LON_FINM2
ID LON_FINM2 Reviewed; 776 AA.
AC B0S2N4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=FMG_1206;
OS Finegoldia magna (strain ATCC 29328 / DSM 20472 / WAL 2508)
OS (Peptostreptococcus magnus).
OC Bacteria; Firmicutes; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Finegoldia.
OX NCBI_TaxID=334413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29328 / DSM 20472 / WAL 2508;
RX PubMed=18263572; DOI=10.1093/dnares/dsm030;
RA Goto T., Yamashita A., Hirakawa H., Matsutani M., Todo K., Ohshima K.,
RA Toh H., Miyamoto K., Kuhara S., Hattori M., Shimizu T., Akimoto S.;
RT "Complete genome sequence of Finegoldia magna, an anaerobic opportunistic
RT pathogen.";
RL DNA Res. 15:39-47(2008).
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; AP008971; BAG08624.1; -; Genomic_DNA.
DR RefSeq; WP_002839518.1; NC_010376.1.
DR AlphaFoldDB; B0S2N4; -.
DR SMR; B0S2N4; -.
DR STRING; 334413.FMG_1206; -.
DR MEROPS; S16.001; -.
DR PRIDE; B0S2N4; -.
DR EnsemblBacteria; BAG08624; BAG08624; FMG_1206.
DR KEGG; fma:FMG_1206; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_9; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000001319; 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..776
FT /note="Lon protease"
FT /id="PRO_0000396564"
FT DOMAIN 12..207
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 596..776
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 683
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 726
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 360..367
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 776 AA; 87866 MW; BC677B9C16222023 CRC64;
MKEYYTISEK KLPIIALRGL WLFPNNIQHF EVGREVSLNA LNASLLRNSE IFICTQKDPM
LENITKEDFY HTGVLASIKQ TIKMPNGNIR VLVEAYDRAK IVDFVENDSF LEANVEVMEY
DKTKYHPTDK SLTMIRMIIS SFESLAEIIK KPLPQDLLGG LLNEEDPSSL IDTIAMLISL
NDKDSILLLE TLDMDERIEL VYKFVIKEIE FLKIKEDIEE RTNKEISDTQ KEYFLQEQLR
QIKMELGEEY DIEDTDDYAN RVKKLKLKKD SEEHVLKEIN RLSSMNPNNP ESTVIRNYID
QVLDIPWNKK SKSSIDLKVA EKVLNDGHFG LEDVKKRILE YLAVKKMTGS LKGPILCLVG
PPGVGKTSIA RSIADATNRK FVSMRLGGVR DEAEIRGHRK TYIGAMPGRI ITQLQKAKKL
NPVFLLDEID KLASDFRGDP ASALLEVLDP EQNSEFTDNY IEIPVDLSDV LFITTANSQE
QIPDALLDRM EVIRVTSYTD SEKFEIANRY LLPRQLKENG MDKSQFHITR DAIYTIINNY
TRESGVRELE RNIGKVIRKA VVKIVKDDVK KVVVNNKNLE KFLGSKLVLD DEIPREDTVG
VVNGLAWTQV GGVILTIEAN VMDGSGKTQL TGKLGDVMKE SAMAAISYIR SNQEALGIKG
EFYKEKDIHI HVPEGAVPKD GPSAGVTMVT ALVSALTGRK VKHDFAMTGE ITLTGRVLAI
GGVKEKVLAA HRYGINKVFL PKENKRDIQD IDPKIRQKIK FYFTSNVKEI LDEVLI
