LON_MAGMM
ID LON_MAGMM Reviewed; 809 AA.
AC A0L516;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Mmc1_0534;
OS Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC Magnetococcaceae; Magnetococcus.
OX NCBI_TaxID=156889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX PubMed=19465526; DOI=10.1128/aem.02874-08;
RA Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT coccus strain MC-1.";
RL Appl. Environ. Microbiol. 75:4835-4852(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; CP000471; ABK43059.1; -; Genomic_DNA.
DR RefSeq; WP_011712226.1; NC_008576.1.
DR AlphaFoldDB; A0L516; -.
DR SMR; A0L516; -.
DR STRING; 156889.Mmc1_0534; -.
DR EnsemblBacteria; ABK43059; ABK43059; Mmc1_0534.
DR KEGG; mgm:Mmc1_0534; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_5; -.
DR OMA; VLDCVPM; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000002586; 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; PTHR43718; PTHR43718; 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..809
FT /note="Lon protease"
FT /id="PRO_0000396578"
FT DOMAIN 42..240
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 629..809
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 716
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 759
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 395..402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 809 AA; 89847 MW; CB76FC109A871089 CRC64;
MSEQRSDEPE VVDAIIEDQQ GAQATTDATP PVRIENSLPT ELVIYPLGGR PFFPGMLTPI
QVEGSPYYET IKKAMDSHGR LFGILASHAE DGQEVFDANQ LFGIGTVVRI LEASVNEEAK
QIKLLAEGLW RFEVRDVVSV GPPIVAQVTH HNNPVSVVDT DALKPYTMAV INTLKEILKY
DSLYQEQVKM FLSRHNFSEP DRLADFVASM TSSSREELQE VLETLPIMAR LEKVLTLLKK
ELEVVKLQNK IQRQVEEGIA EHQRQFFLRE QLKEIQKELG ITKDDRTAEI DRFRERLEKL
TLSEEAEQKI EEELDKLAIL ETGSSEYGVT RNYVDWLTSL PWGVHSTDKL NIARARRILD
RDHDGLEDVK ERILEFLAVG KLKGEIGGSI ILLVGPPGVG KTSIGRSVAT AVGREFYRFS
VGGMRDEAEI KGHRRTYVGA MPGKFVQAIK HTKVANPLIM LDEVDKIGAS YQGDPASALL
EVLDPEQNSE FLDHYMDVRF DLSKVLFICT ANQLDTIPRP LLDRMEVIRL SGYITSEKVR
IARNHLLPKQ LEKNGLDKSQ LRVSNGALRE IIEGYAREAG VRRLEQKIGA IARKVAVKVL
EEAELPISVG QNDLDSYLGK PDFREEKPLT GVGIVTGLAW TALGGATLDI ESAQTSTEGN
TLLLTGQLGD VMKESARIAF SFLQSNVEKL GGKSERLKGN IHLHVPEGAT PKDGPSAGIT
IATALLSLAR TQPLPRRLAM TGEITLTGSV LAVGGVREKV IAARRVGIRE LIIPEACRKD
YDEVPEHIRE GFTVHFVKKY AEVAKLVFG
