVGPPG VGKTSLAKSI ARATGRKFVR LSLGGVRDEA EIRGHRRTYI GALPGKLIQS
LKKVGTNNPV FLLDEVDKMS TDFRGDPAAA LLEVLDPEQN HTFNDHYLDL DYDLSDVMFI
TTANTLSGIP VPLQDRMEVI QLSGYTEFEK LNIAVKYLVP RQRKECGLED VSLDFTEGAL
RTIIHHYTKE SGVRSLEREI ASVCRKVARR VVSDGKEKPI EVVAKSIPKY LGVPKYRLGR
REERDEVGLV NGLAVTNVGG DLLPAEATVV PGKGKLVITG LLEKGMEESG HAAMSYVRSR
LDRLGLEADV YQKVDVHIHF PDFVRKDGPS AGVTMVTALV SSLMKVPVRR DLAMTGEITL
RGRVMPIGGL KEKLLAAHRG GIATVILPKE NRKDLRDVPR RVLKALRLVL VEHVDDVLRE
ALILPDAYAI FGPPKGVLEY RDGELVTEAA PVKAPPAAAG EPTPAAPPGA
