LON_SYNWW
ID LON_SYNWW Reviewed; 812 AA.
AC Q0AWF3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-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=Swol_1653;
OS Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=335541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2245B / Goettingen;
RX PubMed=21966920; DOI=10.1111/j.1462-2920.2010.02237.x;
RA Sieber J.R., Sims D.R., Han C., Kim E., Lykidis A., Lapidus A.L.,
RA McDonnald E., Rohlin L., Culley D.E., Gunsalus R., McInerney M.J.;
RT "The genome of Syntrophomonas wolfei: new insights into syntrophic
RT metabolism and biohydrogen production.";
RL Environ. Microbiol. 12:2289-2301(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; CP000448; ABI68951.1; -; Genomic_DNA.
DR RefSeq; WP_011641049.1; NC_008346.1.
DR AlphaFoldDB; Q0AWF3; -.
DR SMR; Q0AWF3; -.
DR STRING; 335541.Swol_1653; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; ABI68951; ABI68951; Swol_1653.
DR KEGG; swo:Swol_1653; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_9; -.
DR OMA; GAWQVVD; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000001968; 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..812
FT /note="Lon protease"
FT /id="PRO_0000396607"
FT DOMAIN 12..203
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 593..774
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 680
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 723
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 357..364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 812 AA; 91461 MW; B783693ECB5289CB CRC64;
MPTEEHQTYR ELPMLPLRGV LVFPYTVIHL DVGRKKSINA IEDAMLGSKE IFLATQKEAQ
TDEPDEEDIY EVGTVAEIRQ ILKMPGGTMR VLVEGLFRAE INAYLANDPY MKVRVEELRD
KKIKSPELEA LMRNLVGQFE QYVRMSKKIP PETVVSVVAI EEGGRLADVI ASHLNLRINE
KQRILELSDI NKRLNYLCEL LAKEMEVLEL ERKINIRVRK QMEKTQKEYY LREQIKAIQK
ELGEKDERSS EVEEFRERIK KANMPKDAEE KAFKELERLE KMPPMVAEAV VVRNYLDWIL
SLPWSLETRD RLDLKAAEAI LDEDHYGLEK PKERILEYLA IRKLAKKMKG PILCLVGPPG
VGKTSLGKSV GRSLGRKFIR MSLGGIRDEA EIRGHRRTYV GSMPGRILQG MKTAGSKNPV
FLLDEIDKMT MDFRGDPASA LLEVLDPEQN YIFSDHYLEI PFDLSKVMFI TTANSVFNIP
RPLLDRMEII EITGYTEEDK VHIATDYLVP KQIKEHGLKE SNITFSEGTL RRIIREYTRE
AGVRNLERQI ASICRKVARQ VVEDKDTFVH VASNSLNRFL GAGRYRYGVA ESENQVGVAT
GLAWTESGGD ILSIEVALLK GKGNLTLTGK LGEVMKESAQ AALTYVRSKA DELGINDEIR
DKYDVHIHIP EGAIPKDGPS AGITLATALA SAMSGLPVRS DVAMTGEITL RGRILPIGGV
KEKILAAHRA GIAKVLLPVE NKKDLAEIPA PVKRKIKLVL VSHMDEVLEE TLLKLEAIQP
GEDFPGVLLN PELVGENLNQ DRVEPEANKD LC
