UniProt: G0A267

Database: UniProt
Entry: G0A267_METMM

LinkDB:  G0A267_METMM 
Original site:  G0A267_METMM

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (19)   
   InterPro (12)   
   Pfam (3)   
   PROSITE (2)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (32)   

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ID   G0A267_METMM            Unreviewed;       804 AA.
AC   G0A267;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
DE            EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
DE   AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973};
GN   Name=lon {ECO:0000256|HAMAP-Rule:MF_01973};
GN   OrderedLocusNames=Metme_4260 {ECO:0000313|EMBL:AEG02610.1};
OS   Methylomonas methanica (strain MC09).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methylomonas.
OX   NCBI_TaxID=857087 {ECO:0000313|EMBL:AEG02610.1, ECO:0000313|Proteomes:UP000008888};
RN   [1] {ECO:0000313|EMBL:AEG02610.1, ECO:0000313|Proteomes:UP000008888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC09 {ECO:0000313|EMBL:AEG02610.1,
RC   ECO:0000313|Proteomes:UP000008888};
RX   PubMed=22123758; DOI=10.1128/JB.06267-11;
RA   Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.G.,
RA   Jetten M.S., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA   Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.F., Goodwin L.,
RA   Han C., Hauser L., Land M.L., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA   Stein L., Murrell J.C.;
RT   "Complete Genome Sequence of the Aerobic Marine Methanotroph Methylomonas
RT   methanica MC09.";
RL   J. Bacteriol. 193:7001-7002(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MC09;
RA   Boden R., Cunliffe M., Scanlan J., Moussard H., Kits K.D., Klotz M.,
RA   Jetten M., Vuilleumier S., Han J., Peters L., Mikhailova N., Teshima H.,
RA   Tapia R., Kyrpides N., Ivanova N., Pagani I., Cheng J.-F., Goodwin L.,
RA   Han C., Hauser L., Land M., Lapidus A., Lucas S., Pitluck S., Woyke T.,
RA   Stein L.Y., Murrell C.;
RT   "Complete genome sequence of the aerobic marine methanotroph Methylomonas
RT   methanica MC09.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000008888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC09 {ECO:0000313|Proteomes:UP000008888};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Stein L., Woyke T.;
RT   "Complete sequence of Methylomonas methanica MC09.";
RL   Submitted (MAY-2011) 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:0000256|HAMAP-Rule:MF_01973}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01973,
CC         ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-ProRule:PRU01122};
CC   -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC       {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174}.
CC   -!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC       Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174, ECO:0000256|PROSITE-
CC       ProRule:PRU01122}.
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DR   EMBL; CP002738; AEG02610.1; -; Genomic_DNA.
DR   RefSeq; WP_013820825.1; NC_015572.1.
DR   AlphaFoldDB; G0A267; -.
DR   STRING; 857087.Metme_4260; -.
DR   MEROPS; S16.001; -.
DR   KEGG; mmt:Metme_4260; -.
DR   eggNOG; COG0466; Bacteria.
DR   HOGENOM; CLU_004109_4_3_6; -.
DR   OrthoDB; 9803599at2; -.
DR   Proteomes; UP000008888; 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   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   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; 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; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10046:SF56; LON PROTEASE; 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.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01973}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PIRNR:PIRNR001174};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01973,
KW   ECO:0000256|PIRNR:PIRNR001174};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01973};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008888};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW   Rule:MF_01973};
KW   Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW   Rule:MF_01973}.
FT   DOMAIN          11..203
FT                   /note="Lon N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51787"
FT   DOMAIN          593..774
FT                   /note="Lon proteolytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51786"
FT   COILED          191..265
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   ACT_SITE        680
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   ACT_SITE        723
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT                   ECO:0000256|PIRSR:PIRSR001174-1"
FT   BINDING         357..364
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT                   ECO:0000256|PIRSR:PIRSR001174-2"
SQ   SEQUENCE   804 AA;  89531 MW;  AD4C311C16F8EBB0 CRC64;
     MTHVKSKDEL IPVLPLRDVV VYPHMVIPLF VGRGMSIDAL DAAIKQDKQV LLIAQKQADV
     DEPEFDDLYK VGTLANILQL LKLPDGTVKV LVEGTQRCSV IQYQEFEGYC AAGVLELEDE
     LSIDEQELDV LQRTAISSFD QYVKLNNKIP PEVLNSLAGI DDPSRLADTM AAHMALKVEE
     KQNMLEMVDV AKRLESLMTL MEGEVDILEM EKKIRGRVKK QMEKNQREYY LNEQMKAIQK
     ELGEMDEASN EVEELEKKIE TAGMSAEAKT KAMAELNKLK MMSPMSAEAT VVRNYIDWMV
     SVPWKKKTKV RHDLKVAEQV LESEHYGLEK VKERILEYLA VQQRVKQLKG PILCLVGPPG
     VGKTSLGQSI ARATNRKYVR MALGGVRDEA EIRGHRRTYI GSMPGKILQN LSKIKTRNPM
     FLLDEIDKMA ADFRGDPASA LLEVLDPEQN HTFSDHYLEV DFDLSDVMFV ATANTMNIPA
     PLMDRMEVIR LAGYTEDEKI NIAMRFLIPK QVKNNGLAEA EIEISEEAVK DIIRYYSREA
     GVRSLEREIS KICRKVVKDL LLQKDKDKIC VGKDNLDKYL GVRRFSYGMA EDSDQVGQVT
     GLAWTEVGGE LLTIETAVMP GKGKQQATGK LGDVMKESID AAVTVVRSRS HVLGIDNEVF
     QKNDIHIHVP EGATPKDGPS AGIGMCTAII SALTKIPVRA DVAMTGEITL RGEVLPIGGL
     KEKLLAAHRG GIRTVVIPSE NEKDLTEIPD NVKSNLTIKC VRWIDEVLEI ALQKMPVPIV
     IESGERADAA NGKNDGKSQA VVAH
//

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