LON_SYNAS
ID LON_SYNAS Reviewed; 790 AA.
AC Q2LVS9;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=SYNAS_23100;
GN ORFNames=SYN_00783;
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB;
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(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; CP000252; ABC78189.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2LVS9; -.
DR SMR; Q2LVS9; -.
DR STRING; 56780.SYN_00783; -.
DR EnsemblBacteria; ABC78189; ABC78189; SYN_00783.
DR KEGG; sat:SYN_00783; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_7; -.
DR OMA; MVNIEDK; -.
DR Proteomes; UP000001933; 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..790
FT /note="Lon protease"
FT /id="PRO_0000396608"
FT DOMAIN 23..218
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 608..789
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 695
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 738
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 372..379
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 790 AA; 88439 MW; 8D45E5ABEE381660 CRC64;
MEVPMPESTI NEDSKIFKLP EILPIMPIFH TVAFPKMMFP MDIVGNRFIQ LVDEAMAKDR
LLGLVLTRKA PSAEGPLCQC EDLHRVGTCV SILKLAKQAG EKAQLVVQGL ARFRIVEFLE
EEPYIQARVE KIEADILIKD LEIEALMANL STLFDRVIKL SPFLPQEFAA MAKSIQEPGD
LADIIASIVN ASVEDKQKIL ETLDIRQRLR EITLIVNHQL EILELGSKIQ SQVQEDIDKS
QRDFYLRQQL KAIREELGES DENRVEVAEY RKKIEEKMLT EEARKEAFRE LDRMSRMHPA
SAEYSVATTY LDWITSLPWN ERTQDNQDIR QARRILDEDH YGLDKAKKRI IEYLAVRKLK
PDTKGPILCF VGPPGTGKTS LAQSIARALG RKFYRISLGG VHDEAEIRGH RRTYVGALPG
RIIQGIRRAE SSNPVFVLDE IDKVGSDFRG DPSSALLEVL DPEQNFAFMD HYLGVAFDLS
HVTFITTANI LDTIPPALRD RLEVIELPGY TQDEKLRIAE RYLIPRQREA NGLTPEQIKF
TRGAARLIIS GYTREAGVRN LEREIAAVCR GVASQIAEGE ISSALISARD IHRYLGPVRM
ISDARERISK PGIAMGLAWT PTGGDLLFVE ATAMKGRKGL TLTGQLGEVM KESASAALSF
IRSNAVKIGI PVDFFEETDI HIHVPAGAIP KDGPSAGVTM LAALASLLTN RTVKNDLAMT
GEITLRGLVL PVGGIKEKVL AAHRAGIKTI ILPKWNRKDL EEIPSKVRKE MNFVFVNDMR
EVLNIALSRK
