LON_GEOMG
ID LON_GEOMG Reviewed; 823 AA.
AC Q39QP7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=Gmet_3214;
OS Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=269799;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Geobacter metallireducens GS-15.";
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; CP000148; ABB33427.1; -; Genomic_DNA.
DR RefSeq; WP_004512652.1; NC_007517.1.
DR AlphaFoldDB; Q39QP7; -.
DR SMR; Q39QP7; -.
DR STRING; 269799.Gmet_3214; -.
DR MEROPS; S16.001; -.
DR EnsemblBacteria; ABB33427; ABB33427; Gmet_3214.
DR KEGG; gme:Gmet_3214; -.
DR eggNOG; COG0466; Bacteria.
DR HOGENOM; CLU_004109_4_3_7; -.
DR OMA; KKMNPVM; -.
DR OrthoDB; 128102at2; -.
DR Proteomes; UP000007073; 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..823
FT /note="Lon protease"
FT /id="PRO_0000396571"
FT DOMAIN 22..215
FT /note="Lon N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01123"
FT DOMAIN 605..786
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 788..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 692
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT ACT_SITE 735
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
FT BINDING 369..376
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01973"
SQ SEQUENCE 823 AA; 91223 MW; 92D55831BA3458FF CRC64;
MEEIEDKEPR QENEELKIPD VLPLLPVRDV VVYPYMILPL FVGREISINA VDQALSRDRL
IFLATQKEMG DEEPTPEGMY TVGTVAMIMR MLKLPDGRVK VLVQGLAKGL ITEFVESKPA
YTVRIERIVE PSVPEESLET EALMRAVKEQ LTQIVSLGKA VSPEVLVIVE NMQEPGSLAD
LIASNIGLKV DDAQALLEII DPVQRLQKVN EHLNKEHELL DMQVKIQSAA KEEMGKSQRE
YFLREQLRAI QQELGETDPR SEELNELRKA IEQAKMPPVV EKEAFKQLGR LEQMHPDAAE
AGMLRTFLDW MVELPWGKAT KDVLDIKRAR QILDEDHFYL EKIKERILEF LAVRKLRKKM
KGPILCFVGP PGVGKTSLGK SIARAMGRKF VRISLGGVRD EAEIRGHRRT YVGALPGRII
QGLKQAGSNN PVFMLDELDK LGADFRGDPS SALLEVLDPE QNHMFSDHYI NLPFNLSNVM
FIATANQIDT VPGPLRDRME VIQLSGYTEE EKLEIAKRYL IPRQMKENGI SEKEIVISDE
AVRTIIAKYT REAGLRNLER EIGSVCRKVA RKVAEGDGRR FRITPATVAK YLGPARFIRE
GEMEKNEVGI VTGLAWTPVG GEVLFVEATI MKGKGGLTLT GHLGDVMKES VQAALSYIRS
KAKEFHLAED FLSGYDIHVH VPAGAIPKDG PSAGVTMATA LVSALTRVPV RKDVAMTGEI
TLRGKVLPIG GLKEKMLAAI RAGIKTIVIP EQNEKDLEEI PKHILKKVTV VSAKVIDDVL
AVALETFPPP PPASEGKPAA TVKAPPRRGI AAPRKGAMAG AKS
