LON_DESAL
ID LON_DESAL Reviewed; 826 AA.
AC B8F9K1;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Dalk_1244;
OS Desulfatibacillum aliphaticivorans.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfatibacillum.
OX NCBI_TaxID=218208;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK-01;
RX PubMed=21651686; DOI=10.1111/j.1462-2920.2011.02516.x;
RA Callaghan A.V., Morris B.E., Pereira I.A., McInerney M.J., Austin R.N.,
RA Groves J.T., Kukor J.J., Suflita J.M., Young L.Y., Zylstra G.J., Wawrik B.;
RT "The genome sequence of Desulfatibacillum alkenivorans AK-01: a blueprint
RT for anaerobic alkane oxidation.";
RL Environ. Microbiol. 14:101-113(2012).
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; CP001322; ACL02947.1; -; Genomic_DNA.
DR RefSeq; WP_012610383.1; NC_011768.1.
DR AlphaFoldDB; B8F9K1; -.
DR SMR; B8F9K1; -.
DR MEROPS; S16.001; -.
DR PRIDE; B8F9K1; -.
DR EnsemblBacteria; ACL02947; ACL02947; Dalk_1244.
DR KEGG; dal:Dalk_1244; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_7; -.
DR OMA; KKMNPVM; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000000739; 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..826
FT /note="Lon protease"
FT /id="PRO_0000396553"
FT DOMAIN 26..219
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 609..790
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 788..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..814
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 696
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 739
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 373..380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 826 AA; 92194 MW; FF54000CEBD36C98 CRC64;
MAHTDTDDLV GLLDADDQNL DIPATLPMLP VRDVVVFTHM IIPLFVGRDK SVRAVDAAMA
KDRFLFLATQ MDGAVENPES DQIFKHGTAA RILRVLKLPD GRVKVLVQGL AKAKIVRYTK
KSDMFRVRIE LLHEEDLGDL DMETEALMRN VKESCEKILG LRGELTPDVT MVLDGIDHPG
RLADLVASNL NLKIEEAQSI FETIDPVQRL LAVNGFVSRE VELSAMQARI QSSVRDEISK
SQKDYFLREQ MRAINRELGE MDEKTQEIKE YQDKIRKAKM PKEAKEEAER QLKRLEQMHP
EAGEAPTVRT YLDWLVEVPW KKATKDTLDI KKAKEILEED HYGLEKVKDR ILEYLAVRKL
NPKMKGPILC FVGPPGVGKT SLGKSIARAM GRKFYRLSLG GIRDEAEIRG HRRTYIGALP
GRIIQGLKHC KSNNPVFMMD EIDKIGADFR GDPSSALLEA LDPEQNFAFS DHYLNVPFDL
SSVMFITTAN MTDTIPSALL DRMEVINLAG YTENEKVLIA QQYLVPRQVK ENGLKPEDIT
ISGNALLKMA TEYTSESGLR NLEREIGTLC RKVSRKIAEG KKGPYQITAS SLVKYLGLEK
FLPEMDQEEP QIGLATGLAW THWGGEALYI ETTLMRGKGE LVLTGQLGEV MQESARAALS
YARTNEDELE IDPDLFDNFD IHIHVPAGAI PKDGPSAGIA MTTALVSALT ERPVANDIAM
TGEVTIRGRV LPIGGLREKS LGALRAGIKT IIIPEKNKKE LSEVPQQVRR KLKYITVSHV
NEVLEKALLP AEKKKAPPKK KPPKKAAKPK AKKTQPKAKT TEAADK
