LONB_METJA
ID LONB_METJA Reviewed; 649 AA.
AC Q58812;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Archaeal Lon protease;
DE EC=3.4.21.-;
DE AltName: Full=ATP-dependent protease La homolog;
GN OrderedLocusNames=MJ1417;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 456-640, AND ACTIVE SITE.
RX PubMed=15456757; DOI=10.1074/jbc.m410437200;
RA Im Y.J., Na Y., Kang G.B., Rho S.H., Kim M.K., Lee J.H., Chung C.H.,
RA Eom S.H.;
RT "The active site of a lon protease from Methanococcus jannaschii distinctly
RT differs from the canonical catalytic Dyad of Lon proteases.";
RL J. Biol. Chem. 279:53451-53457(2004).
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; L77117; AAB99427.1; -; Genomic_DNA.
DR PIR; H64476; H64476.
DR RefSeq; WP_010870934.1; NC_000909.1.
DR PDB; 1XHK; X-ray; 1.90 A; A/B=456-640.
DR PDBsum; 1XHK; -.
DR AlphaFoldDB; Q58812; -.
DR SMR; Q58812; -.
DR STRING; 243232.MJ_1417; -.
DR MEROPS; S16.008; -.
DR EnsemblBacteria; AAB99427; AAB99427; MJ_1417.
DR GeneID; 1452320; -.
DR KEGG; mja:MJ_1417; -.
DR eggNOG; arCOG02160; Archaea.
DR HOGENOM; CLU_392630_0_0_2; -.
DR InParanoid; Q58812; -.
DR OMA; GLYFWNL; -.
DR OrthoDB; 7657at2157; -.
DR PhylomeDB; Q58812; -.
DR EvolutionaryTrace; Q58812; -.
DR Proteomes; UP000000805; 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; -; 2.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Hydrolase; Membrane;
KW Nucleotide-binding; Protease; Reference proteome; Serine protease;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..649
FT /note="Archaeal Lon protease"
FT /id="PRO_0000076150"
FT TOPO_DOM 1..114
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 136..138
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 456..639
FT /note="Lon proteolytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01122"
FT ACT_SITE 550
FT /evidence="ECO:0000269|PubMed:15456757"
FT ACT_SITE 593
FT /evidence="ECO:0000269|PubMed:15456757"
FT BINDING 47..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 461..466
FT /evidence="ECO:0007829|PDB:1XHK"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:1XHK"
FT STRAND 475..485
FT /evidence="ECO:0007829|PDB:1XHK"
FT STRAND 490..496
FT /evidence="ECO:0007829|PDB:1XHK"
FT HELIX 498..517
FT /evidence="ECO:0007829|PDB:1XHK"
FT STRAND 533..541
FT /evidence="ECO:0007829|PDB:1XHK"
FT TURN 545..547
FT /evidence="ECO:0007829|PDB:1XHK"
FT HELIX 548..551
FT /evidence="ECO:0007829|PDB:1XHK"
FT HELIX 552..564
FT /evidence="ECO:0007829|PDB:1XHK"
FT STRAND 570..574
FT /evidence="ECO:0007829|PDB:1XHK"
FT STRAND 583..585
FT /evidence="ECO:0007829|PDB:1XHK"
FT HELIX 590..599
FT /evidence="ECO:0007829|PDB:1XHK"
FT STRAND 603..608
FT /evidence="ECO:0007829|PDB:1XHK"
FT HELIX 609..614
FT /evidence="ECO:0007829|PDB:1XHK"
FT STRAND 620..628
FT /evidence="ECO:0007829|PDB:1XHK"
FT HELIX 629..636
FT /evidence="ECO:0007829|PDB:1XHK"
SQ SEQUENCE 649 AA; 71918 MW; 2419207160114DBB CRC64;
MFSIKFKTTE ELPEPSPRLI DQVIGQEEAV KIVLSAVKNK RNVILLGDPG VGKSMIVKAV
GEILSDFGEF TPYYVIAKPN LKNMERPIVE VIDGEYKEDS KDMPKLDFKA PSSTTLLLIM
IGAILLSEYL LKYLPQNYLL AAVTITALIV LIFGFVIILT SIMGASRASM PNNLNPMDLK
PVLLYECKKR PLVRASAYNV TRLLGDIKHC PLGGRPPLGT PPHKRIILGA IHEAHRGILY
VDEIKTMPLE VQDYILTALQ DKQLPISGRN PNSSGATVET NPIPCDFILI MSGNMDDVYN
LRAPLLDRID YKIVLKNKMD NTLENRDKLL QFIVQEIKNN NLNPMTYDGC CEVVRIAQYL
AGSKDKLTLR LRLLANIIKM ANDVAMGKDV EELLGNFDDK GEYHPETQKD KSNKVYITAE
HVRKVFDTGI YSMEKQVALN YIKNFKRYKH IVPNDEPKVG VIYGLAVLGA GGIGDVTKII
VQILESKNPG THLLNISGDI AKHSITLASA LSKKLVAEKK LPLPKKDIDL NNKEIYIQFS
QSYSKIDGDS ATAAVCLAII SALLDIPLKQ DFAITGSLDL SGNVLAIGGV NEKIEAAKRY
GFKRVIIPEA NMIDVIETEG IEIIPVKTLD EIVPLVFDLD NRGGAERFN
