LON_SULMW
ID LON_SULMW Reviewed; 855 AA.
AC A8Z5Z0;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=SMGWSS_129;
OS Sulcia muelleri (strain GWSS).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Candidatus Sulcia.
OX NCBI_TaxID=444179;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GWSS;
RX PubMed=18048332; DOI=10.1073/pnas.0708855104;
RA McCutcheon J.P., Moran N.A.;
RT "Parallel genomic evolution and metabolic interdependence in an ancient
RT symbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19392-19397(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; CP000770; ABS30541.1; -; Genomic_DNA.
DR AlphaFoldDB; A8Z5Z0; -.
DR SMR; A8Z5Z0; -.
DR STRING; 444179.SMGWSS_129; -.
DR PRIDE; A8Z5Z0; -.
DR EnsemblBacteria; ABS30541; ABS30541; SMGWSS_129.
DR KEGG; smg:SMGWSS_129; -.
DR HOGENOM; CLU_004109_4_3_10; -.
DR OMA; GAWQVVD; -.
DR Proteomes; UP000000781; 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..855
FT /note="Lon protease"
FT /id="PRO_0000396603"
FT DOMAIN 45..286
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 674..855
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 761
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 804
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 439..446
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 855 AA; 98939 MW; 33A704AAD507BBA5 CRC64;
MLLHETESEY DSKSKKNNYS YYESSDFKPL IEKYNRIKYS VTEYIYLLTV KNVVLFPDVV
IPITAVKQKS INLFKSAYYT YKKIGILTKK YFNTTFSIAK LNIQTFNIYS FNKFNKINKF
NKINKFNKIN KFNKINKFNK INKFNKTNNI YYIGTVAKIL KLLIMPDGNT TVILQGISRF
KIIKLIQVYP YFKAEIIYLK DEKPQKKDKE YLILIDSIKE IAIKIIQDNY KIPSESSFAI
SNIESKSFLI NFVAYNLNIE IKNKQILLEY DFLKQRAIET FRFLNIEYEK IKLKNDIQYR
VRYDIDQQQK EYFLNQQIKA LQEELGDFSY EKEVEVLRIK SYKKNWSKEA QNQFDRELSK
LKRTNPQMPE YTILRNYLDL MLDLPWKKYS QDNYDLYRAQ KILDKDHFGI DKVKERIIEY
LSVLKLKGDL RSPILCFYGP PGVGKTSLGR SIASALNRKY VRISLGGLND EAEIRGHRKT
YIGAMPGRVL QSIKKAGTSN PVFVLDEIDK MGLGSQGNPS SAMLEVLDPE QNKEFYDNFL
EMGYDLSKVI FIATANSLYT INIALLDRME IIDMNGYTVE EKIEISKKHL IPKQLKENGL
KSKDIILGVK QIEKIIESYT RESGVRSLEK NISKIVRYAA KNIAMNKKYL KRINMSKIEE
VLGPPNDPEK YELIQVPGVV TGLAWTIVGG EIIYIESTLL KGRGNLSITG NVGEVMKESA
TIAFKYIKAH NYEFGIDEKM FELYNIHIHA PEGGIHKDGP SAGITMLTSI ISSFLKKKIR
PYLAMTGEIT LRGKVLPVGG IKEKILAAKR ANIKEIILSK ANKKDIDDIK KVYLKGLKFH
FVSKMNEVID LSIIK
