LON_AMOA5
ID LON_AMOA5 Reviewed; 827 AA.
AC B3ERM8;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Aasi_0470;
OS Amoebophilus asiaticus (strain 5a2).
OC Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Amoebophilaceae;
OC Candidatus Amoebophilus.
OX NCBI_TaxID=452471;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=5a2;
RX PubMed=20023027; DOI=10.1128/jb.01379-09;
RA Schmitz-Esser S., Tischler P., Arnold R., Montanaro J., Wagner M.,
RA Rattei T., Horn M.;
RT "The genome of the amoeba symbiont 'Candidatus Amoebophilus asiaticus'
RT reveals common mechanisms for host cell interaction among amoeba-associated
RT bacteria.";
RL J. Bacteriol. 192:1045-1057(2010).
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; CP001102; ACE05880.1; -; Genomic_DNA.
DR RefSeq; WP_012472643.1; NC_010830.1.
DR AlphaFoldDB; B3ERM8; -.
DR SMR; B3ERM8; -.
DR STRING; 452471.Aasi_0470; -.
DR EnsemblBacteria; ACE05880; ACE05880; Aasi_0470.
DR KEGG; aas:Aasi_0470; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_10; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000001227; 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..827
FT /note="Lon protease"
FT /id="PRO_0000396532"
FT DOMAIN 38..231
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 619..800
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 706
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 749
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 384..391
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 827 AA; 92880 MW; 5E820E5DABD5AECF CRC64;
MFKNMTLLGT LIEHSDGLPL LETNMKNMHK DHNQDASLTL LASKYNVLFP GIYMPMTLEN
ASIIRLVKKV YETGGIIGIV AQKKEDVEAT SAQDIFTIGT TARILKLINL PDERVRILLQ
GEEKFQIEDV IAETPYLLAS ISRLKDKTSN TQSKHFKAVV SSIKETVAKL ISLQPEFPTE
IKLLLDNIND FNLLTYFLAS GLDTDIKSKQ KLLEIHDSKK RGTVLLKYLL KDLEVSKLRK
KIQDKVHTDI EQLQHDFYIR RQIKVLQEEL GENEFEDEID ELRAEGEKKQ WPKEVADYFY
KALDKAERLS PNSADYPVLI SHAELMLELP WSVYTTDNMD LKMAKKVLDT EHYGLEKVKE
RLLEYLAVRK LTQNMKGPIL CLYGPPGVGK TSLGKSIAKA LNRKYVKVSL GGLHDEAEIR
GHRKTYVGAM PGRIIKGIQN SGSSNPVFML DELDKITDLR GDPAAALLEV LDPEQNQAFV
DTFLEVPYDL SKVLFIATAN QLDTIPPALR DRLEIIEING YTIEEKLQIA KKYLFPKQRK
ENGLKATDLS IHDTAIVKVI ESYTRESGVR ELDRKLASLV RKVGKAMVLE EPYPKKIHKE
DVISLLGIEL FDQEMYQQTH LPGVAIGLAW TPVGGDILFI EAILSAGKGK LTLSGQLGDV
MKESAMTAFT YLKANTNLLG IPDKVFESYD LHIHLPAGAV PKDGPSAGIT LFAALASLYT
QRKVKDKVAM TGEITLRGKV LPVGGIKEKI LAAKRAGIKE VILSKENKKD IQEIKQKDIQ
DLKFHYVEFV EEVIQLALQP SKVEAAKDWS ITKKRKQQPG IGHVSTL
