LONB_METTH
ID LONB_METTH Reviewed; 644 AA.
AC O26878;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Archaeal Lon protease;
DE EC=3.4.21.-;
DE AltName: Full=ATP-dependent protease La homolog;
GN OrderedLocusNames=MTH_785;
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 -!- 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. Degrades polypeptides processively (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. Archaeal LonB
CC subfamily. {ECO:0000305}.
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DR EMBL; AE000666; AAB85287.1; -; Genomic_DNA.
DR PIR; H69204; H69204.
DR RefSeq; WP_010876422.1; NC_000916.1.
DR AlphaFoldDB; O26878; -.
DR SMR; O26878; -.
DR STRING; 187420.MTH_785; -.
DR MEROPS; S16.005; -.
DR EnsemblBacteria; AAB85287; AAB85287; MTH_785.
DR GeneID; 1471193; -.
DR KEGG; mth:MTH_785; -.
DR PATRIC; fig|187420.15.peg.772; -.
DR HOGENOM; CLU_392630_0_0_2; -.
DR OMA; GLYFWNL; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041699; AAA_32.
DR InterPro; IPR004663; Lon_arc.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10046; PTHR10046; 1.
DR Pfam; PF13654; AAA_32; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF01078; Mg_chelatase; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00764; lon_rel; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Hydrolase; Membrane; Nucleotide-binding;
KW Protease; Reference proteome; Serine protease; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..644
FT /note="Archaeal Lon protease"
FT /id="PRO_0000076153"
FT TOPO_DOM 1..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..644
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 438..617
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 524
FT /evidence="ECO:0000250"
FT ACT_SITE 567
FT /evidence="ECO:0000250"
FT BINDING 71..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 644 AA; 70212 MW; A04A3C18412C3BD0 CRC64;
MKTTIKNSRT QESVSYEGNE TKKGTGETLS YETSKDIEVP ERLIDQIIGQ EEAVETIKKA
AEQRRNVLLI GEPGVGKSML AKAMAELLPR EQLQDILVYP NIEDPNNPLI GAVPAGEGRK
IVMNHKNKAR SQDEKKNLFM MLIISFILVL GFMMNQFLAA IIAAGIIFLA LQQFRPRTTV
MVPKLLVNNE GRQVAPFVDA TGAHAGALLG DVRHDPYQSG GLGTPAHERV EAGMIHKANK
GVLYIDEIGT MKMKTQQELL TAMQEKRYSI TGQSETSSGA MVRSQAVPCD FVLVASGNLQ
VLEGMHPALR SRIRGYGYEV FMKDTMPDTP ENRDKLVQFV AQEVEKDGRI PHFSREAVEE
IIREAQRRAG KKDSLTLKLR ELGGLVRAAG DIAKSRGAEL VETEDVIEAK KLSRTLEQQI
ADRYIVQKKK YSVFKSEGGE VGRVNGLAII GDRSGIILPI AAEAAPAQSK EEGRIIATGK
LGEIAREAVQ NVSALIKKYT GTDISNYDIH IQFLQAYDGV EGDSASVSVA TAVISALEEI
PVDQSVALTG SLSIRGDVLP VGGVTGKIEA AAEAGIRKVL IPASNMGDVM IEKKYEDMVE
IVPVETLGDV LEHALIGKGK ESLIQRMQKI SDIVPSIMKK PAMH
