LON2_SYNC1
ID LON2_SYNC1 Reviewed; 796 AA.
AC Q3A334;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Lon protease 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01973};
GN Name=lon2 {ECO:0000255|HAMAP-Rule:MF_01973}; OrderedLocusNames=Pcar_1982;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000142; ABA89223.1; -; Genomic_DNA.
DR RefSeq; WP_011341730.1; NC_007498.2.
DR AlphaFoldDB; Q3A334; -.
DR SMR; Q3A334; -.
DR STRING; 338963.Pcar_1982; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; ABA89223; ABA89223; Pcar_1982.
DR KEGG; pca:Pcar_1982; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_7; -.
DR OMA; DVMKMID; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000002534; 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..796
FT /note="Lon protease 2"
FT /id="PRO_0000396590"
FT DOMAIN 13..202
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 592..773
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 679
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 722
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 796 AA; 88582 MW; 95A2159A72901ACF CRC64;
MTGHPLDAIP PELPVYPLHD QVIFPHMSFP LFIGKEHMGL VEEALRNNRL LVVLTVLAID
PITGREQFAR VGTICRINQV LRFPEGGCKI ILEGVNRVRL ITTLQVTPFA MASVSLIPER
ENRNSVAQAL MQSIIALLRV AQSLGQMLPE DAHHAIDRID ESGKLADSLA VYLNMEVKDQ
QRLLETLDPL ERLKDVYLFL TTEIQKMQAR GGGSADRSRQ AVRSQKEHLL REQLKHIQNQ
LGEEDPHQAD IRQFRSIVQS DEMPEVVRSV AEKELARLER INPSSPEYTV ARSYVEYLCN
MPWQRGTSDI LDIDRAQQTL DDDHYDLVEV KERILEFLAV HSLKSSLKGP ILCFVGPPGV
GKTSLGRSIA RSLGRKFIRI SLGGMKDEAE IRGHRRTYIG AMPGRIIQEI CRAGANNPVF
MLDEVDKIGQ DFRGDPAAAL LEVLDPEQNY SFTDHYLDVP FDLSHVMFIT TANVMDTVPP
PLRDRMEVLR LPGYSDEEKL QIAFKYLIPK QVSENGLDKH PLQFEEQAVL KIIKNYTREA
GVRSIDRQIA SVCRKVAKAV AQGKDAPEVI RSDQVEKMLG PRKYFSDVAA EEDRVGVVTG
LAWTESGGDI IFVEVSTMAG RKDLTLTGSL GNVMQESAKT ALSYVRAHHA DFGIDAQVFE
NLDIHLHVPS GAIPKDGPSA GVTIATALIS QLTRRPARRN VAMTGELTLT GRILPIGGVK
EKVLAARRAG VTTVLLPERN RENLKELDDH ILAEMTVLLV DNLSEVVAHT LIPDTEHGPR
LFDCPQHLAV DPPSGS
