ID E8LMB1_SUCHY Unreviewed; 859 AA.
AC E8LMB1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE RecName: Full=Lon protease {ECO:0000256|PIRNR:PIRNR001174};
DE EC=3.4.21.53 {ECO:0000256|PIRNR:PIRNR001174};
GN Name=lon {ECO:0000313|EMBL:EFY06383.1};
GN ORFNames=HMPREF9444_01896 {ECO:0000313|EMBL:EFY06383.1};
OS Succinatimonas hippei (strain DSM 22608 / JCM 16073 / KCTC 15190 / YIT
OS 12066).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Succinivibrionaceae; Succinatimonas.
OX NCBI_TaxID=762983 {ECO:0000313|EMBL:EFY06383.1, ECO:0000313|Proteomes:UP000018458};
RN [1] {ECO:0000313|EMBL:EFY06383.1, ECO:0000313|Proteomes:UP000018458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22608 / JCM 16073 / KCTC 15190 / YIT 12066
RC {ECO:0000313|Proteomes:UP000018458};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC ProRule:PRU01122};
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000256|PIRNR:PIRNR001174}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR001174}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family.
CC {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122,
CC ECO:0000256|RuleBase:RU000591}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFY06383.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AEVO01000131; EFY06383.1; -; Genomic_DNA.
DR AlphaFoldDB; E8LMB1; -.
DR STRING; 762983.HMPREF9444_01896; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_6; -.
DR OrthoDB; 9803599at2; -.
DR Proteomes; UP000018458; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
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_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR43718; LON PROTEASE; 1.
DR PANTHER; PTHR43718:SF2; LON PROTEASE HOMOLOG, MITOCHONDRIAL; 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 PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00464; LON; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR001174};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR001174};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001174,
KW ECO:0000256|PIRSR:PIRSR001174-2};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR001174};
KW Reference proteome {ECO:0000313|Proteomes:UP000018458};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|PIRNR:PIRNR001174}.
FT DOMAIN 49..248
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 636..820
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT ACT_SITE 726
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 769
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-1,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 403..410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR001174-2"
SQ SEQUENCE 859 AA; 95630 MW; CB3443466A2F7024 CRC64;
MSEPKNTKDE ETLQDLVHKI EHLEHLVKNP GDNNKESRTG LGEQMPEEMH IIPIFGRPVM
PSQITPVQLS IDWEDVLMKV AETKSKVFAI FSIGEKPGDR DKILPEDYPP VGCAVKLLHA
KATNSEIHFI CEGIARVKIE SWTNYEKTSL AKVSYPEPSL PDPESQEAID VKAYSMALVS
SIQELLPLNP LYTEEMRQYL LRFNQNDPSL LADCAASIST GSYSELQNVL NEIEILPRLK
MSLTMIKKEL KAAKLQNKIK GSVSEKLNKR QRDYILREQL NEIQKELGIK MDDKSADAIE
FEKRMKKLSP PNYILERFNS EIKKLKVLES GSPEYAVTRN YLDVITSIPW GKMSKESIDL
KKARTILDKD HEGLKDVKDR IIEFLAIGAL KGETKGSIML FVGPPGVGKT SIGKSIAKAL
NRPFFRLSLG GVDDESVIKG HRKTYIGSMP GKMVQALRET KVMNPVIMLD EIDKLGRSYQ
GDPSAALLET LDPEQNNNFL DHYLDEKLDL SNCLFICTAN TVESIPEPLL DRMDPIRLSG
YIAKEKLLIA KKHLLPRALK QAAIRKAQLK LSDEVLLKII EEYARESGVR SLERAIAKIV
RKAAVKIVEG ENSVTITKDN LEDFLGTAPF KKEKNIKGVG VITGLAWTSV GGATLPIESV
LVNRDNKSFE LTGSLGDVMK ESAHIAYSFI QANLQRYVGK KGADFFKKGT VHLHVPEGAT
PKDGPSAGIT MASSLLSLAL NSEPKQGFAM TGELSLTGQV LAIGGIREKV IAARRMGIFN
LIVPKANAGD VKELPSEVKD GVNFYYADAY DDVAKVLFDE VKNRLDKIEN KYKPELIDLK
AEELPLKNEE KQQNEVAVS
//
