ID   LONH_METTH              Reviewed;         501 AA.
AC   O26978;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Putative lon protease homolog;
DE            EC=3.4.21.-;
DE   AltName: Full=ATP-dependent protease La homolog;
GN   OrderedLocusNames=MTH_892;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000305}.
CC   -!- CAUTION: Lacks the conserved Ser-Lys catalytic dyad essential for
CC       proteolytic activity. Its enzyme activity is therefore unsure.
CC       {ECO:0000305}.
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DR   EMBL; AE000666; AAB85390.1; -; Genomic_DNA.
DR   PIR; C69219; C69219.
DR   RefSeq; WP_010876525.1; NC_000916.1.
DR   AlphaFoldDB; O26978; -.
DR   SMR; O26978; -.
DR   STRING; 187420.MTH_892; -.
DR   EnsemblBacteria; AAB85390; AAB85390; MTH_892.
DR   GeneID; 1471300; -.
DR   KEGG; mth:MTH_892; -.
DR   PATRIC; fig|187420.15.peg.877; -.
DR   HOGENOM; CLU_550564_0_0_2; -.
DR   OMA; HDPYGGH; -.
DR   Proteomes; UP000005223; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR027065; Lon_Prtase.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10046; PTHR10046; 2.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Nucleotide-binding; Protease; Reference proteome;
KW   Serine protease.
FT   CHAIN           1..501
FT                   /note="Putative lon protease homolog"
FT                   /id="PRO_0000076156"
FT   REGION          481..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   501 AA;  56284 MW;  BDAEA390AF039B45 CRC64;
     MYVDMNREYL KDINTTEDVK IPEDPLERVI GHEDVMPMIK IAAKQRRHLL LVGPPGIGKS
     LLAQAISFHL PEPSEEITVV HNPERPERPF VEIKNRKEIE DEILEIERAE GELIDPQSAP
     DAVAERLGFK CIHCGEYSSA YNSICPRCGG DKFSHIKARR KHIGDLLGMF EMSSGSLSVP
     QKRVTTTRII DGVEEVVIYE RVGGEEIKVL DQRALEKRRQ IVEEKPRNVI VPLDRKTFVQ
     ATGASETELL GDVRHDPYGG HPDLGSQPYE RVVPGAIHEA HEGVLFIDEI VHIAGLQRFI
     FSAMQDKTFP IVGRNPQSAG SSVKVDEVPC DFIFVGACNI ADLQYILPPL RSRIQGEGYE
     LLLNTTMPDT DENRAKIAQF VAQEIELDGK IPHARAAAVE LLIEEARRRA RAVDDVDNAL
     TLRLRDLGGV VRMAGDLAVM DGSPYIETRH MEVAIRKAVS VEDQIIRRYK SYEKALEKDL
     SSSQRMSQHG YSSENIDRSY M